Anti-CD235a / Glycophorin A Monoclonal Antibody (Clone:JC159)-APC Conjugated

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. Protein function: 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). [The UniProt Consortium]