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Glycophorin-A / CD235a Monoclonal Mouse Antibody (A63-B/C2)

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Note: Please be advised that primary antibodies with catalog numbers that begin with “BN” will only be offered conjugated to CF®405S, CF®488A, CF®568, CF®594, CF®640R, CF®647, and biotin as of 5/27/2022. However, previously available primary antibody conjugates that are in stock will remain available until inventory is exhausted. Please view the list of available conjugates on the product page. We also recommend our easy-to-use Mix-n-StainTM Antibody Labeling Kits for labeling antibodies with all CF® Dyes. We apologize for the inconvenience.
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Product Description

Recognizes a sialoglycoprotein of 39 kDa, 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.

This antibody is available purified with BSA/azide at 200 ug/mL, or BSA/azide-free at 1 mg/mL.

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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