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Glycophorin C (GYPC) is an integral membrane glycoprotein. Additionally we are shipping Glycophorin C (Gerbich Blood Group) Proteins (9) and many more products for this protein.
Showing 10 out of 137 products:
Human Monoclonal GYPC Primary Antibody for IHC (fro), IP - ABIN2479395
King, Holmes, Mushens, Mawby, Reid, Scott: Reactivity with erythroid and non-erythroid tissues of a murine monoclonal antibody to a synthetic peptide having amino acid sequence common to cytoplasmic domain of human glycophorins C and D. in British journal of haematology 1995
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Human Monoclonal GYPC Primary Antibody for AGG, H - ABIN319934
Dahr, Blanchard, Kiedrowski, Poschmann, Cartron, Moulds: High-frequency antigens of human erythrocyte membrane sialoglycoproteins. VI. Monoclonal antibodies reacting with the N-terminal domain of glycophorin C. in Biological chemistry Hoppe-Seyler 1990
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The authors set out to understand the similarities and differences among the GYPC deletion alleles Yus and Gerbich by positional PCR sequence analysis to identify the breakpoints. They developed a set of diagnostic PCRs that can be used to classify both Yus and Gerbich phenotypic variants on the basis of their nucleotide deletion. The Yus phenotype was defined by 4 different breakpoints and the Ger
Plasmodium falciparum STEVOR functions as an erythrocyte-binding protein that recognizes Glycophorin C (GPC) on the red blood cell (RBC (show CACNA1C Antibodies)) surface and that its binding correlates with the level of GPC on the RBC (show CACNA1C Antibodies) surface.
Rosetting assays using CD236R knockdown normocytes derived from hematopoietic stem cells further supports the role of glycophorin C as a receptor in P vivax rosette formation.
Precise definition of the binding site for the EBA-140 ligand on glycophorin C may be important with respect to human erythrocyte invasion inhibition strategies based on a receptor.
Glycophorin C delta (exon3) is not associated with protection against severe anaemia in Papua New Guinea.
The Gerbich blood group (show DARC Antibodies) system
The molecular evolution of GYPC among the Hominoidea (Greater and Lesser Apes) and the pattern of polymorphism at the locus in a global human sample, were examined.
Recombinant Ge2, Ge3 & Ge4 antigens were cloned, expressed and purified. Yus and Ge mutants behaved in SDS (show SDS Antibodies)-PAGE similarly to normal GPC forms with diffuse glycosylation.
Data show that the receptor for Plasmodium falciparum erythrocyte-binding antigen 140 (EBA140) is glycophorin C (GYPC) and that this interaction mediates a principal P. falciparum invasion pathway into human erythrocytes.
Glycophorin C is identified as the receptor for PfEBP-2, the erythrocyte binding ligand of Plasmodium falciparum, and the binding domain on GPC is determined to be amino acid residues 14 through 22 within exon 2.
Glycophorin C (GYPC) is an integral membrane glycoprotein. It is a minor species carried by human erythrocytes, but plays an important role in regulating the mechanical stability of red cells. A number of glycophorin C mutations have been described. The Gerbich and Yus phenotypes are due to deletion of exon 3 and 2, respectively. The Webb and Duch antigens, also known as glycophorin D, result from single point mutations of the glycophorin C gene. The glycophorin C protein has very little homology with glycophorins A and B. Alternate splicing results in multiple transcript variants.
, Gerbich antigen
, glycoprotein beta
, sialoglycoprotein D