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anti-Mouse (Murine) LCP2 Antibodies:
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Human Monoclonal LCP2 Primary Antibody for ICS - ABIN1177174
Fang, Motto, Ross, Koretzky: Tyrosines 113, 128, and 145 of SLP-76 are required for optimal augmentation of NFAT promoter activity. in Journal of immunology (Baltimore, Md. : 1950) 1996
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Human Monoclonal LCP2 Primary Antibody for IP, WB - ABIN2476521
Sarrafian: Fasciotomy of the foot: an anatomical study with special reference to release of the calcaneal compartment. in Foot & ankle 1990
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Human Monoclonal LCP2 Primary Antibody for ICS - ABIN1177173
Wu, Koretzky: The SLP-76 family of adapter proteins. in Seminars in immunology 2004
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Human Monoclonal LCP2 Primary Antibody for ICS - ABIN1176934
Bonilla, Fujita, Pivniouk, Chan, Geha: Adapter proteins SLP-76 and BLNK both are expressed by murine macrophages and are linked to signaling via Fcgamma receptors I and II/III. in Proceedings of the National Academy of Sciences of the United States of America 2000
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Human Polyclonal LCP2 Primary Antibody for ELISA, WB - ABIN250246
Jackman, Motto, Sun, Tanemoto, Turck, Peltz, Koretzky, Findell: Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells. in The Journal of biological chemistry 1995
Human Monoclonal LCP2 Primary Antibody for IHC (p), IHC - ABIN269168
Lin, Liu, Moore, Elizer, Veach, Hawiger, Ruley: Cutting edge: the "death" adaptor CRADD/RAIDD targets BCL10 and suppresses agonist-induced cytokine expression in T lymphocytes. in Journal of immunology (Baltimore, Md. : 1950) 2012
Human Polyclonal LCP2 Primary Antibody for IHC, ELISA - ABIN1532089
Tomomura, Hasegawa, Suda, Sakagami, Tomomura et al.: Serum calcium-decreasing factor, caldecrin, inhibits receptor activator of NF-?B ligand (RANKL)-mediated Ca2+ signaling and actin ring formation in mature osteoclasts via suppression of Src signaling ... in The Journal of biological chemistry 2012
Human Monoclonal LCP2 Primary Antibody for ICS - ABIN1176936
Bubeck Wardenburg, Fu, Jackman, Flotow, Wilkinson, Williams, Johnson, Kong, Chan, Findell: Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function. in The Journal of biological chemistry 1996
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, and cytokine expression of iNKT cells via ADAP-dependent and -independent mechanisms.
findings identify ACK1 as a novel SLP-76-associated protein-tyrosine kinase that modulates early activation events in T cells.
immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 and NF-kappaB p65 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-Lat-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/SKAP-HOM and SLP-76/Vav/PLCgamma2 signaling hubs may be critical for Yersinia survival.
analysis of a costimulatory mechanism by which CXCL12 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 and the IL-3 receptor.
These findings reveal a novel role for SLP-76 in CXCR4-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+ memory pool, suggesting that homeostatic turnover is not required for persistence of this population.
SLP-76 and ADAP are involved in E-selectin-mediated integrin activation and neutrophil recruitment to inflamed kidneys, which may underlie the development of life-threatening ischemia-reperfusion-induced acute kidney injury in humans.
Data show that development of the CD8+ ILLs present in SH2 domain-containing leukocyte protein, 76-kDa Y145F mice require Eomes and PLZF.
Loss of Lcp2 leads to loss of tonic T-cell receptor signals altering the rate of memory versus effector cell differentiation independent of initial T-cell expansion.
Loss of Lcp2 leads to loss of tonic T-cell receptor signals altering the generation but not the persistence of CD8+ memory T cells.
HPK1 competes with ADAP for SLP-76 binding and via Rap1 negatively affects T-cell adhesion.
While SLP-76 and LAT1 depend on each other for many of their functions, LAT2/SLP-76 interactions and SLP-76-independent LAT1 functions also mediate a positive signaling pathway downstream of FcepsilonRI in mast cells.
A nonhemostatic pathway in which platelet CLEC-2 receptors bind lymphatic endothelial PDPN and activate SLP-76 signaling to regulate embryonic vascular development.
a previously unappreciated role for PLC-gamma1 in the positive regulation of Zap-70 and T-cell receptor tyrosine phosphorylation. Conversely, PLC-gamma1 negatively regulated the phosphorylation of SLP-76-associated proteins, including previously established Lck substrate phosphorylation sites within this complex.
These data are consistent with a model in which bivalent recruitment of a GADS/SLP-76 complex is required for costimulation by CD6.
LAT 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.
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 and Nck-SLP-76 interaction 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 facilitates the assembly of SLP-76 microclusters.
Data indicate a role for the SAM domain in mediating SLP-76 self-association for T-cell function.
Data indicate that the intracellular signaling of ITK-SYK requires both SLP-76 and the adapter function of SYK/ZAP-70 kinases.
Unique modes of regulation of positive and negative feedback pathways in T cells by SLP-76.
Complementary phosphorylation sites in the adaptor protein SLP-76 promote synergistic activation of natural killer cells.
Nef employs a dual mechanism to disturb early TCR signaling by limiting the communication between LAT and SLP-76
both T cell activation and the association between SLP-76 and Nck. After T cell receptor stimulation, SLP-76 was phosphorylated, which enabled the binding of Nck.
our studies demonstrate a novel role for the adaptor molecule SLP-76 in regulating HIV-1 infection in T cells
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