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LCP2

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 cell lines or mice have provided strong evidence that SLP-76 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function.
Predicted location

Intracellular

Single cell type specificity

Cell type enhanced (Macrophages, Kupffer cells, granulocytes, T-cells, NK-cells)

Immune cell specificity

Low immune cell specificity

Cell line specificity

Cell line enhanced (HEL, HL-60, HMC-1, Karpas-707, MOLT-4, THP-1, U-937)

Interaction

Interacts with SLA. Interacts with CBLB (By similarity). Interacts with GRB2 (PubMed:7706237). Interacts with SHB (PubMed:12084069). Interacts with PRAM1 (PubMed:11301322). Interacts (via SH2 domain) with CD6 (via tyrosine phosphorylated C-terminus) (PubMed:16914752, 24584089). Interacts with FYB1 and the phosphorylated form of FYB2 (PubMed:27335501).

More Types Infomation

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For Research Use Only. Not For Clinical Use.

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