human LCP2 shRNA silencing AAV

76 kDa tyrosine phosphoprotein; lymphocyte cytosolic protein 2; SH2 domain-containing leukocyte protein of 76 kDa; SLP76; SLP-76; SLP-76 tyrosine phosphoprotein

Lymphocyte cytosolic protein 2 (LCP2) 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. LCP2 also contains a central proline-rich domain and a COOH-terminal SH2 domain. A number of additional proteins have been identified that associate with LCP2 both constitutively and inducibly following receptor ligation, supporting the notion that LCP2 functions as an adaptor or scaffold protein. Studies using SLP-76 deficient T cell lines or mice have provided strong evidence that LCP2 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function [taken from NCBI Entrez Gene (Gene ID: 3937)].

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.

3937

lymphocyte cytosolic protein 2

lymphocyte cytosolic protein 2

LCP2

HGNC:6529

9606.0

1602

1602 bp

Lymphocyte cytosolic protein 2

NM_005565

NM_005565, BC016618,

B-cell Receptor Signaling,Fc Receptor Signaling,Immunology,Innate Immunity,Signal Transduction,T-cell Receptor Signaling

signal_transduction,immunology,signal_transduction

human

Lymphocyte cytosolic protein 2 (LCP2) 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. LCP2 also contains a central proline-rich domain and a COOH-terminal SH2 domain. A number of additional proteins have been identified that associate with LCP2 both constitutively and inducibly following receptor ligation, supporting the notion that LCP2 functions as an adaptor or scaffold protein. Studies using SLP-76 deficient T cell lines or mice have provided strong evidence that LCP2 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function [taken from NCBI Entrez Gene (Gene ID: 3937)].

Hs.304475

Q13094