Mouse Anti-Human CD98 Antibody (S-5622)

CD98 (also known as 4F2hc or SLC3A2) is a multifunctional type II membrane glycoprotein that serves as a heavy chain and forms heterodimers with various amino acid transporter light chains through disulfide bonds, playing key roles in amino acid transport, cell adhesion, cell fusion, and tumorigenesis. It consists of an intracellular N-terminal domain, a single transmembrane region, and a large extracellular domain. The crystal structure of the extracellular domain reveals homology to bacterial alpha-amylase, featuring a TIM barrel and a beta-sandwich fold, but it lacks catalytically active residues. CD98 covalently binds to light chains such as LAT1, LAT2, y+LAT1, and xCT via Cys109, transporting them to the plasma membrane and regulating their transport functions, thereby mediating the activity of L-type, y+L-type, and other amino acid transport systems. In addition, CD98 participates in beta1 integrin signaling, cell fusion, viral infection, and mTOR pathway regulation. It is highly expressed in various tumors and is associated with tumor progression and metastatic potential.