A portion of amino acids 249-335 from the human protein was used as the immunogen for the SLAMF7 antibody.
CS1, also known as novel Ly9, SLAMF7, 19A24 or CRACC, is a homophilic cell surface receptor. It is a member of the SLAM (signaling lymphocytic activation molecule) family of receptors expressed on natural killer (NK) cells, T cells and stimulated B cells. CS1 contains immunoreceptor tyrosine-based switch motifs in its cytoplasmic domain but, unlike other SLAM receptors, it does not recruit SAP (SLAM-associated protein). In humans, CS1 activates NK cells through an EAT-2-mediated pathway that is SAP-independent. CS1 recruits and associates with EAT-2, a protein closely related to SAP. EAT-2 induces phosphorylation of CS1 which then, upon ligand binding, activates downstream cytotoxicity effectors PLC and PI 3K. In mice, the EAT-2 association with CS1 has an inhibitory effect on the activation of NK cells.
