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SHP (show LAMC1 Proteins) 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 Proteins)-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
human microbiota was able to reduce the levels of tauro-beta-muricholic acid and induce expression of FXR (show NR1H4 Proteins) target genes Fgf15 and Shp (show LAMC1 Proteins) in ileum after long-term colonization. We show that a human microbiota can change BA composition and induce FXR (show NR1H4 Proteins) signaling in colonized mice, but the levels of secondary BAs produced are lower than in mice colonized with a mouse microbiota
SHP (show LAMC1 Proteins) and REV-ERBalpha (show NR1D1 Proteins) play a critical role in controlling rhythmic CHOP (show DDIT3 Proteins) 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 Proteins) upregulation upon high-fat feeding leads to lipid accumulation, insulin (show INS Proteins) 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 Proteins)(+) and CD8 (show CD8A Proteins)(+) 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.
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 Proteins)/Akt (show AKT1 Proteins)-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 Proteins) and regulated by histone acetylation
The Shp1 functions as a positive regulator and acts in a novel mechanism through promoting EGFR (show EGFR Proteins) protein expression in human epithelial cells.
SHP1 DNA methylation (show HELLS Proteins) 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 Proteins) and SOCS-1 (show SOCS1 Proteins) gene expression in patient plasma cells supports the constitutive activation of the JAK (show JAK3 Proteins)/STAT3 (show STAT3 Proteins) 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 Proteins) resistance, podocyte dysfunction, and DN.
Low SHP1 expression is associated with primary central nervous system lymphoma.
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