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Glycophorin A / CD235a (Erythrocyte Marker) Antibody - With BSA and Azide
Mouse Monoclonal Antibody [Clone A63-B/C2 ]
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IF, FC |
|---|---|
| Primary Accession | P02724 |
| Other Accession | 2993, 2994, 434973, 654368 |
| Reactivity | Human, Bovine |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | Mouse / IgM, kappa |
| Clone Names | A63-B/C2 |
| Calculated MW | 39kDa |
| Gene ID | 2993 |
|---|---|
| Other Names | Glycophorin-A, MN sialoglycoprotein, PAS-2, Sialoglycoprotein alpha, CD235a, GYPA, GPA |
| Storage | Store at 2 to 8°C.Antibody is stable for 24 months. |
| Precautions | Glycophorin A / CD235a (Erythrocyte Marker) Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | GYPA (HGNC:4702) |
|---|---|
| Function | Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). 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. |
| Cellular Location | Cell membrane; Single-pass type I membrane protein Note=Appears to be colocalized with SLC4A1 |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Cartron JP and Rahuel C. Human erythrocyte glycophorins: protein and gene structure analyses. Transfus Med Rev 1992,6(2):63-92 | Gahmberg CG et al. Biosynthesis of the major human red cell sialoglycoprotein, glycophorin A. A review. Rev Fr Transfus Immunohematol 1981,24(1):53-73 | Wybenga LE et al. Glycophorin as a receptor for Sendai virus. Biochemistry 1996,35(29):9513-8 | Rahuel C et al. Post-transcriptional regulation of the cell surface expression of glycophorins A, B, and E. J Biol Chem 1994, 269(52):32752-8 | Thacker TC and Johnson FB. Binding of bovine parvovirus to erythrocyte membrane sialylglycoproteins. J Gen Virol 1998, 79:2163-
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