SLP-76 Recombinant Rabbit mAb (S-3472-13)

SLP-76 (SH2 domain-containing leukocyte protein of 76 kDa) is a 76 kDa adaptor protein encoded by the LCP2 gene. It is primarily expressed in hematopoietic cells such as T cells, natural killer (NK) cells, mast cells, and platelets, where it plays a central scaffolding role in immune receptor signal transduction. The protein contains multiple functional domains: an N-terminal acidic domain, three tyrosine-based signaling motifs (Tyr112, Tyr128, Tyr145), and three serine/proline-rich regions, while the C-terminus harbors an SH2 domain and a SAM domain. Upon T cell receptor (TCR) activation, the upstream kinase ZAP-70 first phosphorylates the N-terminal tyrosine residues of SLP-76; these phosphorylated tyrosine sites then recruit and activate multiple downstream effector molecules, including Vav1 (regulating cytoskeletal rearrangement), Nck (mediating actin polymerization), PLCγ1 (initiating calcium signaling and PKC activation), and Gads (connecting SLP-76 to LAT to form the signalosome). Through these interactions, SLP-76 precisely regulates key processes such as T cell activation, proliferation, differentiation, as well as cytoskeletal remodeling, adhesion, and migration. At the developmental level, SLP-76 is indispensable for positive selection and maturation of T cells in the thymus; knockout of SLP-76 leads to severe blockade of T cell development. Under pathophysiological conditions, dysfunction of SLP-76 is closely associated with immunodeficiency diseases, autoimmune disorders (such as systemic lupus erythematosus), and T cell leukemia/lymphoma.