SLP-76 (pY128) Mouse, PE, Clone: J141-668.36.58, BD

Description

• SLP-76 (SH2 domain-containing Leukocyte Protein of 76kDa) is a tyrosine phosphoprotein that is involved in the T cell receptor (TCR) -mediated intracellular signaling pathway
• It may be involved in the signaling pathways of other peripheral blood leukocytes; thymic/splenic cells; and in human T, B, and monocytic cell lines
• SLP-76 consists of several motifs that signify its importance in protein-protein interactions involved in intracellular signaling pathways, such as the SH2 domain in the C-terminus, the three amino-terminus 17-amino acid repeats with conserved tyrosine and acidic residues (DYE(S/P)P), and a proline rich region
• SLP-76 has been shown to associate with Gads, Grb2, PLCg1, SLAP-130, and Vav, all of which are part of the signaling cascade in T lymphocytes
• An early event in the T cell activation pathway is the phosphorylation, by the Syk-family kinase ZAP-70, of SLP-76 at the three conserved tyrosine motifs, which then mediate interactions with downstream effectors
• The phosphorylated tyrosine 128 (Y128) brings the Rho family guanine nucleotide exchange factor Vav1 and the Nckm adapter protein, which binds to p21-activated kinase (PAK1) and Wiskott-Aldrich syndrome protein (WASP), into the activation complex
• Vav1, PAK1, and WASP may mediate TCR-stimulated actin cytoskeletal rearrangement
• The J141-688.36.58 monoclonal antibody recognizes the phosphorylated Y128 of activated SLP-76
• Intracellular Staining