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anti-Human PTPN6 Antibodies:
anti-Mouse (Murine) PTPN6 Antibodies:
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Human Polyclonal PTPN6 Primary Antibody for IF, IHC (p) - ABIN1882123
Korporaal, Koekman, Verhoef, van der Wal, Bezemer, Van Eck, Akkerman: Downregulation of platelet responsiveness upon contact with LDL by the protein-tyrosine phosphatases SHP-1 and SHP-2. in Arteriosclerosis, thrombosis, and vascular biology 2009
Show all 2 Pubmed References
Human Polyclonal PTPN6 Primary Antibody for ICC, IF - ABIN4348608
McKenzie, Jones, Tosi, Caesar, Whittaker, Mitchell: Constitutive activation of STAT3 in Sézary syndrome is independent of SHP-1. in Leukemia 2012
Human Polyclonal PTPN6 Primary Antibody for IF (p) - ABIN879862
Lopes, Bálint, Valvo, Felce, Hessel, Dustin, Davis: Membrane nanoclusters of FcγRI segregate from inhibitory SIRPα upon activation of human macrophages. in The Journal of cell biology 2017
Human Polyclonal PTPN6 Primary Antibody for ELISA, WB - ABIN188850
Dubois, Bergeron, Kim, Dombrowski, Perreault, Fournès, Faure, Olivier, Beauchemin, Shulman, Siminovitch, Kim, Marette: The SHP-1 protein tyrosine phosphatase negatively modulates glucose homeostasis. in Nature medicine 2006
Human Polyclonal PTPN6 Primary Antibody for IF, IHC (p) - ABIN5586488
Sauer, Herbst, Diekmann, Rudd, Kardinal: SHP-1 Acts as a Key Regulator of Alloresponses by Modulating LFA-1-Mediated Adhesion in Primary Murine T Cells. in Molecular and cellular biology 2016
M. tuberculosis-initiated human mannose receptor signaling regulates macrophage recognition and vesicle trafficking by gamma Fc receptors, Grb2, and SHP-1.
Data suggest that SHP-1/p-STAT3 (show STAT3 Antibodies)/VEGF-A (show VEGFA Antibodies) axis is a potential therapeutic target for metastatic triple-negative breast cancer (TNBC).
these data highlight a signaling pathway in which SHP-1 acts through CrkII to reshape the pattern of Rap1 activation in the immunological synapse.
observations suggest that Chikungunya virus (CHIKV) has the ability to induce host PTPN6 expression, and induction of PTPN6 may favour the attenuation of the pro-inflammatory immune response of the host, which is otherwise detrimental for the survival of CHIKV and establishment of an infection
The results reveal that SHP1 is the long-sought phosphatase that can antagonize Helicobacter pylori CagA. Augmented Helicobacter pylori CagA activity, via SHP1 inhibition, might also contribute to the development of Epstein-Barr virus-positive gastric cancer.
Analyzed gene expression profiles of monocytes from symptomatic congestive heart failure patients; there is a down-regulation of the phosphatase SHP-1 which induces a significant activation of TAK-1 (show MAP3K7 Antibodies)/IKK (show CHUK Antibodies)/NF-kB signaling.
crocin induced the expression of SHP-1, a tyrosine protein phosphatase, and pervanadate treatment reversed the crocin-induced downregulation of STAT3 (show STAT3 Antibodies), suggesting the involvement of a protein tyrosine phosphatase (show ACP1 Antibodies).
this review focalizes upon the implication of SHP-1 in the pathogenesis of autoimmune disorders, and addresses developing therapeutic strategies targeting SHP-1
we demonstrated that SHP-1 dephosphorylates PKM2Y105 to inhibit the Warburg effect and nucleus-dependent cell proliferation, and the dephosphorylation of PKM2Y105 by SHP-1 determines the efficacy of targeted drugs for hepatocellular carcinoma treatment
These findings have provided first lines of evidences that PDZK1 expression is negatively correlated with SHP-1 activation and poor clinical outcomes in clear cell renal cell carcinoma (ccRCC) . PDZK1 was identified as a novel tumor suppressor in ccRCC by negating SHP-1 activity
Deletion of AT2 receptor (show AGTR2 Antibodies) reduced SHP-1 activity and restored VEGF (show VEGFA Antibodies) actions, leading to an increased blood flow reperfusion after ischemia in diabetes mellitus.
These findings show a novel role for Shp-1 in the regulation of IEC growth and secretory lineage allocation, possibly via modulation of PI3K/Akt (show AKT1 Antibodies)-dependent signaling pathways.
These findings suggest that protein tyrosine phosphatase SHP-1 may act as a positive regulator of osteoblast differentiation through direct association with and dephosphorylation of GSK3beta.
data establish SHP-1 as a critical player in setting the threshold downstream of TCR signaling and identify a novel function of SHP-1 as a regulator of T cell susceptibility to Treg-mediated suppression in vitro and in vivo
Results are consistent with predicted/observed reduction in the Lyn-SHIP-1-PTEN-SHP-1 axis function in B cells from systemic lupus
Our data show that SHP1 is required for the survival of mature thymocytes and the generation of the functional T-cell repertoire, as its absence leads to a reduction in the numbers of CD4 (show CD4 Antibodies)(+) and CD8 (show CD8A Antibodies)(+) naive T cells in the peripheral lymphoid compartments.
Our study suggests that metformin exerts its insulin sensitizing effects via inhibition of SHP-1 activity and expression.
we found that THEMIS directly regulated the catalytic activity of the tyrosine phosphatase SHP-1.
Studies indicate that SHP1 and SYK (show SYK Antibodies) crosstalk as a critical regulator of MyD88 (show MYD88 Antibodies) post-translational modifications and IL-1 (show IL1A Antibodies)-driven inflammation.
Our findings uncover an important role for PP6 as an indispensable guardian of genomic integrity of the lengthy prophase I oocyte arrest, maintenance of primordial follicle pool, and thus female fertility.
we present a new hyperinsulinemia animal model and propose ptpn6 as a key mediator triggering hyperinsulinemia-derived insulin (show INS Antibodies) resistance and immune suppression.
ptpn6 knockdown induces a spontaneous inflammation-associated phenotype at the late larval stage.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.
hematopoietic cell phosphatase
, hematopoietic cell protein-tyrosine phosphatase
, protein-tyrosine phosphatase 1C
, protein-tyrosine phosphatase SHP-1
, tyrosine-protein phosphatase non-receptor type 6
, dentatorubro-pallidoluysian atrophy protein
, non-receptor type protein tyrosine phosphatase SHP1
, hemopoietic cell phosphatase
, SH2 phosphatase 1
, protein tyrosine phosphatase, non-receptor type 6 L homeolog