Paradigm Shifts in Mast Cell and Basophil Biology and Operate: An Rising View of Immune Regulation in Well being and Illness
The physiological position of the mast cell and basophil has for a few years remained enigmatic. On this chapter, we briefly summarize a number of the more moderen research that shed new mild on the position of mast cells and basophils in well being and illness
. What we achieve from these research is a brand new appreciation for mast cells and basophils as sentinels in host protection and an extra understanding that dysregulation of mast cell and basophil perform generally is a element of assorted ailments aside from allergy symptoms.
Maybe a very powerful perception reaped from this work is the rising consciousness that mast cells and basophils can perform as immunoregulatory cells that modulate the immune response in well being and illness. Collectively, the current data supplies new challenges and alternatives towards the event of novel therapeutic methods to enhance host safety and modify illness by manipulation of mast cell and basophil perform.
Pure killer cells in most cancers biology and remedy
The tumor microenvironment is extremely advanced, and immune escape is at present thought-about an essential hallmark of most cancers, largely contributing to tumor development and metastasis. Named for his or her functionality of killing goal cells autonomously, pure killer (NK) cells function the primary effector cells towards most cancers in innate immunity and are extremely heterogeneous within the microenvironment.
Most present therapy choices harnessing the tumor microenvironment give attention to T cell-immunity, both by selling activating indicators or suppressing inhibitory ones. The restricted success achieved by T cell immunotherapy highlights the significance of creating new-generation immunotherapeutics, for instance using beforehand ignored NK cells.
Though tumors additionally evolve to withstand NK cell-induced cytotoxicity, cytokine complement, blockade of suppressive molecules and genetic engineering of NK cells could overcome such resistance with nice promise in each strong and hematological malignancies. On this overview, we summarized the elementary traits and up to date advances of NK cells inside tumor immunometabolic microenvironment, and mentioned potential utility and limitations of rising NK cell-based therapeutic methods within the period of presicion medication.
Replace on the Biology, Administration, and Therapy of Small Cell Lung Most cancers (SCLC)
Small-cell lung most cancers (SCLC) accounts for 13-15% of all new lung most cancers circumstances within the US. The tumor tends to disseminate early leading to 80-85% of sufferers being identified with in depth illness (ES-SCLC). Chemotherapy has offered SCLC sufferers appreciable survival advantages over the previous three many years. Nonetheless, most sufferers relapse and barely survive past 2 years.
Regardless of constant total response charges of ≥50%, till lately, median survival occasions and 2-year survivals solely ranged between 7-10 months and 10-20%, respectively.
A number of chemotherapy brokers possess exercise towards SCLC, each, as single brokers and in mixtures however etoposide-platinum emerged as the popular first line routine.
Upon relapse, many sufferers stay candidates for extra remedy. Nonetheless, the sensitivity of relapsed SCLC to additional therapies is markedly decreased and dependent upon the extent and length of response to the preliminary therapy (platinum-sensitive vs. resistant relapse).
A number of elements counsel a therapeutic position for immunotherapy in SCLC: SCLC has been related to immune-mediated paraneoplastic processes (cerebellar degeneration, limbic encephalitis, and Lambert-Eaton syndrome) and sufferers presenting with these paraneoplastic syndromes have proven extra favorable outcomes, suggesting an underlying immune response mechanism.
Complete genomic profiling of SCLC signifies that almost all lack purposeful p53 (90%) and Rb1 (65%).
These common genetic aberrations facilitate poor genomic stability, thus perpetuating the technology of tumor related antigens, amenable to concentrating on with immunotherapy.
SCLC has one of many highest mutational masses, probably a mirrored image of the myriad of insults inflicted by smoking-related carcinogens.
The connection between tumor mutational load and response to immune checkpoint inhibitors has been established in a number of strong tumors, together with preliminary ends in relapsed SCLC.
On this manuscript, we overview the early (some failed and discontinued, some partly profitable, and nonetheless ongoing) makes an attempt to include immunotherapy (significantly vaccine primarily based approaches) to the therapy of SCLC, and the most recent makes an attempt (principally incorporating using checkpoint inhibitors), together with these with favorable however preliminary outcomes (CheckMate 032, Keynote 028 and 158), and people with extra definitive optimistic (iMpower 133 and CASPIAN) and unfavourable (CheckMate 331 and 451) outcomes.
Description: A polyclonal antibody against LIN28A. Recognizes LIN28A from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC, IF; Recommended dilution: IHC:1:20-1:200, IF:1:50-1:200
Description: A polyclonal antibody against LIN28A. Recognizes LIN28A from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC, IF
Description: A polyclonal antibody against LIN28A. Recognizes LIN28A from Human, Mouse. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:1000-1:2000, IHC:1:25-1:100
Description: A polyclonal antibody against LIN28A. Recognizes LIN28A from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB;WB:1:500-1:1000
Description: A polyclonal antibody against LIN28A. Recognizes LIN28A from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB;WB:1:500-1:1000
Description: Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 [removed]By similarity). Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let- 7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre- let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, LIN28A down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'-GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation.
Description: Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 [removed]By similarity). Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let- 7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre- let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, LIN28A down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'-GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation.
Description: Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre- let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, Lin28a down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'- GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation.
Description: Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre- let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, Lin28a down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'- GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation.
Description: LIN28A is a translational enhancer that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression (By similarity). Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation.[UniProt]
Description: LIN28A is a translational enhancer that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression (By similarity). Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation.[UniProt]
Description: Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression (By similarity). Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, LIN28A down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'-GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation.
Description: Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression (By similarity). Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, LIN28A down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'-GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation.
Description: Protein lin-28 homolog A is a protein that in humans is encoded by the LIN28A gene. It is mapped to 1p36.11. This gene encodes a LIN-28 family RNA-binding protein that acts as a posttranscriptional regulator of genes involved in developmental timing and self-renewal in embryonic stem cells. The encoded protein functions through direct interaction with target mRNAs and by disrupting the maturation of certain miRNAs involved in embryonic development. This protein prevents the terminal processing of the LET7 family of microRNAs which are major regulators of cellular growth and differentiation. Aberrant expression of this gene is associated with cancer progression in multiple tissues.
Description: A polyclonal antibody against LIN7A. Recognizes LIN7A from Human, Mouse, Zebrafish. This antibody is Unconjugated. Tested in the following application: ELISA, WB; Recommended dilution: WB:1:1000-1:5000
Description: Human LIN28A, also known as Lin-28 Homolog A, with N-terminal FLAG-Avi-Tag, GenBank Accession No. NM_024674, a.a. 2-209 (end), expressed in a HEK293 cell expression system. MW = 26 kDa.
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Lin-28 Homolog A (LIN28A) in samples from tissue homogenates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Lin-28 Homolog A (LIN28A) in samples from tissue homogenates or other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Lin-28 Homolog A (LIN28A) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Lin-28 Homolog A (LIN28A) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Lin-28 Homolog A (LIN28A) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Lin-28 Homolog A (LIN28A) in tissue homogenates, cell lysates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Lin-28 Homolog A (LIN28A) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Lin-28 Homolog A (LIN28A) in Tissue homogenates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Lin-28 Homolog A (LIN28A) in Tissue homogenates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Lin-28 Homolog A (LIN28A) in Tissue homogenates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Lin-28 Homolog A (LIN28A) in Tissue homogenates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Lin-28 Homolog A (LIN28A) in samples from Tissue homogenates and other biological fluids. with no significant corss-reactivity with analogues from other species.
Methods biology method to exploring the impact of cyclic stretching on cardiac cell physiology
Though mechanical forces are concerned in pressure-overloaded cardiomyopathy, their results on gene transcription profiles will not be absolutely understood.
Right here, we used next-generation sequencing (NGS) to analyze adjustments in genomic profiles after cyclic mechanical stretching of human cardiomyocytes.
We discovered that 85, 87, 32, 29, and 28 genes had been differentially expressed after 1, 4, 12, 24, and 48 hours of stretching. Moreover, 10 of the 29 genes that had been up-regulated and 11 of the 28 that had been down-regulated after 24 h confirmed the identical adjustments after 48 h.
We then examined expression of the genes that encode serpin household E member 1 (SERPINE1), DNA-binding protein inhibitor 1 (ID1), DNA-binding protein inhibitor 3 (ID3), and CCL2, a cytokine that acts as chemotactic think about monocytes, in an RT-PCR experiment.
The identical adjustments had been noticed for all 4 genes in any case cyclic stretching durations, confirming the NGS outcomes. Taken collectively, these findings counsel that cyclical stretching can alter cardiac cell physiology by activating cardiac cell metabolism and impacting ldl cholesterol biosynthesis signaling.
Description: A sandwich quantitative ELISA assay kit for detection of Human Glycophorin A (GYPA) in samples from tissue homogenates, cell lysates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Human Glycophorin A (GYPA) in samples from tissue homogenates, cell lysates or other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Glycophorin A (GYPA) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Glycophorin A (GYPA) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Glycophorin A (GYPA) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Glycophorin A (GYPA) in tissue homogenates, cell lysates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Glycophorin A (GYPA) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A (MNS blood group), also known as GYPA, is a protein which in humans is encoded by the GYPA gene. GYPA has also been designated CD235a. Glycophorins A (GYPA) and B (GYPB) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups. [Wiki]
Description: Glycophorin A (MNS blood group), also known as GYPA, is a protein which in humans is encoded by the GYPA gene. GYPA has also been designated CD235a. Glycophorins A (GYPA) and B (GYPB) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups. [Wiki]
Description: Glycophorin A (MNS blood group), also known as GYPA, is a protein which in humans is encoded by the GYPA gene. GYPA has also been designated CD235a. Glycophorins A (GYPA) and B (GYPB) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups. [Wiki]
Description: Glycophorin A (MNS blood group), also known as GYPA, is a protein which in humans is encoded by the GYPA gene. GYPA has also been designated CD235a. Glycophorins A (GYPA) and B (GYPB) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups. [Wiki]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). [UniProt]
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
Description: A sandwich ELISA kit for detection of Glycophorin A from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids.
Description: GYPA Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 81 amino acids (20-91a.a.) and having a molecular mass of 9.1kDa. (Molecular size on SDS-PAGE under reducing conditions 18-28kDa).;GYPA is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Description: A competitive ELISA for quantitative measurement of Rat Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rat Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rat Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Porcine Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Porcine Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Porcine Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Canine Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Canine Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Canine Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Goat Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Goat Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Goat Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Mouse Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Mouse Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Mouse Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: Glycophorin-A, a member of the glycophorin-A family, is also known as CD235a and Gypa, which is heavily glycosylated on serine and threonine residues at the N-terminal extracellular domain. CD235a,a single-pass type III membrane protein,is the major intrinsic membrane sialoglycoprotein of the erythrocyte. Also,CD235a appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. Furthermore,CD235a may be involved in translocation of SLC4A1 to the plasma membrane.
Description: A competitive ELISA for quantitative measurement of Rabbit Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rabbit Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rabbit Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Monkey Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Monkey Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Monkey Glycophorin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Glycophorin A (GYPA) Polyclonal Antibody (Human), PE
Description: A competitive ELISA for quantitative measurement of Human Glycophorin E in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Human Glycophorin E in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
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