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anti-Mouse (Murine) PTPN6 Antibodies:
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Dog (Canine) Monoclonal PTPN6 Primary Antibody for IF, IP - ABIN967766
Duchene, Schanstra, Pecher, Pizard, Susini, Esteve, Bascands, Girolami: A novel protein-protein interaction between a G protein-coupled receptor and the phosphatase SHP-2 is involved in bradykinin-induced inhibition of cell proliferation. in The Journal of biological chemistry 2002
Show all 5 Pubmed References
Dog (Canine) Monoclonal PTPN6 Primary Antibody for IF, IP - ABIN967767
Keilhack, Müller, Böhmer, Frank, Weidner, Birchmeier, Ligensa, Berndt, Kosmehl, Günther, Müller, Birchmeier, Böhmer: Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1. in The Journal of cell biology 2001
Show all 5 Pubmed References
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 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 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 ICC, IF - ABIN4348608
McKenzie, Jones, Tosi, Caesar, Whittaker, Mitchell: Constitutive activation of STAT3 in Sézary syndrome is independent of SHP-1. in Leukemia 2012
SHP (show LAMC1 Antibodies) deficiency protects myocardia from lipid accumulation in high fat diet-fed mice.
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 (show GSK3b Antibodies).
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
human microbiota was able to reduce the levels of tauro-beta-muricholic acid and induce expression of FXR (show NR1H4 Antibodies) target genes Fgf15 and Shp (show LAMC1 Antibodies) in ileum after long-term colonization. We show that a human microbiota can change BA composition and induce FXR (show NR1H4 Antibodies) signaling in colonized mice, but the levels of secondary BAs produced are lower than in mice colonized with a mouse microbiota
SHP (show LAMC1 Antibodies) and REV-ERBalpha (show NR1D1 Antibodies) play a critical role in controlling rhythmic CHOP (show DDIT3 Antibodies) expression in alcoholic fatty liver
Results are consistent with predicted/observed reduction in the Lyn-SHIP-1-PTEN-SHP-1 axis function in B cells from systemic lupus
our results suggest that SHP (show LAMC1 Antibodies) upregulation upon high-fat feeding leads to lipid accumulation, insulin (show INS Antibodies) resistance and inflammation in cardiomyocytes.
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.
luteolin inhibited STAT3 activation through disrupting the binding of HSP-90 to STAT3, which promoted its interaction to SHP-1.
These findings show a novel role for Shp-1 in the regulation of IEC growth and secretory lineage allocation, possibly via modulation of PI3K (show PIK3CA Antibodies)/Akt (show AKT1 Antibodies)-dependent signaling pathways.
the role of Shp1 in myeloid cells and how its dysregulation affects immune function, which can impact human disease.
PTPN6 is associated with progression of chronic myeloid leukaemia. Low expression level of PTPN6 was associated with DNA methylation (show HELLS Antibodies) and regulated by histone acetylation
The Shp1 functions as a positive regulator and acts in a novel mechanism through promoting EGFR (show EGFR Antibodies) protein expression in human epithelial cells.
SHP1 DNA methylation (show HELLS Antibodies) in in patients with B cell non-Hodgkin lymphoma
these results indicate that DNMT1 mediates aberrant methylation and silencing of SHP-1 gene in chronic myelogenous leukemia cells
Results provide evidence that repression of SHP-1, SHP-2 (show PTPN11 Antibodies) and SOCS-1 (show SOCS1 Antibodies) gene expression in patient plasma cells supports the constitutive activation of the JAK (show JAK3 Antibodies)/STAT3 (show STAT3 Antibodies) pathway and probably leads to higher degrees of bone marrow invasion.
we found that THEMIS directly regulated the catalytic activity of the tyrosine phosphatase SHP-1.
Hyperglycemia induces SHP-1 promoter epigenetic modifications, causing its persistent expression and activity and leading to insulin (show INS Antibodies) resistance, podocyte dysfunction, and DN.
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.
nuclear receptor subfamily 0 group B member 2
, orphan nuclear receptor SHP
, small heterodimer partner
, hematopoietic cell phosphatase
, hematopoietic cell protein-tyrosine phosphatase
, protein-tyrosine phosphatase 1C
, protein-tyrosine phosphatase SHP-1
, tyrosine-protein phosphatase non-receptor type 6
, hemopoietic cell phosphatase
, SH2 phosphatase 1
, dentatorubro-pallidoluysian atrophy protein
, non-receptor type protein tyrosine phosphatase SHP1