Anti-Hu CD235a Purified GYPA Monoclonal Antibody

CD235a (Glycophorin A, GPA) is a transmembrane sialoglycoprotein expressed on erythrocytes and their precursors. Similarly to glycophorin B (GPB), these molecules provide the cells with a large mucin-like surface, which minimalizes aggregation between erythrocytes in the circulation. GPA is the carrier of blood group M and N specificities, while GPB accounts for S, s and U specificities. CD235a is a receptor of Hsa, an Streptococcus adhesin.

Membrane preparation from splenic hairy cell leukemia. The mouse monoclonal antibody JC159 recognizes an epitope between amino acids 27 and 40 of the extracellular portion of CD235a (glycophorin A), a sialoglycoprotein expressed on early erythroblasts, late erythroblasts, erythroblasts, mature erythrocytes and the cells of erythroid cell lines K562 and HEL. The antibody does not react with glycophorin B.

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) .