APC/Cy7® Anti-Glycophorin A antibody [JC159]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Glycophorin A also known as CD235a is a major glycoprotein of red blood cell membranes with a mass around 31 kDa. It is importantly expressed on the surface of erythrocytes. Glycophorin A plays an important role in maintaining cell membrane integrity and is associated with various antigenic sites which are important for compatibility testing. Researchers often detect Glycophorin A using antibodies such as Glycophorin A APC or Glycophorin A FITC in flow cytometry studies due to its distinct expression on red blood cells.

Biological function summary

Glycophorin A interacts with other membrane proteins to form part of the membrane's skeletal protein network. This network stabilizes the erythrocyte structure and contributes to its flexibility essential for passing through narrow capillaries. Glycophorin A does not form part of any large multiprotein complex but does interact with other glycophorins such as Glycophorin B. These interactions help to form the MN and Ss blood group antigens.

Pathways

Glycophorin A is involved in several pathways including the erythrocyte development and lipid raft pathways. These pathways are important for cell signaling and membrane transport processes. Glycophorin A's role in erythrocyte development is connected to protein 4.1R which links the membrane to the underlying cytoskeleton influencing red blood cell shape and stability. Additionally its role in lipid raft-mediated signaling intersects with proteins involved in immune response regulation.

Associated diseases and disorders

Glycophorin A has associations with several conditions including malaria and hereditary spherocytosis. The interaction between Plasmodium falciparum and Glycophorin A contributes to the parasite's ability to invade erythrocytes indicating its relevance in malaria research. Additionally abnormalities with Glycophorin A expression or structure can lead to hereditary spherocytosis often related to a disruption in its interaction with ankyrin another structural protein. Understanding these associations helps elucidate the pathological mechanisms and potential therapeutic targets for these diseases.