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findings identify ACK1 (show TNK2 Proteins) as a novel SLP-76-associated protein-tyrosine kinase (show YES1 Proteins) that modulates early activation events in T cells.
immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 (show RANGAP1 Proteins) of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (show NFATC1 Proteins) and NF-kappaB (show NFKB1 Proteins) p65 (show NFkBP65 Proteins) 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 Proteins)-Lat (show LAT Proteins)-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 Proteins)/SKAP-HOM (show SKAP2 Proteins) and SLP-76/Vav (show VAV1 Proteins)/PLCgamma2 (show PLCG2 Proteins) signaling hubs may be critical for Yersinia survival.
analysis of a costimulatory mechanism by which CXCL12 (show CXCL12 Proteins) 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 Proteins) and the IL-3 (show IL-3 Proteins) receptor.
These findings reveal a novel role for SLP-76 in CXCR4 (show CXCR4 Proteins)-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.
findings identify ACK1 (show TNK2 Proteins) as a novel SLP-76-associated protein-tyrosine kinase (show EPHA8 Proteins) that modulates early activation events in T cells.
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 (show SH2D2A Proteins) binds to and co-localizes with Nck (show NCK1 Proteins). Expression of TSAD (show SH2D2A Proteins) increases both Nck (show NCK1 Proteins)-Lck (show LCK Proteins) and Nck (show NCK1 Proteins)-SLP-76 interaction in T cells.
immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 (show RANGAP1 Proteins) of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (show NFATC1 Proteins) and NF-kappaB (show NFKB1 Proteins) p65 (show GORASP1 Proteins) 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 Proteins) facilitates the assembly of SLP-76 microclusters.
Data indicate a role for the SAM (show TTN Proteins) domain in mediating SLP-76 self-association for T-cell function.
Data indicate that the intracellular signaling of ITK (show ITK Proteins)-SYK (show SYK Proteins) requires both SLP-76 and the adapter function of SYK (show SYK Proteins)/ZAP-70 (show ZAP70 Proteins) 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