Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Weitere Synonyme anzeigen
Wählen Sie die gewünschte Spezies
Although binding of PTP1B increases with decrease in c-Met activation and acts as negative regulator of receptor, increased binding and phosphorylation of SHP-2 coincide with maximal stimulation of c-Met, acting as positive regulator.
Data indicate multiple protein tyrosine phosphatase 1B (PTP1B) structures in different conformational states.
Cav-2beta isoform yielded by alternative translation initiation desensitizes insulin receptor (IR) via dephosphorylation by PTP1B, and subsequent endocytosis and lysosomal degradation of IR, causing insulin resistance.
Data show that overexpression of protein-tyrosine phosphatase 1B (PTP1B) activated the c-Jun N-terminal kinase (JNK) signaling pathway.
High-Resolution PTP1B Inhibition Profiling Combined with HPLC-HRMS-SPE-NMR for Identification of PTP1B Inhibitors from Miconia albicans.
The expression of PTP1B in skeletal muscle was increased after caloric restriction and prolonged exercise.
preliminary data show that heterozygous or homozygous deletion of PTPN1 increases the severity of MPN in Jak2V617F-knock-in mice. Future studies will determine whether loss of PTPN1 cooperates with the JAK2V617F mutation in the pathogenesis of MPN
we demonstrated a novel oncogenic mechanism of PTP1B on affecting PITX1/p120RasGAP in colorectal carcinoma(CRC). Regorafenib inhibited CRC survival through reserving PTP1B-dependant PITX1/p120RasGAP downregulation. PTP1B may be a potential biomarker predicting regorafenib effectiveness, and a potential solution for CRC
this study highlights an important role for Nck1 in fine-tuning IRE1alpha expression and signaling that regulate PTP1B expression and subsequent activation of the PI3K-Akt pathway in HepG2 cells.
In conclusion, HDAC6 might enhance aggressive melanoma cells progression via interacting with PTPN1, which was independent of its histone modifying activity.
PTP1B is widely expressed in the human breast gland with highest expression in myoepithelial cells and fibroblasts. Inhibition of PTP1B in D492 and HMLE affects cell-cell adhesion and induces anoikis-like effects.
The results of the present study highlight the expression quantitative trait loci enrichment and pleiotropy in psoriasis and schizophrenia, and also suggest a possible key role of the PTPN1 gene in the etiology of psoriasis
The structural fragments which are important for PTP1B inhibition were identified by naive Bayesian method and can be further exploited to design new molecules around the identified scaffolds. The descriptive and predictive modeling strategy applied in this study is capable of identifying PTP1B inhibitors from the large compound libraries
The gained results are observed not only the unbinding mechanism of IRK-PTP1B complexes came from pulling force profile, number of hydrogen bonds, and interaction energy between IRK and PTP1Bs but also described PTP1B's point mutations could variably change its binding affinity towards IRK.
these results suggest that inhibition of PTP1B activity is a promising new target in the treatment of colorectal cancer and the prevention of metastasis
the molecular mechanisms by which PTP1B and TC-PTP loss co-operates with other genetic aberrations will need to be elucidated to design more effective therapeutic strategies.
Experimental results indicate that methylmercury inhibits the activity of protein tyrosine phosphatase 1B, which in turn activates the epidermal growth factor receptor-p38 mitogen-activated protein kinase pathway that induces cyclooxygenase-2 expression.
The findings show that reduced PTP1B responses contribute to disease symptoms in part by enhancing S100A9 expression during viral-associated chronic obstructive pulmonary disease exacerbations.
Both the rs2904268 C>G CG and GG genotype frequencies were markedly higher in the ESCC group relative to the control group (both p < 0.05). However, the genotype frequencies of rs2230605A>G and rs16995309 C>T were similar between the ESCC and control groups These results indicated that the PTPN1 gene polymorphism rs2904268 is associated with susceptibility to Esophageal Squamous Cell Carcinoma in Inner Mongolia.
Data suggest TrxR1 and NADPH directly protect PTP1B from inactivation by oxidation; this protection is independent of TRX1 and PRX2; this protection is blocked by auranofin (an inhibitor of TrxR1 and requires an intact selenocysteine residue in TrxR1. (TrxR1 = thioredoxin reductase 1; PTP1B = protein tyrosine phosphatase, non-receptor type 1; TRX1 = thioredoxin-1; PRX2 = paired related homeobox 2 protein)
Regulation of platelet-activating factor-mediated PTP1B activation by a Janus kinase 2/ calpain pathway has been reported.
PTP1B role in the mast cell activation and anaphylaxis.Sirt1 negatively regulates Fc epsilon RI-stimulated mast cell activation and anaphylaxis through two mutually regulated pathways involving AMP-activated protein kinase (AMPK) and protein tyrosine phosphatase 1B.
The present study shows that protein tyrosine phosphatase 1B inactivation in aged mice improves left ventricular systolic and diastolic function associated with reduced adverse cardiac remodeling (hypertrophy, fibrosis, and capillary rarefaction) and limits vascular endothelial dysfunction.
POMC-specific PTP1B deficiency improved glucose tolerance and attenuated diet-induced fatty liver only in male mice and attenuated weight gain in males and females.
Findings collectively suggested that PTP1B ablation protects against ER stress-induced cardiac anomalies through regulation of autophagy.
Activity of PTP1B specifically in myeloid lineage cells protects against atherosclerotic plaque formation, under atherogenic conditions, in an ApoE-/- mice.
A potent, selective, and orally bioavailable inhibitor of the protein-tyrosine phosphatase PTP1B improves insulin and leptin signaling in animal models.
PTP1B has a tumor suppressor function in myeloid lineage cells.PTP1B deficiency leads to shorter lifespan and the development of acute leukemia.
These results demonstrate a key role for PTP1B in the protection against the cytotoxicity of irradiation in intact animal and in macrophages, which might be therapeutically relevant.
PTP1B gene deletion significantly limited CLP-induced insulin resistance, improved AMP-activated protein kinase signaling pathway and Glucose Transporter 4 translocation, and decreased inflammation. These effects were associated with a reduction of sepsis-induced endothelial dysfunction/impaired NO production and especially of insulin-mediated dilatation.
Sleep fragmentation induces increased food intake, reduced leptin signaling in hypothalamus, systemic insulin resistance, and reduced visceral white adipose tissue insulin sensitivity and inflammation that are mediated by increased PTP-1B activity.
S-nitrosylation of endogenous SHP2 Phosphatase and PTP1B in endothelial insulin signaling has been demonstrated.
Under normoglycemia control and pod-PTP1B KO mice exhibited comparable renal functions. However, podocyte PTP1B disruption attenuated hyperglycemia-induced albuminuria and renal injury and preserved glucose control. Also, podocyte PTP1B disruption was accompanied with improved renal insulin signaling and enhanced autophagy with decreased inflammation and fibrosis.
Endothelial PTP1B deletion improves cardiac VEGF signalling and angiogenesis and protects against chronic afterload-induced heart failure.
PTP1B inhibitors protect against atherosclerotic plaque formation in the LDLR(-/-) mouse model of atherosclerosis.
The results suggest a deficiency of PTP1B improves hypothalamic insulin sensitivity resulting in the attenuation of AgRP mRNA expression under HFD conditions.
cadherin 2 (CDH2) and CDH4 cooperate to regulate radial migration in mouse brain via the protein tyrosine phosphatase 1B (PTP1B) and alpha- and beta-catenins.
this paper shows that PTP1B specifically regulates IgE-mediated STAT5 pathway, but is redundant in influencing mast cell function in vivo
PTP1B/RNF213/alpha-KGDD pathway is critical for survival of HER2(+) breast cancer, and possibly other malignancies, in the hypoxic tumour microenvironment
data for the first time demonstrate a calpain/PTP1B/VEGFR2 negative feedback loop in the regulation of VEGF-induced angiogenesis. Modulation of local PTP1B and/or calpain activities may prove beneficial in the treatment of impaired wound healing in diabetes.
PTP-1B increased posthypoxia by about 30% and persisted for 2 weeks while Src kinase inhibition attenuated the expected PTP-1B-increased expression.
The protein encoded by this gene is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP has been shown to act as a negative regulator of insulin signaling by dephosphorylating the phosphotryosine residues of insulin receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to interferon stimulation.
protein tyrosine phosphatase, non-receptor type 1
, tyrosine-protein phosphatase non-receptor type 1
, tyrosine-protein phosphatase non-receptor type 1-like
, protein tyrosine phosphatase, placental
, protein-tyrosine phosphatase 1B
, protein-protein-tyrosine phosphatase HA2
, protein-tyrosine phosphatase HA2
, protein tyrosine phosphatase 1b
, non-receptor protein tyrosine phosphatase
, phosphoprotein phosphatase
, tyrosine phosphatase 1B