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anti-Human PTPN6 Antikörper:
anti-Mouse (Murine) PTPN6 Antikörper:
anti-Rat (Rattus) PTPN6 Antikörper:
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Human Polyclonal PTPN6 Primary Antibody für 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 für 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
Human Polyclonal PTPN6 Primary Antibody für 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 für 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 für ICC, IF - ABIN4348608
McKenzie, Jones, Tosi, Caesar, Whittaker, Mitchell: Constitutive activation of STAT3 in Sézary syndrome is independent of SHP-1. in Leukemia 2012
This study demonstrates that VB inhibits glioblastoma cell proliferation, migration, and invasion while promoting apoptosis via SHP-1 activation and inhibition of STAT3 (zeige STAT3 Antikörper) phosphorylation.
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 (zeige STAT3 Antikörper)/VEGF-A (zeige VEGFA Antikörper) 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 (zeige MAP3K7 Antikörper)/IKK (zeige CHUK Antikörper)/NF-kB signaling.
crocin induced the expression of SHP-1, a tyrosine protein phosphatase, and pervanadate treatment reversed the crocin-induced downregulation of STAT3 (zeige STAT3 Antikörper), suggesting the involvement of a protein tyrosine phosphatase (zeige ACP1 Antikörper).
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
Deletion of AT2 receptor (zeige AGTR2 Antikörper) reduced SHP-1 activity and restored VEGF (zeige VEGFA Antikörper) 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 (zeige AKT1 Antikörper)-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 (zeige CD4 Antikörper)(+) and CD8 (zeige CD8A Antikörper)(+) 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 (zeige SYK Antikörper) crosstalk as a critical regulator of MyD88 (zeige MYD88 Antikörper) post-translational modifications and IL-1 (zeige IL1A Antikörper)-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 (zeige INS Antikörper) 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