The State of Artwork of Regenerative Remedy in Cardiovascular Ischemic Illness: Biology, Signaling Pathways, and Epigenetics of Endothelial Progenitor Cells
Ischemic coronary heart illness is presently a serious reason for mortality and morbidity worldwide. Nonetheless, the precise therapeutic situation doesn’t goal myocardial cell regeneration and consequently, the development towards the late stage of power coronary heart failure is frequent. Endothelial progenitor cells (EPCs) are bone marrow-derived stem cells that contribute to the homeostasis of the endothelial wall in acute and power ischemic illness. Calcium modulation and different molecular pathways (NOTCH, VEGFR, and CXCR4) contribute to EPC proliferation and differentiation. The current evaluate supplies a abstract of EPC biology with a selected concentrate on the regulatory pathways of EPCs and describes promising functions for cardiovascular cell remedy.
Understanding angiodiversity: insights from single cellbiology
Blood vessels have lengthy been thought-about as passive conduits for delivering blood. Nevertheless, lately, cells of the vessel wall (endothelial cells, clean muscle cells and pericytes) have emerged as lively, extremely dynamic parts that orchestrate crosstalk between the circulation and organs.
Encompassing the entire physique and being specialised to the wants of distinct organs, it’s not shocking that vessel lining cells come in several flavours.
There may be calibre-specific specialization (arteries, arterioles, capillaries, venules, veins), but in addition organ-specific heterogeneity in several microvascular beds (steady, discontinuous, sinusoidal).
Latest technical advances within the discipline of single cell biology have enabled the profiling of hundreds of single cells and, therefore, have allowed for the molecular dissection of such angiodiversity, yielding a hitherto unparalleled stage of spatial and useful decision.
Right here, we evaluate how these approaches have contributed to our understanding of angiodiversity.
Description: CXCL4 is a CXC chemokine that is expressed in megakaryocytes and stored in the alpha-granules of platelets. CXCL4 is chemotactic towards neutrophils and monocytes and has been shown to inhibit angiogenesis. Recombinant human CXCL4 is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved residues present in CXC chemokines.
Description: CXCL8 (IL-8) is a proinflammatory CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is secreted by monocytes and endothelial cells. CXCL8 (IL-8) chemoattracts and activates neutrophils. Recombinant human CXCL8 (IL-8) (endothelial-derived) is an 8.9 kDa protein containing 77 amino acid residues.
Description: CXCL8 (IL-8) is a proinflammatory CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is secreted by monocytes and endothelial cells. CXCL8 (IL-8) chemoattracts and activates neutrophils. Recombinant human CXCL8 (IL-8) (endothelial-derived) is an 8.9 kDa protein containing 77 amino acid residues.
Description: BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines and plays an important role in B cell development, function and regulation. BCMA also has the capability to activate NF-kappaB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid extracellular domain. Recombinant soluble BCMA is a 50 amino acid polypeptide (5.3 kDa) comprising the TNFR homologous region of the BCMA protein.
Description: BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines and plays an important role in B cell development, function and regulation. BCMA also has the capability to activate NF-kappaB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid extracellular domain. Recombinant soluble BCMA is a 50 amino acid polypeptide (5.3 kDa) comprising the TNFR homologous region of the BCMA protein.
Description: Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue. Recently, Visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity. Like insulin, Visfatin exerts hypoglycemic effects by interacting with the insulin receptor. The binding affinity of Visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites. The circulating levels of Visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of Visfatin may not be of physiological importance. The plasma Visfatin levels, like those of Leptin, correlate positively with the percent of body fat and increase during the development of obesity. Another similarity between Visfatin and Leptin is that their amino acid sequence is highly conserved across different mammalian species and shows no homology to any known protein. Receptors for both Leptin (Ob-R) and Visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism. Although the metabolic function of Visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of Leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat. Recombinant human Visfatin is a 52.5 kDa protein containing 465 amino acid residues (isoform 1).
Description: Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue. Recently, Visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity. Like insulin, Visfatin exerts hypoglycemic effects by interacting with the insulin receptor. The binding affinity of Visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites. The circulating levels of Visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of Visfatin may not be of physiological importance. The plasma Visfatin levels, like those of Leptin, correlate positively with the percent of body fat and increase during the development of obesity. Another similarity between Visfatin and Leptin is that their amino acid sequence is highly conserved across different mammalian species and shows no homology to any known protein. Receptors for both Leptin (Ob-R) and Visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism. Although the metabolic function of Visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of Leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat. Recombinant human Visfatin is a 52.5 kDa protein containing 465 amino acid residues (isoform 1).
Description: Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRalpha (alpha1-alpha4) receptors. Artemin prefers the receptor GFRalpha3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia such as sympathetic, neural crest and placodally derived sensory neurons, and dompaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer, of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Recombinant human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
Description: Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRalpha (alpha1-alpha4) receptors. Artemin prefers the receptor GFRalpha3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia such as sympathetic, neural crest and placodally derived sensory neurons, and dompaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer, of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Recombinant human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
Description: Sox2, also known as sex determining region Y (SRY)-box 2, belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4, into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in the capacity to form teratomas in immune-deficient mice. Recombinant human Sox2 is a 34.3 kDa protein containing 317 amino-acid residues.
Description: Sox2, also known as sex determining region Y (SRY)-box 2, belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4, into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in the capacity to form teratomas in immune-deficient mice. Recombinant human Sox2 is a 34.3 kDa protein containing 317 amino-acid residues.
Description: Nanog is a regulatory protein that is associated with undifferentiated pluripotent cells. The expression of Nanog, which is suppressed in all adult tissues, is restricted to embryonic stem cells and to certain pluripotent cancer cells. Decreased expression of Nanog is strongly correlated with cell differentiation. Nanog, most likely, acts as an intracellular regulator, which maintains pluripotency and self renewal via a STAT3 independent pathway. Recombinant human Nanog is a 34.5 kDa protein, which is synthesized as a 304 amino acid polypeptide lacking a signal sequence for secretion.
Description: Nanog is a regulatory protein that is associated with undifferentiated pluripotent cells. The expression of Nanog, which is suppressed in all adult tissues, is restricted to embryonic stem cells and to certain pluripotent cancer cells. Decreased expression of Nanog is strongly correlated with cell differentiation. Nanog, most likely, acts as an intracellular regulator, which maintains pluripotency and self renewal via a STAT3 independent pathway. Recombinant human Nanog is a 34.5 kDa protein, which is synthesized as a 304 amino acid polypeptide lacking a signal sequence for secretion.
Description: Osteopontin is a secreted glycoprotein that functions as a ligand to alphavbeta3 integrin and possibly other receptors. It binds tightly to hydroxyapatite and can act as a structural component of the extracellular mineralized matrix. Osteopontin is initially secreted as a 298 amino acid protein, which is subject to multiple post-translational modifications including glycosylation, phosphorylation, and specific proteolytic cleavages into various smaller molecular weight fragments. Osteopontin is expressed in a wide range of cells and tissues including osteoblasts, various tumor cell lines, extraosseous cells in the inner ear, brain, kidney, deciduum, placenta and odontoblasts. In addition to its involvement in mineralized matrix formation, Osteopontin can also function as a cytokine that stimulates the release of IFNγ and IL-12, while inhibiting the production of IL-10. Recombinant human Osteopontin is a 298 amino acid protein, which, due to glycosylation, migrates at an apparent molecular weight of 60.0-65.0 kDa by SDS-PAGE analysis under reducing conditions.
Description: Osteopontin is a secreted glycoprotein that functions as a ligand to alphavbeta3 integrin and possibly other receptors. It binds tightly to hydroxyapatite and can act as a structural component of the extracellular mineralized matrix. Osteopontin is initially secreted as a 298 amino acid protein, which is subject to multiple post-translational modifications including glycosylation, phosphorylation, and specific proteolytic cleavages into various smaller molecular weight fragments. Osteopontin is expressed in a wide range of cells and tissues including osteoblasts, various tumor cell lines, extraosseous cells in the inner ear, brain, kidney, deciduum, placenta and odontoblasts. In addition to its involvement in mineralized matrix formation, Osteopontin can also function as a cytokine that stimulates the release of IFNγ and IL-12, while inhibiting the production of IL-10. Recombinant human Osteopontin is a 298 amino acid protein, which, due to glycosylation, migrates at an apparent molecular weight of 60.0-65.0 kDa by SDS-PAGE analysis under reducing conditions.
Description: Neuroserpin is an inhibitory serpin that is expressed predominantly in central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggest that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory, i.e. cerebral cortex, hippocampus, and amygdala. The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the familial encephalopathy with neuroserpin inclusion bodies (FENIB). Recombinant human neuroserpin is a 44.6 kDa non-glycosylated protein containing 394 amino-acid residues.
Description: Neuroserpin is an inhibitory serpin that is expressed predominantly in central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggest that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory, i.e. cerebral cortex, hippocampus, and amygdala. The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the familial encephalopathy with neuroserpin inclusion bodies (FENIB). Recombinant human neuroserpin is a 44.6 kDa non-glycosylated protein containing 394 amino-acid residues.
Description: ApoE3 belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. E3 is the most common isoform and is present in 40-90% of the population. Recombinant human ApoE3 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE3 belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. E3 is the most common isoform and is present in 40-90% of the population. Recombinant human ApoE3 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease. Recombinant human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease. Recombinant human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. It’s interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. E2 allele carriers had significantly lower levels of total cholesterol, low-density lipoprotein cholesterol, and non-high-density lipoprotein cholesterol, as well as increased ApoE levels. Recombinant human ApoE2 is a 34.3 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. It’s interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. E2 allele carriers had significantly lower levels of total cholesterol, low-density lipoprotein cholesterol, and non-high-density lipoprotein cholesterol, as well as increased ApoE levels. Recombinant human ApoE2 is a 34.3 kDa protein containing 300 amino acid residues.
Description: CD22 is a B-lineage restricted 135 kDa glycoprotein whose cell surface expression is limited to resting and activated B lymphocytes. The physiological role of CD22 is still unknown. Targeted disruption of CD22 in mice results in a reduced level of surface IgM on peripheral B cells suggesting a role for CD22 in limiting antigen receptor signaling. CD22 is a member of the Ig gene superfamily that uniquely binds a sialic acid-dependent ligand. Recombinant human CD22 is a soluble 75.0 kDa protein which corresponds to the extracellular domain of CD22.
Description: CD22 is a B-lineage restricted 135 kDa glycoprotein whose cell surface expression is limited to resting and activated B lymphocytes. The physiological role of CD22 is still unknown. Targeted disruption of CD22 in mice results in a reduced level of surface IgM on peripheral B cells suggesting a role for CD22 in limiting antigen receptor signaling. CD22 is a member of the Ig gene superfamily that uniquely binds a sialic acid-dependent ligand. Recombinant human CD22 is a soluble 75.0 kDa protein which corresponds to the extracellular domain of CD22.
Description: Epiregulin is an EGF related growth factor that binds specifically to EGFR (ErbB1) and ErbB4, but not ErbB2 or ErbB3. It is expressed mainly in the placenta and peripheral blood leukocytes and in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence. Recombinant human Epiregulin is a 5.6 kDa monomeric protein, containing 50 amino residues, which corresponds to the mature secreted Epiregulin sequence.
Description: Epiregulin is an EGF related growth factor that binds specifically to EGFR (ErbB1) and ErbB4, but not ErbB2 or ErbB3. It is expressed mainly in the placenta and peripheral blood leukocytes and in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence. Recombinant human Epiregulin is a 5.6 kDa monomeric protein, containing 50 amino residues, which corresponds to the mature secreted Epiregulin sequence.
Description: Prolactin is a neuroendocrine hormone secreted by the pituitary gland. Its primary function is to promote and maintain lactation during pregnancy and suckling. In addition, Prolactin plays an immune-regulatory role by stimulating the activities of ornithine decarboxylase and protein kinase C, which are important for the proliferation, differentiation, and function of lymphocytes. Recombinant human Prolactin is a 23 kDa globular protein containing 200 amino acid residues.
Description: Prolactin is a neuroendocrine hormone secreted by the pituitary gland. Its primary function is to promote and maintain lactation during pregnancy and suckling. In addition, Prolactin plays an immune-regulatory role by stimulating the activities of ornithine decarboxylase and protein kinase C, which are important for the proliferation, differentiation, and function of lymphocytes. Recombinant human Prolactin is a 23 kDa globular protein containing 200 amino acid residues.
Description: PTHrP is a polypeptide hormone produced by almost every tissue of the body. PTHrP is closely related to parathyroid hormone (PTH), which is secreted from the parathyroid gland, and plays a central role in regulating the extracellular concentrations of calcium and phosphorous. Recombinant human PTHrP is a 9.8 kDa linear polypeptide of 86 amino acid residues.
Description: PTHrP is a polypeptide hormone produced by almost every tissue of the body. PTHrP is closely related to parathyroid hormone (PTH), which is secreted from the parathyroid gland, and plays a central role in regulating the extracellular concentrations of calcium and phosphorous. Recombinant human PTHrP is a 9.8 kDa linear polypeptide of 86 amino acid residues.
Description: Keratinocyte Growth Factor (KGF/FGF-7) is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of variety of tissues, by promoting cellular proliferation and differentiation. KGF/FG-7 is a mitogen factor specific for epithelial cells and keratinocytes and signals through FGFR 2b. KGF/FGF-7 plays a role in kidney and lung development, angiogenesis, and wound healing. Recombinant human KGF/FGF-7 is an 18.9 kDa protein consisting of 163 amino acid residues.
Description: Keratinocyte Growth Factor (KGF/FGF-7) is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of variety of tissues, by promoting cellular proliferation and differentiation. KGF/FG-7 is a mitogen factor specific for epithelial cells and keratinocytes and signals through FGFR 2b. KGF/FGF-7 plays a role in kidney and lung development, angiogenesis, and wound healing. Recombinant human KGF/FGF-7 is an 18.9 kDa protein consisting of 163 amino acid residues.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through the three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant human VEGF165 is a 38.2 kDa disulfide-linked homodimeric protein consisting of two 165 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through the three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant human VEGF165 is a 38.2 kDa disulfide-linked homodimeric protein consisting of two 165 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Due to its increased acidity, VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant human VEGF121 is a 28.4 kDa disulfide-linked homodimeric protein consisting of two 121 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Due to its increased acidity, VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant human VEGF121 is a 28.4 kDa disulfide-linked homodimeric protein consisting of two 121 amino acid polypeptide chains.
Description: HGF is a mesenchymally derived potent mitogen for mature parenchymal hepatocyte cells and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Human HGF is expressed as a linear 697 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of HGF, which consists of two polypeptide chains (α-chain and β-chain) held by a single disulfide bond resulting in formation of a biologically active heterodimer. The α-chain consists of 463 amino acid residues and four kringle domains. The β-chain consists of 234 amino acid residues.
Description: HGF is a mesenchymally derived potent mitogen for mature parenchymal hepatocyte cells and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Human HGF is expressed as a linear 697 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of HGF, which consists of two polypeptide chains (α-chain and β-chain) held by a single disulfide bond resulting in formation of a biologically active heterodimer. The α-chain consists of 463 amino acid residues and four kringle domains. The β-chain consists of 234 amino acid residues.
Description: Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems. Recombinant E. coli derived Human Sonic HedgeHog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted for the natural occurring chemically modified Cys residue.
Description: Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems. Recombinant E. coli derived Human Sonic HedgeHog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted for the natural occurring chemically modified Cys residue.
Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Human Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant human Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino residues, which comprises the mature EGF homologous portion of the Betacellulin protein.
Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Human Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant human Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino residues, which comprises the mature EGF homologous portion of the Betacellulin protein.
Description: Epigen is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. It is produced in several tissues, including the testis, liver, heart and in certain tumor cells. Epigen is mitogenic for fibroblasts and epithelial cells. Human Epigen is initially synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence. Recombinant human Epigen is a 7.9kDa monomeric protein, containing 72 amino acid residues, which comprises the EGF homologous portion of the Epigen precursor.
Description: Epigen is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. It is produced in several tissues, including the testis, liver, heart and in certain tumor cells. Epigen is mitogenic for fibroblasts and epithelial cells. Human Epigen is initially synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence. Recombinant human Epigen is a 7.9kDa monomeric protein, containing 72 amino acid residues, which comprises the EGF homologous portion of the Epigen precursor.
Description: Klotho is a glycosylated protein that plays an important role in the regulation of phosphate and calcium homeostasis. The full length transmembrane form has a large extracellular domain composed of two homologous subunits termed KL1 and KL2, which contain 516 and 439 amino acid residues, respectively, The predominant circulating form, which is derived from alternative RNA splicing, contains the KL1 subunit and constitutes the N-terminal sequence of transmembrane Klotho. A third Klotho protein of about 128 kDa has been identified in the blood and cerebrospinal fluid. This circulating protein arises from the action of an as yet unidentified protease which cleaves transmembrane Klotho just above and/or within the plasma membrane. Klotho has been shown to play a key role in the signaling cascade of fibroblast growth factor-23 (FGF-23), a bone derived hormone that acts in the kidney to inhibit phosphate reabsorption and vitamin D biosynthesis. Klotho promotes FGF-23 signaling through binding to FGFRI (IIIc) which converts this canonical FGF receptor into a specific receptor for FGF-23. In the absence of Klotho the function of FGF-23 is literally abolished. Recombinant human Klotho is a 65-70 kDa glycoprotein containing 516 amino acid residues.
Description: Klotho is a glycosylated protein that plays an important role in the regulation of phosphate and calcium homeostasis. The full length transmembrane form has a large extracellular domain composed of two homologous subunits termed KL1 and KL2, which contain 516 and 439 amino acid residues, respectively, The predominant circulating form, which is derived from alternative RNA splicing, contains the KL1 subunit and constitutes the N-terminal sequence of transmembrane Klotho. A third Klotho protein of about 128 kDa has been identified in the blood and cerebrospinal fluid. This circulating protein arises from the action of an as yet unidentified protease which cleaves transmembrane Klotho just above and/or within the plasma membrane. Klotho has been shown to play a key role in the signaling cascade of fibroblast growth factor-23 (FGF-23), a bone derived hormone that acts in the kidney to inhibit phosphate reabsorption and vitamin D biosynthesis. Klotho promotes FGF-23 signaling through binding to FGFRI (IIIc) which converts this canonical FGF receptor into a specific receptor for FGF-23. In the absence of Klotho the function of FGF-23 is literally abolished. Recombinant human Klotho is a 65-70 kDa glycoprotein containing 516 amino acid residues.
Description: Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the Activin-binding protein Follistatin, and by the propeptide of Myostatin. Recombinant Human myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Description: Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the Activin-binding protein Follistatin, and by the propeptide of Myostatin. Recombinant Human myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Description: Twisted Gastrulation Protein (TSG) is a secreted BMP binding protein structurally related to the BMP antagonists Chordin and Noggin. TSG can inhibit BMP activity by binding directly to BMP proteins, and can act either as a BMP4 agonist or antagonist (depending on the specific biochemical environment) by binding to the BMP4/Chordin complex. Recombinant human TSG is a 199 amino acid 22.2 kDa protein containing the BMP/TGFβ binding portion of the full length TSG protein.
Description: Twisted Gastrulation Protein (TSG) is a secreted BMP binding protein structurally related to the BMP antagonists Chordin and Noggin. TSG can inhibit BMP activity by binding directly to BMP proteins, and can act either as a BMP4 agonist or antagonist (depending on the specific biochemical environment) by binding to the BMP4/Chordin complex. Recombinant human TSG is a 199 amino acid 22.2 kDa protein containing the BMP/TGFβ binding portion of the full length TSG protein.
Description: Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death and recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant human Noggin is a 46 kDa disulfide-linked homodimer (120-10C) consisting of two 206 amino acid polypeptide chains. Monomeric glycosylated Noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death and recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant human Noggin is a 46 kDa disulfide-linked homodimer (120-10C) consisting of two 206 amino acid polypeptide chains. Monomeric glycosylated Noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Follistatin is a secreted protein that binds to ligands of the TGF-β family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as activin antagonists whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-β ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-β1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.
Description: Follistatin is a secreted protein that binds to ligands of the TGF-β family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as activin antagonists whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-β ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-β1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.
Description: CTGFL/WISP-2 is a 24.3 kDa protein that belongs to the CCN family of cysteine rich regulatory proteins. Members of this family stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest, and migration of multiple cell types. The protein is expressed in primary osteoblasts, fibroblasts, ovary, testes, and heart. In addition to promoting adhesion of osteoblasts, CTGFL/WISP-2 inhibits osteocalcin production, as well as binding of fibrinogen to integrin receptors. Recombinant human CTGFL/WISP-2 is a 24.3 kDa protein of 228 amino acid residues.
Description: CTGFL/WISP-2 is a 24.3 kDa protein that belongs to the CCN family of cysteine rich regulatory proteins. Members of this family stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest, and migration of multiple cell types. The protein is expressed in primary osteoblasts, fibroblasts, ovary, testes, and heart. In addition to promoting adhesion of osteoblasts, CTGFL/WISP-2 inhibits osteocalcin production, as well as binding of fibrinogen to integrin receptors. Recombinant human CTGFL/WISP-2 is a 24.3 kDa protein of 228 amino acid residues.
Description: CTGF is a member of the CCN family of secreted cysteine rich regulatory proteins and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial, and epithelial cells, and binds to IGF, TGF beta1, and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Recombinant human CTGF is a 11.2 kDa protein of 98 amino acid residues.
Description: CTGF is a member of the CCN family of secreted cysteine rich regulatory proteins and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial, and epithelial cells, and binds to IGF, TGF beta1, and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Recombinant human CTGF is a 11.2 kDa protein of 98 amino acid residues.
Description: CYR61 is a member of the CCN family of secreted cysteine rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant human CYR61 is a 39.5 kDa protein containing 357 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: CYR61 is a member of the CCN family of secreted cysteine rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant human CYR61 is a 39.5 kDa protein containing 357 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: NOV is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell surface integrins and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant human NOV is a 36.2 kDa protein containing 331 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: NOV is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell surface integrins and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant human NOV is a 36.2 kDa protein containing 331 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: MIA is the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family; MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells that promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis. Recombinant human MIA is a 12.2 kDa globular protein containing 108 amino acid residues including two intramolecular disulfide bonds.
Description: MIA is the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family; MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells that promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis. Recombinant human MIA is a 12.2 kDa globular protein containing 108 amino acid residues including two intramolecular disulfide bonds.
Description: OTOR, also called Otoraplin and MIAL, is a secreted cytokine and a member of the MIA/OTOR family. Members of this family which also includes MIA, MIA2, and TANGO share a Src homology-3 (SH3)-like domain. OTOR is predominantly expressed in the cochlea of the inner-ear and to a lesser extent in fetal brain and in some cartilage tissues. OTOR appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. Recombinant human OTOR is a 12.7 kDa globular protein containing 112 amino acid residues.
Description: OTOR, also called Otoraplin and MIAL, is a secreted cytokine and a member of the MIA/OTOR family. Members of this family which also includes MIA, MIA2, and TANGO share a Src homology-3 (SH3)-like domain. OTOR is predominantly expressed in the cochlea of the inner-ear and to a lesser extent in fetal brain and in some cartilage tissues. OTOR appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. Recombinant human OTOR is a 12.7 kDa globular protein containing 112 amino acid residues.
Description: Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of Vaspin predicts the presence of three β-sheets, nine α-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal”) serine-protease inhibitors, characterized by having more than 30% sequence homology with α1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In human, the serpins represent approximately 2% of total serum proteins, of which 70% is α1- antitrypsin. Vaspin exhibits 40.2% sequence identity with α-1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of Vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines including leptin, adiponectin, resistin, and TNF-α. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant human Vaspin is a 45.2 kDa protein containing 395 amino-acid residues.
Description: Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of Vaspin predicts the presence of three β-sheets, nine α-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal”) serine-protease inhibitors, characterized by having more than 30% sequence homology with α1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In human, the serpins represent approximately 2% of total serum proteins, of which 70% is α1- antitrypsin. Vaspin exhibits 40.2% sequence identity with α-1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of Vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines including leptin, adiponectin, resistin, and TNF-α. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant human Vaspin is a 45.2 kDa protein containing 395 amino-acid residues.
Description: Maspin (mammary serine protease inhibitor) is a non-inhibitory serpin that is expressed predominantly in normal mammary epithelial cells but at significantly reduced levels or absent in most breast carcinomas. It has the ability to block the growth, invasiveness, and metastatic potential of breast and lung tumors. This anti-tumor activity is achieved, in part, by the ability of Maspin to inhibit angiogenesis and to preferentially promote apoptosis of tumor cells. Recombinant human Maspin is a 42.2 kDa non-glycosylated protein containing 375 amino acid residues.
Description: Maspin (mammary serine protease inhibitor) is a non-inhibitory serpin that is expressed predominantly in normal mammary epithelial cells but at significantly reduced levels or absent in most breast carcinomas. It has the ability to block the growth, invasiveness, and metastatic potential of breast and lung tumors. This anti-tumor activity is achieved, in part, by the ability of Maspin to inhibit angiogenesis and to preferentially promote apoptosis of tumor cells. Recombinant human Maspin is a 42.2 kDa non-glycosylated protein containing 375 amino acid residues.
Description: PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity (1) should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers. Recombinant PEDF is a 44.5 kDa non-glycosylated protein containing 400 amino acid residues. (1) Notari, I. et al. J Biol Chem., Vol. 281, 38022-38037.
Description: PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity (1) should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers. Recombinant PEDF is a 44.5 kDa non-glycosylated protein containing 400 amino acid residues. (1) Notari, I. et al. J Biol Chem., Vol. 281, 38022-38037.
Description: Endostatin is a naturally occurring 20 kDa polypeptide derived from the C-terminal portion of type XVIII collagen. It functions as an anti-angiogenic cytokine that is expressed in various organs with the highest levels in liver, lung and kidney. Endostatin inhibits angiogenesis by blocking the pro-angiogenic activities of VEGF and FGF-basic. Recombinant human Endostatin is a 20.2 kDa protein consisting 184 amino acid residues.
Description: Endostatin is a naturally occurring 20 kDa polypeptide derived from the C-terminal portion of type XVIII collagen. It functions as an anti-angiogenic cytokine that is expressed in various organs with the highest levels in liver, lung and kidney. Endostatin inhibits angiogenesis by blocking the pro-angiogenic activities of VEGF and FGF-basic. Recombinant human Endostatin is a 20.2 kDa protein consisting 184 amino acid residues.
Description: Stem Cell Factor (SCF) is a hematopoietic growth factor that exerts its activity by signaling through the c-Kit receptor. SCF and c-Kit are essential for the survival, proliferation and differentiation of hematopoietic cells committed to the melanocyte and germ cell lineages. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. Recombinant human SCF is an 18.4 kDa polypeptide containing 165 amino acid residues, which corresponds to the sequence of the secreted soluble form of SCF.
Description: Stem Cell Factor (SCF) is a hematopoietic growth factor that exerts its activity by signaling through the c-Kit receptor. SCF and c-Kit are essential for the survival, proliferation and differentiation of hematopoietic cells committed to the melanocyte and germ cell lineages. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. Recombinant human SCF is an 18.4 kDa polypeptide containing 165 amino acid residues, which corresponds to the sequence of the secreted soluble form of SCF.
Description: TPO is a lineage specific growth factor, produced in the liver, kidney and skeletal muscle. It stimulates the proliferation and maturation of megakaryocytes, and promotes increased circulating levels of platelets in vivo. TPO signals through the c-mpl receptor and acts as an important regulator of circulating platelets. Human and murine TPO exhibits cross-species reactivity. Recombinant human TPO is a fully biologically active 174 amino acid polypeptide (18.6 kDa), which contains the erythropoietin-like domain of the full length TPO protein.
Description: TPO is a lineage specific growth factor, produced in the liver, kidney and skeletal muscle. It stimulates the proliferation and maturation of megakaryocytes, and promotes increased circulating levels of platelets in vivo. TPO signals through the c-mpl receptor and acts as an important regulator of circulating platelets. Human and murine TPO exhibits cross-species reactivity. Recombinant human TPO is a fully biologically active 174 amino acid polypeptide (18.6 kDa), which contains the erythropoietin-like domain of the full length TPO protein.
Description: Encoded by the ob (obese) gene, Leptin is an adipose-derived cytokine that suppresses appetite and increases thermogenesis. Leptin exerts its anorectic effect via signaling through a hypothalamic receptor termed OB-R. Leptin has been shown to reduce body weight, food consumption, and plasma glucose levels in various in vivo models. Recombinant human Leptin is a 16.0 kDa protein containing 147 amino acid residues.
Description: Encoded by the ob (obese) gene, Leptin is an adipose-derived cytokine that suppresses appetite and increases thermogenesis. Leptin exerts its anorectic effect via signaling through a hypothalamic receptor termed OB-R. Leptin has been shown to reduce body weight, food consumption, and plasma glucose levels in various in vivo models. Recombinant human Leptin is a 16.0 kDa protein containing 147 amino acid residues.
Description: TSLP is a hemopoietic protein that is expressed in the heart, liver and prostate. TSLP overlaps biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the IL-7R alpha chain (IL-7Rα) and the TSLP-specific chain (TSLPR). Like IL-7, TSLP induces phosphorylation of STAT3 and STAT5, but uses kinases other than the JAKs for activation. TSLP prohibited apoptosis and stimulated growth of the human acute myeloid leukemia (AML)-derived cell line MUTZ3. It induces the release of T cell-attracting chemokines TARC and MDC from monocytes and activates CD11c(+) dendritic cells (DCs). TSLP activated DCs primed naïve T cells to produce the proallergic cytokines (IL-4, IL-5, IL-13, TNFα) while down-regulating IL-10 and IFN-γ suggesting a role in initiating allergic inflammation. Recombinant human TSLP is a 15.0 kDa protein consisting of 132 amino acid residues.
Description: TSLP is a hemopoietic protein that is expressed in the heart, liver and prostate. TSLP overlaps biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the IL-7R alpha chain (IL-7Rα) and the TSLP-specific chain (TSLPR). Like IL-7, TSLP induces phosphorylation of STAT3 and STAT5, but uses kinases other than the JAKs for activation. TSLP prohibited apoptosis and stimulated growth of the human acute myeloid leukemia (AML)-derived cell line MUTZ3. It induces the release of T cell-attracting chemokines TARC and MDC from monocytes and activates CD11c(+) dendritic cells (DCs). TSLP activated DCs primed naïve T cells to produce the proallergic cytokines (IL-4, IL-5, IL-13, TNFα) while down-regulating IL-10 and IFN-γ suggesting a role in initiating allergic inflammation. Recombinant human TSLP is a 15.0 kDa protein consisting of 132 amino acid residues.
Description: TRAIL/Apo2L is a cytotoxic protein, which activates rapid apoptosis in tumor cells, but not in normal cells. TRAIL induced apoptosis is achieved through binding to two death-signaling receptors, DR4 and DR5. These receptors belong to the TNFR superfamily of transmembrane proteins and contain a cytoplasmic "death domain", which activates the cell's apoptotic machinery. Recombinant human soluble TRAIL/Apo2L is a 168 amino acid polypeptide (19.6 kDa), consisting of the TNF homologous portion of the extracellular domain of the full length TRAIL/Apo2L protein.
Description: TRAIL/Apo2L is a cytotoxic protein, which activates rapid apoptosis in tumor cells, but not in normal cells. TRAIL induced apoptosis is achieved through binding to two death-signaling receptors, DR4 and DR5. These receptors belong to the TNFR superfamily of transmembrane proteins and contain a cytoplasmic "death domain", which activates the cell's apoptotic machinery. Recombinant human soluble TRAIL/Apo2L is a 168 amino acid polypeptide (19.6 kDa), consisting of the TNF homologous portion of the extracellular domain of the full length TRAIL/Apo2L protein.
Description: TWEAK belongs to the TNF family of ligands and signals through TWEAKR also known as TNFRSF12A. TWEAK is expressed in a variety of tissues, including the adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK has the ability to induce NFkB activation and chemokine secretion, and to exert an apoptotic activity in certain cells, such as HT-29 human adenocarcinoma cells when cultured in the presence of IFN-γ. TWEAK also promotes proliferation and migration of endothelial cells. Recombinant human TWEAK is a soluble 17.0 kDa polypeptide (154 amino acid residues) comprising the TNF homologous region of TWEAK and is generated by proteolytic processing of the full length membrane anchored TWEAK protein.
Description: TWEAK belongs to the TNF family of ligands and signals through TWEAKR also known as TNFRSF12A. TWEAK is expressed in a variety of tissues, including the adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK has the ability to induce NFkB activation and chemokine secretion, and to exert an apoptotic activity in certain cells, such as HT-29 human adenocarcinoma cells when cultured in the presence of IFN-γ. TWEAK also promotes proliferation and migration of endothelial cells. Recombinant human TWEAK is a soluble 17.0 kDa polypeptide (154 amino acid residues) comprising the TNF homologous region of TWEAK and is generated by proteolytic processing of the full length membrane anchored TWEAK protein.
Description: LIGHT belongs to the TNF family of ligands, and can signal through the herpes virus entry mediator type A receptor (HVEM, TNFRSF14), LTβR, or bind to a decoy receptor, DcR3. It is expressed in splenocytes, activated PBL, CD+8 tumor infiltrating lymphocytes, granulocytes, and monocytes. LIGHT has the ability to active NFκB, to co-stimulate the activation of lymphocytes and to induce apoptosis in certain human tumor cells. Recombinant human LIGHT has a calculated mass of 19.3 kDa containing 177 amino acid residues. Due to glycosylation LIGHT migrates between 20.0-22.5 kDa by SDS-PAGE under non-reducing conditions.
Description: LIGHT belongs to the TNF family of ligands, and can signal through the herpes virus entry mediator type A receptor (HVEM, TNFRSF14), LTβR, or bind to a decoy receptor, DcR3. It is expressed in splenocytes, activated PBL, CD+8 tumor infiltrating lymphocytes, granulocytes, and monocytes. LIGHT has the ability to active NFκB, to co-stimulate the activation of lymphocytes and to induce apoptosis in certain human tumor cells. Recombinant human LIGHT has a calculated mass of 19.3 kDa containing 177 amino acid residues. Due to glycosylation LIGHT migrates between 20.0-22.5 kDa by SDS-PAGE under non-reducing conditions.
Description: APRIL, a member of the TNF superfamily, is expressed in monocytes, macrophages, certain transformed cell lines, certain cancers of colon, and lymphoid tissues. APRIL, along with another TNF family member, BAFF, compete for two receptors, TACI and BCMA. ARPIL has the ability to stimulate proliferation of various tumor cell lines including Jurkat T cells and MCF-7 carcinoma cells. Like BAFF, APRIL also stimulates the proliferation of B and T cells. The human APRIL gene codes for at least four alternatively spliced transcriptional variants, which give rise to different isoforms of the APRIL precursor protein. All isoforms can be cleaved by the protease, furin, to release a soluble C-terminal fragment, which comprises the TNF like receptor binding of the APRIL precursor. Recombinant human APRIL is a soluble 16.3 kDa protein, consisting of 146 amino acid residues.
Description: APRIL, a member of the TNF superfamily, is expressed in monocytes, macrophages, certain transformed cell lines, certain cancers of colon, and lymphoid tissues. APRIL, along with another TNF family member, BAFF, compete for two receptors, TACI and BCMA. ARPIL has the ability to stimulate proliferation of various tumor cell lines including Jurkat T cells and MCF-7 carcinoma cells. Like BAFF, APRIL also stimulates the proliferation of B and T cells. The human APRIL gene codes for at least four alternatively spliced transcriptional variants, which give rise to different isoforms of the APRIL precursor protein. All isoforms can be cleaved by the protease, furin, to release a soluble C-terminal fragment, which comprises the TNF like receptor binding of the APRIL precursor. Recombinant human APRIL is a soluble 16.3 kDa protein, consisting of 146 amino acid residues.
Description: BAFF, a member of the TNF family of ligands, is expressed in T cells, macrophages, monocytes and dendritic cells. BAFF is involved in stimulation of B and T cell function, and is an important survival and maturation factor for peripheral B cells. BAFF signals through three different TNF receptors TACI, BCMA and BAFF-R. The human BAFF gene codes for a 285 amino acid type II transmembrane protein containing a 46 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 218 amino acid extracellular domain. Recombinant human soluble BAFF is a 153 amino acid polypeptide (17.0 kDa), which contains the TNF-like portion of the extracellular domain of BAFF.
Description: BAFF, a member of the TNF family of ligands, is expressed in T cells, macrophages, monocytes and dendritic cells. BAFF is involved in stimulation of B and T cell function, and is an important survival and maturation factor for peripheral B cells. BAFF signals through three different TNF receptors TACI, BCMA and BAFF-R. The human BAFF gene codes for a 285 amino acid type II transmembrane protein containing a 46 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 218 amino acid extracellular domain. Recombinant human soluble BAFF is a 153 amino acid polypeptide (17.0 kDa), which contains the TNF-like portion of the extracellular domain of BAFF.
Description: TACI, a member of the TNF Receptor superfamily, is expressed in the small intestine, spleen, thymus, peripheral blood leukocytes, activated T cells, and resting B cells. TACI binds to both APRIL and BAFF and can stimulate the activation of transcription factors; NF-kappaB, AP-1, and mediates calcineurin dependent activation of NF-AT (nuclear-factor of activated T cells). TACI also plays a key role in the stimulation of B and T cell function. Soluble TACI inhibits APRIL-stimulated proliferation of primary B-cells by blocking the binding of APRIL to the membrane anchored TACI receptor. Recombinant human TACI is a soluble 160 amino acid polypeptide (17.8 kDa) comprising the TNFR homologous cysteine rich extracellular domain of the TACI protein.
Description: TACI, a member of the TNF Receptor superfamily, is expressed in the small intestine, spleen, thymus, peripheral blood leukocytes, activated T cells, and resting B cells. TACI binds to both APRIL and BAFF and can stimulate the activation of transcription factors; NF-kappaB, AP-1, and mediates calcineurin dependent activation of NF-AT (nuclear-factor of activated T cells). TACI also plays a key role in the stimulation of B and T cell function. Soluble TACI inhibits APRIL-stimulated proliferation of primary B-cells by blocking the binding of APRIL to the membrane anchored TACI receptor. Recombinant human TACI is a soluble 160 amino acid polypeptide (17.8 kDa) comprising the TNFR homologous cysteine rich extracellular domain of the TACI protein.
Description: AITRL, a member of the TNF superfamily, is expressed in endothelial cells, and signals through the AITR receptor. AITRL regulates T-cell proliferation and survival, and effectuates the interaction between T lymphocytes and endothelial cells. The AITRL gene codes for a type II transmembrane protein comprised of 177 amino acids, including a 28 amino acid cytoplasmic region, a 21 amino acid transmembrane domain and a 128 amino acid extracellular domain. Recombinant human soluble AITRL is a 14.3 kDa protein, containing 126 amino acid residues corresponding to the extracellular domain of AITRL.
Description: AITRL, a member of the TNF superfamily, is expressed in endothelial cells, and signals through the AITR receptor. AITRL regulates T-cell proliferation and survival, and effectuates the interaction between T lymphocytes and endothelial cells. The AITRL gene codes for a type II transmembrane protein comprised of 177 amino acids, including a 28 amino acid cytoplasmic region, a 21 amino acid transmembrane domain and a 128 amino acid extracellular domain. Recombinant human soluble AITRL is a 14.3 kDa protein, containing 126 amino acid residues corresponding to the extracellular domain of AITRL.
Description: Osteoprotegerin (OPG) is a member of the TNFR superfamily that can act as a decoy receptor for RANKL. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. OPG is expressed in a wide variety of tissues including adult heart, lung, kidney, liver, spleen, prostate, lymph node and bone marrow. OPG is secreted both as a monomeric and a dimeric protein. Its primary structure consists of seven distinct domains, four of which corresponds to the extracellular cysteine-rich domains of TNFR proteins and constitutes the soluble OPG. Recombinant human OPG is a soluble 20.0 kDa protein containing 174 amino acid residues.
Description: Osteoprotegerin (OPG) is a member of the TNFR superfamily that can act as a decoy receptor for RANKL. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. OPG is expressed in a wide variety of tissues including adult heart, lung, kidney, liver, spleen, prostate, lymph node and bone marrow. OPG is secreted both as a monomeric and a dimeric protein. Its primary structure consists of seven distinct domains, four of which corresponds to the extracellular cysteine-rich domains of TNFR proteins and constitutes the soluble OPG. Recombinant human OPG is a soluble 20.0 kDa protein containing 174 amino acid residues.
Description: Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The three known members of this family; Resistin, RELM-α and RELM-β share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that Resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that Resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that Resistin expression is severely suppressed in obesity and that it may act as a feedback regulator of Adipogenesis. Recombinant human Resistin is a 19.5 kDa disulfide-linked homodimeric protein composed of two identical 92 amino acid chains linked by a single disulfide bond.
Description: Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The three known members of this family; Resistin, RELM-α and RELM-β share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that Resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that Resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that Resistin expression is severely suppressed in obesity and that it may act as a feedback regulator of Adipogenesis. Recombinant human Resistin is a 19.5 kDa disulfide-linked homodimeric protein composed of two identical 92 amino acid chains linked by a single disulfide bond.
Description: The gAcrp30 variant is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, Acrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. This naturally occurring variant of human gAcrp30/Adipolean is an 18.1 kDa protein, containing 14 amino acids extra at the N-terminus of human gAcrp30/Adipolean.
Description: The gAcrp30 variant is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, Acrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. This naturally occurring variant of human gAcrp30/Adipolean is an 18.1 kDa protein, containing 14 amino acids extra at the N-terminus of human gAcrp30/Adipolean.
Description: gAcrp30 is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, gAcrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. Recombinant human gAcrp30/Adipolean is a 16.6 kDa protein consisting of 145 amino acid residues.
Description: gAcrp30 is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, gAcrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. Recombinant human gAcrp30/Adipolean is a 16.6 kDa protein consisting of 145 amino acid residues.
Description: Adiponectin is an adipose-derived secreted protein containing 226 amino acid residues. It is relatively abundant in humans and rodents, accounting for about 0.01% of total plasma protein. The circulating levels of adiponectin are decreased under conditions of obesity, insulin resistance, and type II diabetes. Disruption of adiponectin in mice causes insulin resistance and neointimal formation. Conversely, administration of recombinant adiponectin suppresses hepatic glucose production, and reverses insulin resistance associated with both lipoatrophy and obesity. The protective role of adiponectin is attributed to its anti-inflammatory properties (e.g. ability to suppress expression of TNF-α and class A scavenger receptor in macrophages). Recombinant adiponectin is a multimeric glycoprotein containing amino acids Glu-19 to Asn-244 of the adiponectin precursor protein fused to an N-terminal histidine tag. Monomeric glycosylated adiponectin migrates at an apparent molecular weight of approximately 25.9 kDa by SDS PAGE analysis under reducing conditions.
Description: Adiponectin is an adipose-derived secreted protein containing 226 amino acid residues. It is relatively abundant in humans and rodents, accounting for about 0.01% of total plasma protein. The circulating levels of adiponectin are decreased under conditions of obesity, insulin resistance, and type II diabetes. Disruption of adiponectin in mice causes insulin resistance and neointimal formation. Conversely, administration of recombinant adiponectin suppresses hepatic glucose production, and reverses insulin resistance associated with both lipoatrophy and obesity. The protective role of adiponectin is attributed to its anti-inflammatory properties (e.g. ability to suppress expression of TNF-α and class A scavenger receptor in macrophages). Recombinant adiponectin is a multimeric glycoprotein containing amino acids Glu-19 to Asn-244 of the adiponectin precursor protein fused to an N-terminal histidine tag. Monomeric glycosylated adiponectin migrates at an apparent molecular weight of approximately 25.9 kDa by SDS PAGE analysis under reducing conditions.
Description: Murine C10 belongs to the CC chemokine family and is expressed in myelopoietic bone marrow cultures when stimulated with GM-CSF, M-CSF, IL-3 or IL-4. It signals primarily through the CCR1 receptor. C10 is chemotactic for B cells, CD4+ T cells, monocytes and NK cells and also exhibits powerful suppressive activity on colony formation by different lineages of hematopoietic progenitors. The C10 contains the four highly conserved cysteine residues present in CC chemokines. The mature protein contains 95 amino acid residues. Recombinant murine C-10 is a 10.7 kDa protein containing 95 amino acid residues.
Description: Murine C10 belongs to the CC chemokine family and is expressed in myelopoietic bone marrow cultures when stimulated with GM-CSF, M-CSF, IL-3 or IL-4. It signals primarily through the CCR1 receptor. C10 is chemotactic for B cells, CD4+ T cells, monocytes and NK cells and also exhibits powerful suppressive activity on colony formation by different lineages of hematopoietic progenitors. The C10 contains the four highly conserved cysteine residues present in CC chemokines. The mature protein contains 95 amino acid residues. Recombinant murine C-10 is a 10.7 kDa protein containing 95 amino acid residues.
Description: RANTES is a CC-chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. It is a chemoattractant towards monocytes, memory T cells (CD4+/CD45RO), basophils, and eosinophils. RANTES also has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV). Recombinant murine RANTES is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: RANTES is a CC-chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. It is a chemoattractant towards monocytes, memory T cells (CD4+/CD45RO), basophils, and eosinophils. RANTES also has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV). Recombinant murine RANTES is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant murine KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant murine KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: CXCL6, also known as GCP-2 in humans and LIX in mice, is a connective tissue-derived CXC chemokine that contains the four conserved cysteine residues shared by CXC chemokines and the ‘ELR’ motif responsible for CXCR1 and CXCR2 receptor signaling. Constitutively expressed in monocytes, platelets, endothelial cells and mast cells, CXCL6 selectively chemoattracts neutrophils and has been shown to exert anti-angiogenic activity. Human GCP-2 and murine LIX respectively exhibit murine and human cell cross-reactivity. There are two naturally occurring variants of murine LIX, the 78 amino-acid-length LIX 1-78 (GCP-2) and the 70 amino-acid-length LIX 9-78 (GCP-2).
Description: CXCL6, also known as GCP-2 in humans and LIX in mice, is a connective tissue-derived CXC chemokine that contains the four conserved cysteine residues shared by CXC chemokines and the ‘ELR’ motif responsible for CXCR1 and CXCR2 receptor signaling. Constitutively expressed in monocytes, platelets, endothelial cells and mast cells, CXCL6 selectively chemoattracts neutrophils and has been shown to exert anti-angiogenic activity. Human GCP-2 and murine LIX respectively exhibit murine and human cell cross-reactivity. There are two naturally occurring variants of murine LIX, the 78 amino-acid-length LIX 1-78 (GCP-2) and the 70 amino-acid-length LIX 9-78 (GCP-2).
Description: MIG, a CXC chemokine, is produced by IFN?× stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant murine MIG is a 12.2 kDa protein containing 105 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.
Description: MIG, a CXC chemokine, is produced by IFN?× stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant murine MIG is a 12.2 kDa protein containing 105 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant murine MDC is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant murine MDC is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: BCA-1/BLC, a CXC chemokine, is expressed in the liver, spleen, lymph nodes, appendix and stomach. It exerts its activities through its only receptor CXCR5. BCA-1/BLC is a potent chemoattractant for B lymphocytes and induces weak chemotactic response in T cells and macrophages. It manifests no activity on neutrophils and monocytes. Recombinant murine BLC is a 9.8 kDa protein containing 88 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines.
Description: BCA-1/BLC, a CXC chemokine, is expressed in the liver, spleen, lymph nodes, appendix and stomach. It exerts its activities through its only receptor CXCR5. BCA-1/BLC is a potent chemoattractant for B lymphocytes and induces weak chemotactic response in T cells and macrophages. It manifests no activity on neutrophils and monocytes. Recombinant murine BLC is a 9.8 kDa protein containing 88 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines.
Description: CTACK is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T-cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant murine CTACK is a 10.9 kDa protein containing 95 amino acid residues.
Description: CTACK is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T-cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant murine CTACK is a 10.9 kDa protein containing 95 amino acid residues.
Description: CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal ?mucin-like stalk? sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant murine CXCL16 is a 9.9 kDa protein containing 88 amino acid residues.
Description: CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal ?mucin-like stalk? sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant murine CXCL16 is a 9.9 kDa protein containing 88 amino acid residues.
Description: MEC is a secreted CC chemokine expressed primarily by epithelial cells of the bronchioles, salivary gland, mammary gland and colon. MEC signals through the CCR10 receptor and chemoattracts resting CD4, CD8 T-cells and eosinophils. MEC contains six cysteines including the four highly conserved cysteine residues present in CC chemokines. Recombinant murine MEC is a 12.6 kDa protein containing 111 amino acid residues.
Description: MEC is a secreted CC chemokine expressed primarily by epithelial cells of the bronchioles, salivary gland, mammary gland and colon. MEC signals through the CCR10 receptor and chemoattracts resting CD4, CD8 T-cells and eosinophils. MEC contains six cysteines including the four highly conserved cysteine residues present in CC chemokines. Recombinant murine MEC is a 12.6 kDa protein containing 111 amino acid residues.
Description: CXCL6, also known as GCP-2 in humans and LIX in mice, is a connective tissue-derived CXC chemokine that contains the four conserved cysteine residues shared by CXC chemokines and the ‘ELR’ motif responsible for CXCR1 and CXCR2 receptor signaling. Constitutively expressed in monocytes, platelets, endothelial cells and mast cells, CXCL6 selectively chemoattracts neutrophils and has been shown to exert anti-angiogenic activity. Human GCP-2 and murine LIX respectively exhibit murine and human cell cross-reactivity. There are two naturally occurring variants of murine LIX, the 78 amino-acid-length LIX 1-78 (GCP-2) and the 70 amino-acid-length LIX 9-78 (GCP-2).
Description: CXCL6, also known as GCP-2 in humans and LIX in mice, is a connective tissue-derived CXC chemokine that contains the four conserved cysteine residues shared by CXC chemokines and the ‘ELR’ motif responsible for CXCR1 and CXCR2 receptor signaling. Constitutively expressed in monocytes, platelets, endothelial cells and mast cells, CXCL6 selectively chemoattracts neutrophils and has been shown to exert anti-angiogenic activity. Human GCP-2 and murine LIX respectively exhibit murine and human cell cross-reactivity. There are two naturally occurring variants of murine LIX, the 78 amino-acid-length LIX 1-78 (GCP-2) and the 70 amino-acid-length LIX 9-78 (GCP-2).
Description: Lungkine is a CXC chemokine that is expressed in lung epithelial cells and, to a lesser extent, in certain fetal tissues. No human homolog has been identified and a specific cell surface receptor has not yet been found. Lungkine expression in lung tissue is elevated in response to inflammation, at which time it acts to specifically recruit neutrophils and direct them into the lung airway. Recombinant murine Lungkine is a 16.3 kDa CXC chemokine consisting of 142 amino acid residues, including four conserved cysteine residues present in CXC chemokines.
Description: Lungkine is a CXC chemokine that is expressed in lung epithelial cells and, to a lesser extent, in certain fetal tissues. No human homolog has been identified and a specific cell surface receptor has not yet been found. Lungkine expression in lung tissue is elevated in response to inflammation, at which time it acts to specifically recruit neutrophils and direct them into the lung airway. Recombinant murine Lungkine is a 16.3 kDa CXC chemokine consisting of 142 amino acid residues, including four conserved cysteine residues present in CXC chemokines.
Description: RANTES is a CC-chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. It is a chemoattractant towards monocytes, memory T cells (CD4+/CD45RO), basophils, and eosinophils. RANTES also has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV). Recombinant human RANTES is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: RANTES is a CC-chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. It is a chemoattractant towards monocytes, memory T cells (CD4+/CD45RO), basophils, and eosinophils. RANTES also has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV). Recombinant human RANTES is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. GRO/MGSA also stimulates mitogenesis in certain human melanoma cells. Recombinant human GRO/MGSA is a 7.8 kDa protein consisting of 73 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. GRO/MGSA also stimulates mitogenesis in certain human melanoma cells. Recombinant human GRO/MGSA is a 7.8 kDa protein consisting of 73 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: Lymphotactin is the only known member of the C-chemokine family and signals through the receptor XCR1, formally known as GPR5. The spleen shows the highest level of lymphotactin compared to peripheral leukocytes, lung, colon and small intestine. Lymphotactin is chemotactic towards lymphocytes but not towards monocytes or neutrophils. Recombinant human Lymphotactin is a 10.0 kDa protein consisting of 92 amino acid residues.
Description: Lymphotactin is the only known member of the C-chemokine family and signals through the receptor XCR1, formally known as GPR5. The spleen shows the highest level of lymphotactin compared to peripheral leukocytes, lung, colon and small intestine. Lymphotactin is chemotactic towards lymphocytes but not towards monocytes or neutrophils. Recombinant human Lymphotactin is a 10.0 kDa protein consisting of 92 amino acid residues.
Description: MIG, a CXC chemokine, is produced by IFN stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant human MIG is an 11.7 kDa protein containing 103 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.
Description: MIG, a CXC chemokine, is produced by IFN stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant human MIG is an 11.7 kDa protein containing 103 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.
Description: TARC, a CC chemokine, is predominantly produced by dendritic cells in the thymus and signals through the CCR4 receptor. TARC is chemotactic towards T cells. Recombinant human TARC is an 8.0 kDa protein containing 71 amino acid residues, including the four conserved cysteine residues present in CC chemokines.
Description: TARC, a CC chemokine, is predominantly produced by dendritic cells in the thymus and signals through the CCR4 receptor. TARC is chemotactic towards T cells. Recombinant human TARC is an 8.0 kDa protein containing 71 amino acid residues, including the four conserved cysteine residues present in CC chemokines.
Description: Human Fractalkine is a member of the newly discovered CX3C family of chemokines which contains both chemokine and mucin domain. Human Fractalkine is an 8.5 kDa protein containing 76 amino acid residues and comprises only the chemokine domain of Fractalkine.
Description: Human Fractalkine is a member of the newly discovered CX3C family of chemokines which contains both chemokine and mucin domain. Human Fractalkine is an 8.5 kDa protein containing 76 amino acid residues and comprises only the chemokine domain of Fractalkine.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant human MDC is an 8.0 kDa protein containing 67 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant human MDC is an 8.0 kDa protein containing 67 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant human MDC is an 8.1 kDa protein containing 69 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant human MDC is an 8.1 kDa protein containing 69 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: LEC is a CC chemokine that can signal through the CCR8 and CCR1 receptors. It is expressed in the liver, spleen, and thymus. LEC is chemotactic towards monocytes and lymphocytes but not neutrophils. Recombinant human LEC is an 11.2 kDa protein containing 97 amino acid residues, including the four conserved cysteine residues present in CC chemokines.
Description: LEC is a CC chemokine that can signal through the CCR8 and CCR1 receptors. It is expressed in the liver, spleen, and thymus. LEC is chemotactic towards monocytes and lymphocytes but not neutrophils. Recombinant human LEC is an 11.2 kDa protein containing 97 amino acid residues, including the four conserved cysteine residues present in CC chemokines.
Description: TECK is a CC chemokine, specifically expressed by thymic stromal cells, and signals through the CCR9 receptor. TECK is chemotactic towards activated macrophages, thymocytes and dendritic cells. Recombinant human TECK is a 14.2 kDa protein containing 127 amino acid residues, including the four conserved cysteine residues present in CC chemokines.
Description: TECK is a CC chemokine, specifically expressed by thymic stromal cells, and signals through the CCR9 receptor. TECK is chemotactic towards activated macrophages, thymocytes and dendritic cells. Recombinant human TECK is a 14.2 kDa protein containing 127 amino acid residues, including the four conserved cysteine residues present in CC chemokines.
Description: BCA-1/BLC, a CXC chemokine, is expressed in the liver, spleen, lymph nodes, appendix and stomach. It exerts its activities through its only receptor CXCR5. BCA-1/BLC is a potent chemoattractant for B lymphocytes and induces weak chemotactic response in T cells and macrophages. It manifests no activity on neutrophils and monocytes. Recombinant Human BCA-1 is a 10.3 kDa protein containing 87 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines.
Description: BCA-1/BLC, a CXC chemokine, is expressed in the liver, spleen, lymph nodes, appendix and stomach. It exerts its activities through its only receptor CXCR5. BCA-1/BLC is a potent chemoattractant for B lymphocytes and induces weak chemotactic response in T cells and macrophages. It manifests no activity on neutrophils and monocytes. Recombinant Human BCA-1 is a 10.3 kDa protein containing 87 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines.
Description: Breast and Kidney-expressed chemokine (BRAK) is a CXC chemokine expressed in normal tissue in the absence of inflammatory stimuli, and infrequently expressed in cancer cell lines. BRAK is known to be a highly selective monocyte chemoattractant. However, main function and receptor selectivity is unknown at this time. BRAK contains the four highly conserved cysteine residues present in CXC chemokines. The sequence of the mature protein consists of 87 amino acid residues, and is approximately 30% homologous to the sequences of MIP-2 alpha and beta. Recombinant human BRAK is a 9.4 kDa protein containing 77 amino acid residues.
Description: Breast and Kidney-expressed chemokine (BRAK) is a CXC chemokine expressed in normal tissue in the absence of inflammatory stimuli, and infrequently expressed in cancer cell lines. BRAK is known to be a highly selective monocyte chemoattractant. However, main function and receptor selectivity is unknown at this time. BRAK contains the four highly conserved cysteine residues present in CXC chemokines. The sequence of the mature protein consists of 87 amino acid residues, and is approximately 30% homologous to the sequences of MIP-2 alpha and beta. Recombinant human BRAK is a 9.4 kDa protein containing 77 amino acid residues.
Description: CTACK is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T-cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant human CTACK is a 10.2 kDa protein containing 88 amino acid residues.
Description: CTACK is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T-cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant human CTACK is a 10.2 kDa protein containing 88 amino acid residues.
Description: CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal mucin-like stalk sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant human CXCL16 is a 10.1 kDa protein containing 89 amino acid residues.
Description: CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal mucin-like stalk sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant human CXCL16 is a 10.1 kDa protein containing 89 amino acid residues.
Description: MEC is a secreted CC chemokine expressed primarily by epithelial cells of the bronchioles, salivary gland, mammary gland and colon. MEC signals through the CCR10 receptor and chemoattracts resting CD4, CD8 T-cells and eosinophils. MEC contains six cysteines including the four highly conserved cysteine residues present in CC chemokines. Recombinant human MEC is a 12.3 kDa protein containing 108 amino acid residues.
Description: MEC is a secreted CC chemokine expressed primarily by epithelial cells of the bronchioles, salivary gland, mammary gland and colon. MEC signals through the CCR10 receptor and chemoattracts resting CD4, CD8 T-cells and eosinophils. MEC contains six cysteines including the four highly conserved cysteine residues present in CC chemokines. Recombinant human MEC is a 12.3 kDa protein containing 108 amino acid residues.
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant rat GRO/KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
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Schwann Cell Cultures: Biology, Expertise and Therapeutics
Schwann cell (SC) cultures from experimental animals and human donors will be ready utilizing almost any kind of nerve at any stage of maturation to render stage- and patient-specific populations. Strategies to isolate, purify, develop in quantity, and differentiate SCs from grownup, postnatal and embryonic sources are environment friendly and reproducible as these have resulted from amassed refinements launched over many a long time of labor.
Albeit some exceptions, SCs will be passaged extensively whereas sustaining their regular proliferation and differentiation controls. Because of their lineage dedication and powerful resistance to tumorigenic transformation, SCs are secure to be used in therapeutic approaches within the peripheral and central nervous programs.
This evaluate summarizes the evolution of labor that led to the strong applied sciences used at present in SC culturing together with the primary options of the first and expanded SCs that make them irreplaceable fashions to grasp SC biology in well being and illness. Conventional and rising approaches in SC tradition are mentioned in mild of their potential functions.
Lastly, some fundamental assumptions in vitro SC fashions are recognized in an try and uncover the mixed worth of previous and new developments in tradition protocols and the mobile merchandise which might be derived.
Atherosclerosis: cellbiology and lipoproteins
Objective of evaluate: Lipoproteins have vital function in each the promotion and prevention of atherosclerosis. This transient evaluate will concentrate on latest stories on relationship between HDL and HDL subclasses and their composition and performance, the function of apoC-III in metabolism of triglyceride-rich lipoproteins, the affect of Lipoprotein (a) (Lp(a)) on endothelial cells, and the mechanism of uptake of aggregated LDL by macrophages.
Latest findings: The complexity of the protein and lipid content material of murine and human HDL and their relationship to its ldl cholesterol efflux capability have been examined. HDL has additionally been proven to have each antiatherogenic and proatherogenic properties.
The connection between apoC-III and LPL exercise, apoprotein E mediated clearance of triglyceride-rich lipoproteins and the potential significance of apoC-III within the elevated threat of heart problems in kind 1 diabetics has been investigated. Oxidized phospholipid in Lp(a) promotes endothelial cells inflammatory and glycolytic responses.
TLR4 participates within the uptake of aggregated LDL to contribute to foam cell formation. Abstract: These research contribute to our mechanistic understanding of how lipoproteins contribute to atherogenesis and determine potential therapeutic targets.
Description: This gene is a member of the septin family of GTPases. Members of this family are required for cytokinesis. One version of pediatric acute myeloid leukemia is the result of a reciprocal translocation between chromosomes 11 and X, with the breakpoint associated with the genes encoding the mixed-lineage leukemia and septin 2 proteins. This gene encodes four transcript variants encoding three distinct isoforms. An additional transcript variant has been identified, but its biological validity has not been determined.
Description: This gene is a member of the septin family involved in cytokinesis and cell cycle control. This gene is a candidate for the ovarian tumor suppressor gene. Mutations in this gene cause hereditary neuralgic amyotrophy, also known as neuritis with brachial predilection. A chromosomal translocation involving this gene on chromosome 17 and the MLL gene on chromosome 11 results in acute myelomonocytic leukemia. Multiple alternatively spliced transcript variants encoding different isoforms have been described.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is highly expressed in brain and heart. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. One of the isoforms (known as ARTS) is distinct; it is localized to the mitochondria, and has a role in apoptosis and cancer.
Description: This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is mapped to 22q11, the region frequently deleted in DiGeorge and velocardiofacial syndromes. A translocation involving the MLL gene and this gene has also been reported in patients with acute myeloid leukemia. Alternative splicing results in multiple transcript variants. The presence of a non-consensus polyA signal (AACAAT) in this gene also results in read-through transcription into the downstream neighboring gene (GP1BB; platelet glycoprotein Ib), whereby larger, non-coding transcripts are produced.
Description: This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. The yeast CDC10 protein is a structural component of the 10 nm filament which lies inside the cytoplasmic membrane and is essential for cytokinesis. This human protein functions in gliomagenesis and in the suppression of glioma cell growth, and it is required for the association of centromere-associated protein E with the kinetochore. Alternative splicing results in multiple transcript variants. Several related pseudogenes have been identified on chromosomes 5, 7, 9, 10, 11, 14, 17 and 19.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Description: This gene encodes a guanine-nucleotide binding protein and member of the septin family of cytoskeletal GTPases. Septins play important roles in cytokinesis, exocytosis, embryonic development, and membrane dynamics. Multiple transcript variants encoding different isoforms have been found for this gene.
Description: This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. The yeast CDC10 protein is a structural component of the 10 nm filament which lies inside the cytoplasmic membrane and is essential for cytokinesis. This human protein functions in gliomagenesis and in the suppression of glioma cell growth, and it is required for the association of centromere-associated protein E with the kinetochore. Alternative splicing results in multiple transcript variants. Several related pseudogenes have been identified on chromosomes 5, 7, 9, 10, 11, 14, 17 and 19.
Description: This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is mapped to 22q11, the region frequently deleted in DiGeorge and velocardiofacial syndromes. A translocation involving the MLL gene and this gene has also been reported in patients with acute myeloid leukemia. Alternative splicing results in multiple transcript variants. The presence of a non-consensus polyA signal (AACAAT) in this gene also results in read-through transcription into the downstream neighboring gene (GP1BB; platelet glycoprotein Ib), whereby larger, non-coding transcripts are produced.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Description: This gene is a member of the septin family of GTPases. Members of this family are required for cytokinesis and the maintenance of cellular morphology. This gene encodes a protein that can form homo- and heterooligomeric filaments, and may contribute to the formation of neurofibrillary tangles in Alzheimer's disease. Alternatively spliced transcript variants have been found but the full-length nature of these variants has not been determined. [provided by RefSeq, Dec 2012]
Description: This is Competitive Enzyme-linked immunosorbent assay for Antibody Detection.detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in serum, plasma and other biological fluids.
Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) ELISA Kit
Description: This is Competitive Enzyme-linked immunosorbent assay for Antibody Detection.detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in serum, plasma and other biological fluids.
Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) ELISA Kit
Description: This is Competitive Enzyme-linked immunosorbent assay for Antibody Detection.detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in serum, plasma and other biological fluids.
Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) ELISA Kit
Description: This is Competitive Enzyme-linked immunosorbent assay for Antibody Detection.detection of Human Anti-Anti-Sperm Antibody Antibody (Anti-AsAb) in serum, plasma and other biological fluids.
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