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immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 (show RANGAP1 ELISA Kits) of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (show NFATC1 ELISA Kits) and NF-kappaB (show NFKB1 ELISA Kits) p65 (show NFkBP65 ELISA Kits) nuclear entry in T cells
these studies establish Slp-76 as a critical determinant of NK-cell development and NK cell mediated elimination of missing-self target cells in mice
Data show that a splice variant of SLP-76 signal transducing adaptor protein (SLP-76 or Lcp2) reduced the amount of SLP-76 protein by ~90%, disrupting immunogenic and tolerogenic pathways to different degrees.
this analysis identified 65 proteins not associated before with the Zap70 (show ZAP70 ELISA Kits)-Lat (show LAT ELISA Kits)-SLP-76 network and thus should provide cues for future functional experiments.
A yopH mutant survived better in the absence of neutrophils, indicating that neutrophil inactivation by YopH by targeting PRAM-1 (show PRAM1 ELISA Kits)/SKAP-HOM (show SKAP2 ELISA Kits) and SLP-76/Vav (show VAV1 ELISA Kits)/PLCgamma2 (show PLCG2 ELISA Kits) signaling hubs may be critical for Yersinia survival.
analysis of a costimulatory mechanism by which CXCL12 (show CXCL12 ELISA Kits) and antigen converge at SLP-76 microcluster formation to enhance T cell responses
Findings indicate that SLP-76 is an essential signaling component for basophil activation downstream of both FcepsilonRI (show FCER1A ELISA Kits) and the IL-3 (show Il3 ELISA Kits) receptor.
These findings reveal a novel role for SLP-76 in CXCR4 (show CXCR4 ELISA Kits)-mediated T lymphocyte trafficking.
a novel regulation mechanism of SLP-76 by ubiquitination and proteasomal degradation of activated SLP-76, which is mediated by Ser-376 phosphorylation, leading to down-regulation of TCR signaling.
Loss of SLP-76 has no effect on persistence of the antigen-specific CD4 (show CD4 ELISA Kits)+ memory pool, suggesting that homeostatic turnover is not required for persistence of this population.
Data strongly suggest that chemokine-stimulated associations between Vav1, SLP-76, and ADAP facilitate Rac1 activation and alpha4beta1-mediated adhesion, whereas Pyk2 opposes this adhesion by limiting Rac1 activation.
TSAD binds to and co-localizes with Nck. Expression of TSAD increases both Nck-Lck (show LCK ELISA Kits) and Nck-SLP-76 interaction in T cells.
immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 (show RANGAP1 ELISA Kits) of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (show NFATC1 ELISA Kits) and NF-kappaB (show NFKB1 ELISA Kits) p65 (show GORASP1 ELISA Kits) nuclear entry in T cells
SLP-76 N-terminal tyrosine residues regulate a dynamic signaling equilibrium involving feedback of proximal T-cell receptor signaling
Multipoint binding of SLP-76 to ADAP (show FYB ELISA Kits) facilitates the assembly of SLP-76 microclusters.
Data indicate a role for the SAM (show TTN ELISA Kits) domain in mediating SLP-76 self-association for T-cell function.
Data indicate that the intracellular signaling of ITK (show ITK ELISA Kits)-SYK (show SYK ELISA Kits) requires both SLP-76 and the adapter function of SYK (show SYK ELISA Kits)/ZAP-70 (show ZAP70 ELISA Kits) kinases.
Unique modes of regulation of positive and negative feedback pathways in T cells by SLP-76.
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.
SH2 domain-containing leukocyte protein of 76 kDa
, SLP-76 tyrosine phosphoprotein
, lymphocyte cytosolic protein 2 (SH2 domain-containing leukocyte protein of 76kD)
, 76 kDa tyrosine phosphoprotein
, SH2 domain-containing leukocyte protein of 76kD
, lymphocyte cytosolic protein 2
, tyrosine phosphoprotein slp-76