Glycophorin A (GPA) is a significant sialoglycoprotein found on the surface of human red blood cells (erythrocytes). It plays a crucial role in the MNS blood group system, which includes the M and N antigens. The mouse anti-human antibody targeting Glycophorin A is widely used in research and clinical diagnostics to study erythrocyte-related disorders and blood group antigens.
Glycophorin A is a type I transmembrane protein with a molecular weight of approximately 10 kDa . It is composed of 151 amino acids and exists as a homodimer in the cell membrane . The protein is heavily glycosylated, with numerous sialic acid residues contributing to its negative charge. This negative charge is essential for preventing red blood cells from sticking together and to the blood vessel walls.
Glycophorin A carries the antigenic determinants for the MNS blood group system. The M and N antigens are determined by the amino acid sequence at positions 1 and 5 of the protein. Specifically, the M antigen has serine and glycine at these positions, while the N antigen has leucine and glutamic acid .
Glycophorin A is not only important for blood group antigenicity but also plays a role in pathogen interactions. It serves as a receptor for various pathogens, including the malaria parasite Plasmodium falciparum, which binds to Glycophorin A during the invasion of red blood cells . Additionally, some viruses, such as the influenza virus and hepatitis A virus, also utilize Glycophorin A as a binding site .
The mouse anti-human Glycophorin A antibody is a monoclonal antibody that specifically binds to the Glycophorin A protein on human erythrocytes. This antibody can recognize both the M and N types of Glycophorin A, making it a valuable tool for various applications in research and diagnostics .