SLP-76 Recombinant Rabbit mAb (SDT-3472-28）

SLP-76 (SH2 domain-containing leukocyte protein of 76 kDa) is a critical adaptor protein in the T cell receptor (TCR) signaling pathway, expressed predominantly in hematopoietic cells, especially T cells, natural killer cells, platelets, and mast cells. Structurally, it contains several functional modules: the N-terminal region has three tandem tyrosine-based motifs responsible for recruiting SH2 domain-containing downstream effector proteins such as Vav, Nck, and Itk; the central region contains a proline-rich motif that binds adaptor proteins like Gads to mediate interaction with LAT (linker for activation of T cells); and the C-terminal SH2 domain participates in feedback regulation of the signal complex. Upon TCR activation, SLP-76 is phosphorylated by ZAP-70 kinase, subsequently recruiting and activating downstream effectors including PLCγ1, Vav, PI3K, and Grb2, thereby initiating multiple critical signaling cascades such as calcium mobilization, the Ras-MAPK pathway, cytoskeletal rearrangement, and integrin activation, ultimately regulating T cell proliferation, differentiation, cytokine production, and immunological synapse formation. SLP-76 is indispensable for early T cell development, thymocyte positive selection, regulatory T cell function, and effector T cell responses; its deficiency leads to T cell developmental arrest, immunodeficiency, and severe autoimmunity. In platelets, SLP-76 participates in collagen-induced platelet activation and thrombus formation via the GPVI receptor. Furthermore, aberrant expression or mutations of SLP-76 are associated with immune dysregulation disorders (e.g., systemic lupus erythematosus), T-cell acute lymphoblastic leukemia, and certain primary immunodeficiencies. Owing to its nature as a central adaptor protein, SLP-76 is considered a potential regulatory node for T cell-mediated immunotherapy, holding significant research value in tumor immunity, autoimmune diseases, and antiviral immunity.