CRACC/SLAMF7 Protein, Mouse (HEK293, mFc)

The CRACC/SLAMF7 protein functions as a self-ligand receptor within the signaling lymphocytic activation molecule (SLAM) family. Through homo- or heterotypic cell-cell interactions, SLAM receptors modulate the activation and differentiation of a diverse array of immune cells, playing a crucial role in the regulation and coordination of both innate and adaptive immune responses. The activities of CRACC/SLAMF7 are intricately controlled by the presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP, and/or SH2D1B/EAT-2. The protein mediates natural killer (NK) cell activation through a SH2D1A-independent extracellular signal-regulated ERK-mediated pathway and positively regulates NK cell functions in a mechanism dependent on the adapter SH2D1B. Additionally, homotypic interactions between NK cells may contribute to activation, but in the absence of SH2D1B, CRACC/SLAMF7 inhibits NK cell function. It also exerts inhibitory effects in T-cells and may play a role in lymphocyte adhesion. In LPS-activated monocytes, CRACC/SLAMF7 negatively regulates the production of pro-inflammatory cytokines. The protein further interacts with various signaling molecules, including SH2D1B, PTPN6/SHP-1, PTPN11/SHP-2, INPP5D/SHIP1, CSK, and FYN, highlighting its involvement in diverse cellular processes and molecular interactions.