NKG2D/CD314 Protein, Human (sf9, His)

NKG2D/CD314 protein operates as an activating and costimulatory receptor essential for immunosurveillance, binding to diverse cellular stress-inducible ligands presented on autologous tumor cells and virus-infected cells. It plays a dual role in innate immune responses, stimulating both activating killer (NK) cells and acting as a costimulatory receptor for T-cell receptors (TCR) in CD8(+) T-cell-mediated adaptive immune responses, enhancing T-cell activation. The receptor facilitates perforin-mediated elimination of ligand-expressing tumor cells, and its signaling cascades involve calcium influx, ultimately leading to TNF-alpha expression. Additionally, NKG2D/CD314 participates in NK cell-mediated bone marrow graft rejection and may regulate the differentiation and survival of NK cells. Its ligand-binding capacity extends to various subfamilies of MHC class I-related glycoproteins, including MICA, MICB, RAET1E, RAET1G, RAET1L/ULBP6, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3), and ULBP4. The protein forms homodimers through disulfide linkage and heterohexamers with HCST/DAP10 subunits, a crucial interaction for NK cell surface expression and cytotoxicity induction. Furthermore, it can establish disulfide-bonded heterodimers with CD94 and interacts with CEACAM1, recruiting PTPN6 for VAV1 dephosphorylation, while not interacting with TYROBP.