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The findings show that reduced PTP1B responses contribute to disease symptoms in part by enhancing S100A9 (zeige S100A9 Proteine) 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 (zeige TXNRD1 Proteine) and NADPH (zeige NQO1 Proteine) directly protect PTP1B from inactivation by oxidation; this protection is independent of TRX1 (zeige MLL Proteine) and PRX2 (zeige PRDX2 Proteine); this protection is blocked by auranofin (an inhibitor of TrxR1 (zeige TXNRD1 Proteine) and requires an intact selenocysteine residue in TrxR1 (zeige TXNRD1 Proteine). (TrxR1 (zeige TXNRD1 Proteine) = thioredoxin reductase 1 (zeige TXNRD1 Proteine); PTP1B = protein tyrosine phosphatase (zeige ACP1 Proteine), non-receptor type 1; TRX1 (zeige MLL Proteine) = thioredoxin-1; PRX2 (zeige PRDX2 Proteine) = paired related homeobox 2 (zeige PRRX2 Proteine) protein)
Regulation of platelet-activating factor-mediated PTP1B activation by a Janus kinase 2/ calpain pathway has been reported.
PTP1B was overexpressed in over 70% of breast cancer tissues, correlating with patients with estrogen receptor (ER (zeige ESR1 Proteine))-negative, progesterone receptor (PR (zeige PGR Proteine))-negative, and human epidermal growth factor receptor (zeige EGFR Proteine) 2 (HER2 (zeige ERBB2 Proteine))-positive tumors. The data also showed that both tumor size and lymph node metastasis were significantly higher in patients with a higher level of PTP1B.
PTP1B uses conformational and dynamic allostery to regulate its activity. Both conformational rigidity and dynamics are essential for controlling protein activity.
PTP1BDelta6 is a positive regulator of JAK (zeige JAK3 Proteine)/STAT (zeige STAT1 Proteine) signaling in classical Hodgkin lymphoma cells.(
In PTP1B and VHR (zeige DUSP3 Proteine), two new allosteric clusters were identified in each enzyme.
PTP1B/RNF213 (zeige RNF213 Proteine)/alpha-KGDD pathway is critical for survival of HER2 (zeige ERBB2 Proteine)(+) 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.
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 (zeige INS Proteine) 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 (zeige LDLR Proteine)(-/-) mouse model of atherosclerosis.
The results suggest a deficiency of PTP1B improves hypothalamic insulin (zeige INS Proteine) sensitivity resulting in the attenuation of AgRP (zeige AGRP Proteine) mRNA expression under HFD conditions.
cadherin 2 (CDH2 (zeige CDH2 Proteine)) and CDH4 (zeige CDH4 Proteine) 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 (zeige STAT5A Proteine) pathway, but is redundant in influencing mast cell function in vivo
These findings reveal a novel role for pancreatic PTP1B in cerulein- and arginine-induced acute pancreatitis.
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