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Description

T-cell surface protein tactile (UniProt: Q3U0X8, also known as Cell surface antigen CD96, T cell-activated increased late expression protein, CD96) is encoded by the Cd96 gene (Gene ID: 85444) in murine species. CD96 is a single-pass type I, disulfide-linked, homodimeric, membrane glycoprotein protein of the poliovirus receptor (PVR, CD155)-nectin family that is synthesized with a signal peptide (aa 1-21), which is subsequently cleaved off to produce the mature form that contains an extracellular domain (aa 22-536), a transmembrane domain (aa 537-557), and a cytoplasmic domain (aa 558-602). It contains two Ig-like V-type 2 domains (aa 24-134 and 138-244) and one Ig-like C2-type domain (aa 250-355). These three Ig-like domains are separated from the transmembrane domain by a long region that is rich in proline, serine, and threonine. The cytoplasmic region contains a proline-rich tandem that is flanked by arginine and lysine residues and represents binding site for SH3 domain containing signaling components. CD96 is expressed mainly by cells of hematopoietic origin, in particular on T and NK cells. It is involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. It promotes NK cell-target adhesion by interacting with CD155 (PVR) present on target cells. Clone 6A6 is reported to bind to the first Ig domain of CD96 and competes with CD155 binding. It is shown to significantly reduce experimental lung metastases in murine models at low doses. (Ref.: Aguilera, AR., et al. (2018). OncoImmunology 7(5), e1424677, Georgiev, H., et al. (2018). Front. Immunol. 9, 1072, Meyer, D., et al. (2009). J. Biol. Chem. 284(4), 2235-2244).