Purity > 90% as determined by SDS-PAGE. MW: 9.9kDa. Extracellular Domain: 20-91aa. N-terminal 6xHis-tagged. Homo sapiens (Human). Glycophorin A is the major intrinsic mbrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte mbrane, 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 mbrane. 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).