redFluor™ 710 Anti-Ly76 antibody [TER-119]

Supplementary info

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

Activity summary

Ly76 also known as glycophorin A is a well-defined protein expressed predominantly on the surface of red blood cells. This protein consisting of approximately 152 amino acids and with a molecular mass of around 31 kilodaltons plays a role in maintaining cell integrity. Glycophorin A is responsible for making the cell membrane more pliable facilitating proper red blood cell function. It is also important for serving as a receptor or a carrier for various molecules that interact with the cell surface.

Biological function summary

Glycophorin A contributes to the structural stability and flexibility of erythrocyte membranes. It participates as a part of the complex with other proteins such as band 3 and protein 4.2 which support the stability of the membrane's cytoskeletal architecture. This interaction is important for the proper shape and resilience of red blood cells enabling them to withstand shear stress as they travel through narrow capillaries. Additionally glycophorin A carries carbohydrate structures that can serve as antigens which are vital for immune recognition.

Pathways

Glycophorin A engages in pathways related to erythrocyte function and immune interactions. It interacts with proteins integral to maintaining red blood cell membrane structure and flexibility such as band 3 and spectrin. Moreover glycophorin A plays a role in pathways involved in the attachment of various pathogens which exploit this protein to gain entry into the erythrocytes. These interactions highlight the protein’s significance within the hematological cellular environment and immune response mechanisms.

Associated diseases and disorders

Glycophorin A is associated with conditions affecting red blood cells such as hereditary spherocytosis and malaria. Hereditary spherocytosis involves abnormalities in erythrocyte membrane proteins where glycophorin A alongside proteins like ankyrin and spectrin can show altered expression or function leading to morphological changes in red blood cells. In malaria the Plasmodium parasite exploits glycophorin A for entry into red blood cells where mutations in glycophorin A can confer some resistance to infection. Understanding its role in these conditions underlines the protein's importance in both physiological and pathological contexts.