IGSF8 Recombinant Rabbit mAb (S-2101-176)

IGSF8 also known as EWI-2 or CD316, is a single-pass transmembrane protein belonging to the EWI subfamily of the immunoglobulin superfamily. Its core function is to act as an adaptor protein, linking tetraspanin-enriched membrane microdomains (such as CD9, CD81, and CD82) to the cytoskeleton, thereby participating in the regulation of various processes including cell migration, adhesion, and signal transduction. The IGSF8 protein structurally contains an EWI (glutamic acid-tryptophan-isoleucine) motif and multiple immunoglobulin-like domains, with the extracellular immunoglobulin-like domains responsible for interacting with tetraspanins such as CD9 and CD81, while the intracellular region can connect to cytoskeletal proteins. Functionally, IGSF8 plays multifaceted roles: it is a key regulator of the immune system, acting as an inducible receptor for HSPA8 on dendritic cells to regulate their migration, and it can also inhibit the killing of tumor cells by natural killer cells through interaction with their receptors; simultaneously, it is an important tumor suppressor that inhibits cancer cell migration and proliferation by suppressing epidermal growth factor receptor endocytosis and promoting the degradation of growth factor receptors. Furthermore, IGSF8 also plays roles in nervous system development and in resisting viral infections such as hepatitis C virus and HIV-1.