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anti-Mouse (Murine) LCP2 Antibodies:
anti-Rat (Rattus) LCP2 Antibodies:
anti-Human LCP2 Antibodies:
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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 - 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
Show all 3 Pubmed References
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
Show all 2 Pubmed References
Human Polyclonal LCP2 Primary Antibody for ELISA, WB - ABIN2476520
Ackermann: [Change and new knowledge in infectious diseases of the nervous system]. in Der Internist 1978
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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
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
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 Antibodies), and cytokine expression of iNKT cells via ADAP (show APP Antibodies)-dependent and -independent mechanisms.
findings identify ACK1 (show TNK2 Antibodies) as a novel SLP-76-associated protein-tyrosine kinase (show YES1 Antibodies) that modulates early activation events in T cells.
immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 (show RANGAP1 Antibodies) of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (show NFATC1 Antibodies) and NF-kappaB (show NFKB1 Antibodies) p65 (show NFkBP65 Antibodies) 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 Antibodies)-Lat (show LAT Antibodies)-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 Antibodies)/SKAP-HOM (show SKAP2 Antibodies) and SLP-76/Vav (show VAV1 Antibodies)/PLCgamma2 (show PLCG2 Antibodies) signaling hubs may be critical for Yersinia survival.
analysis of a costimulatory mechanism by which CXCL12 (show CXCL12 Antibodies) 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 Antibodies) and the IL-3 (show IL-3 Antibodies) receptor.
a previously unappreciated role for PLC-gamma1 (show PLCG1 Antibodies) in the positive regulation of Zap-70 (show ZAP70 Antibodies) and T-cell receptor tyrosine phosphorylation. Conversely, PLC-gamma1 (show PLCG1 Antibodies) negatively regulated the phosphorylation of SLP-76-associated proteins, including previously established Lck (show LCK Antibodies) substrate phosphorylation sites within this complex.
These data are consistent with a model in which bivalent recruitment of a GADS (show GRAP2 Antibodies)/SLP-76 complex is required for costimulation by CD6 (show CD6 Antibodies).
LAT (show ORC3 Antibodies) 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 Antibodies) as a novel SLP-76-associated protein-tyrosine kinase (show EPHA8 Antibodies) that modulates early activation events in T cells.
Data strongly suggest that chemokine (show CCL1 Antibodies)-stimulated associations between Vav1 (show VAV1 Antibodies), SLP-76, and ADAP (show FYB Antibodies) facilitate Rac1 (show RAC1 Antibodies) activation and alpha4beta1-mediated adhesion, whereas Pyk2 (show PTK2B Antibodies) opposes this adhesion by limiting Rac1 (show RAC1 Antibodies) activation.
TSAD (show SH2D2A Antibodies) binds to and co-localizes with Nck (show NCK1 Antibodies). Expression of TSAD (show SH2D2A Antibodies) increases both Nck (show NCK1 Antibodies)-Lck (show LCK Antibodies) and Nck (show NCK1 Antibodies)-SLP-76 interaction in T cells.
immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 (show RANGAP1 Antibodies) of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (show NFATC1 Antibodies) and NF-kappaB (show NFKB1 Antibodies) p65 (show GORASP1 Antibodies) 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