SLP-76 (phospho Tyr128) Rabbit Polyclonal Antibody

SLP-76 was originally identified as a substrate of the ZAP-70 protein tyrosine kinase following T cell receptor (TCR) ligation in the leukemic T cell line Jurkat. The SLP-76 locus has been localized to human chromosome 5q33 and the gene structure has been partially characterized in mice. The human and murine cDNAs both encode 533 amino acid proteins that are 72% identical and comprised of three modular domains. The NH2-terminus contains an acidic region that includes a PEST domain and several tyrosine residues which are phosphorylated following TCR ligation. SLP-76 also contains a central proline-rich domain and a COOH-terminal SH2 domain. A number of additional proteins have been identified that associate with SLP-76 both constitutively and inducibly following receptor ligation, supporting the notion that SLP-76 functions as an adaptor or scaffold protein. Studies using SLP-76 deficient T cdomain:The SH2 domain mediates interaction with SHB., function:Involved in T-cell antigen receptor mediated signaling., PTM:Phosphorylated after T-cell receptor activation by ZAP-70., similarity:Contains 1 SAM (sterile alpha motif) domain., similarity:Contains 1 SH2 domain., subunit:Interacts with SLA. Interacts with CBLB (By similarity) . Interacts with the adapter proteins GRB2 and FYB. Interacts with SHB. Interacts with PRAM1., tissue specificity:Highly expressed in spleen, thymus, and peripheral blood leukocytes. Highly expressed also in T-cell and monocytic cell lines, expressed at lower level in B-cell lines. Not detected in fibroblast or neuroblasatoma cell lines.