Clone REA387 recognizes the human CD98 antigen, a single-pass type II membrane glycoprotein. CD98 is broadly expressed on non-hematopoietic cells and also on peripheral blood lymphocytes, monocytes, and granulocytes. The CD98 heterodimer consists of a 80–85 kDa heavy chain (CD98hc, also known as 4F2 antigen heavy chain or FRP-1) that is disulfide-linked with a multi-pass light chain of 40 kDa. The heavy chain binds to the cytoplasmic tails of integrin-β chains and mediates adhesive signals that control cell spreading, survival, and growth. The light chain functions in amino acid transport. Some of the light chains have broad specificity, but the large neutral amino acid transporters LAT-1 and LAT-2 have preference for importing certain essential amino acids, particularly leucine, isoleucine, and arginine (LAT-1), in exchange for glutamine. Through its nutrient function, CD98 can contribute to the survival and growth of many cell types. CD98hc functions in amplifying integrin signaling and in the transport of amino acids. Both of these functions can contribute to cell survival and proliferation.
Additional information: Clone REA387 displays negligible binding to Fc receptors.