Anti-SLP76 Antibody, Alexa Fluor(R) 488 Conjugate from rabbit, ALEXA FLUOR(R) 488

Lymphocyte cytosolic protein 2 (UniProt: Q13094; also known as Lymphocyte cytosolic protein 2, SH2 domain-containing leukocyte protein of 76 kDa, SLP-76 tyrosine phosphoprotein, SLP76) is encoded by the gene LCP2 (Gene ID 3937) in human. SLP-76 is a cytoplasmic adaptor phosphoprotein that contains both SH2 and SAM domains and is involved in B and T cell receptor signaling. Its amino terminus contains an acidic region that includes a PEST domain and several tyrosine residues that are phosphorylated following TCR ligation. SLP-76 also contains a central proline-rich domain and a SH2 domain at its carboxy terminal. SLP-76 can be phosphorylated on multiple tyrosine residues by the upstream kinases ZAP-70 and Lck. SLP-76 phosphorylation plays an important role in T cell-mediated IL-2 production by allowing phosphorylated Vav to bind and this complex stimulates NFAT and IL-2 gene activation after TCR engagement. SLP-76 is highly expressed in spleen, thymus, and peripheral blood leukocytes and T cells. It is expressed in B cell lines at lower levels and is not detected in fibroblast and neuroblastoma cell lines. SLP-76 is reported to play a positive role in promoting T cell development and activation as well as mast cell and platelet function. Overexpression of SLP-76 is shown to enhance IL-2 transcription after TCR signaling.