SLAMF6 Protein, Human (HEK293)

SLAMF6, a self-ligand receptor within the signaling lymphocytic activation molecule (SLAM) family, plays a crucial role in modulating the activation and differentiation of diverse immune cells, contributing to the intricate regulation and coordination of both innate and adaptive immune responses. The activities of SLAMF6 are finely controlled by the presence or absence of small cytoplasmic adapter proteins, such as SH2D1A/SAP and/or SH2D1B/EAT-2. Notably, SLAMF6 triggers cytolytic activity specifically in natural killer (NK) cells expressing high surface densities of natural cytotoxicity receptors and engages positive signaling in NK cells, involving the phosphorylation of VAV1 and dependence on SH2D1B rather than SH2D1A. In conjunction with SLAMF1, SLAMF6 governs the transition and differentiation of the thymocytic natural killer T (NKT) cell lineage. Additionally, SLAMF6 promotes T-cell differentiation into a Th17 phenotype, leading to increased IL-17 secretion, and acts in concert with SLAMF1 and CD84/SLAMF5 as a potential negative regulator of the humoral immune response. Furthermore, in the absence of SH2D1A/SAP, SLAMF6 can transmit negative signals to CD4(+) T-cells and NKT cells, negatively regulating germinal center formation and potentially contributing to B-cell tolerance in germinal centers while preventing autoimmunity. SLAMF6 exists as a homodimer and interacts with PTN6 and PTN11, as well as with SH2D1A/SAP and SH2D1B/EAT2, with both adapter proteins able to associate with the same SLAMF6 molecule, mediated by ITSM 2.