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Biochemical analyses revealed that mutant T cells were hypersensitive to TCR stimulation. Indeed, phosphorylation of several signaling proteins, including SLP76 itself, phospholipase Cgamma1 and the protein kinases AKT and ERK1/2, was increased
slp-76 contributes to the regulation of the tissue distribution, PLZF (show ZBTB16 Proteins), and cytokine expression of iNKT cells via ADAP (show APP Proteins)-dependent and -independent mechanisms.
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.
a previously unappreciated role for PLC-gamma1 (show PLCG1 Proteins) in the positive regulation of Zap-70 (show ZAP70 Proteins) and T-cell receptor tyrosine phosphorylation. Conversely, PLC-gamma1 (show PLCG1 Proteins) negatively regulated the phosphorylation of SLP-76-associated proteins, including previously established Lck (show LCK Proteins) substrate phosphorylation sites within this complex.
These data are consistent with a model in which bivalent recruitment of a GADS (show GRAP2 Proteins)/SLP-76 complex is required for costimulation by CD6 (show CD6 Proteins).
LAT (show ORC3 Proteins) and SLP-76 are randomly dispersed throughout the clusters that form upon T cell receptor engagement.
SLP76 is ectopically expressed in chronic lymphocytic leukemia cells where it plays a role in B-cell receptor 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
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