Glycophorins are the major sialoglycoprotein component of erythrocyte cell membranes. They are heavily glycosylated and rich in sialic, making the erythrocytes membranes very hydrophilic. This property enables them to circulate without adhering to other cells or the walls of blood vessels. Glycophorins are classified based on the quantity present in the cell membrane. Glycophorin A is the most abundant. The N-terminal glycosylated segment of glycophorin A, which lies outside the erythrocyte membrane, bears MN blood group receptors. It is encoded by the GYPA gene in humans, and many variants exist due to recombination between the GYPA and GYPB genes. Glycophorin A contains a receptor for binding the malaria parasite Plasmodium falciparum; it also binds several viruses. Glycophorin A is also known as sialoglycoprotein alpha, MN sialoglycoprotein, CD235a antigen, MN, GPA, MNS, GPSAT, PAS-2, CD235a, GPErik, HGpMiV, HGpMiXI, and HGpSta(C).
This product is an affinity-purified IgG antibody that recognizes human glycophorin A protein. The antibody was raised in mouse using human glycophorin A, and can be used for immunocytochemical (ICC) detection of human glycophorin A protein.