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Validated All-in-One™ qPCR Primer for PTPN1(NM_002827.3) Search again
Product ID:
HQP015828
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
PTP1B
Gene Description:
protein tyrosine phosphatase non-receptor type 1
Target Gene Accession:
NM_002827.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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.
Gene References into function
- Moderate overabundance of PTP-1B in liver tissue does not alter insulin action on glucose metabolism, and the site of action of PTP-1B is presumably at insulin-responsive target tissue or tissues other than the liver.
- variation in 3' UTR of hPTP1B increases specific gene expression and associates with insulin resistance
- PTP1B reduces the level of gene expression of SOCS3 and other leptin-regulated genes, and conversely, the expression of genes down-regulated by leptin was enhanced by PTP1B over-expression
- Data show that an increase in soluble protein-tyrosine phosphatase 1B activity contributes to the anti-migratory, but not anti-mitogenic, actions of human Sprouty 2.
- PTP1B inhibitory agents can be acquired by targeting the area defined by residues Lys-41, Arg-47, and Asp-48, in addition to the previously identified second aryl phosphate-binding pocket.
- Data show that Y box-binding protein-1 (YB-1) is a regulator of protein tyrosine phosphatase 1B (PTP1B) expression, and highlight PTP1B as a critical regulator of insulin- and cytokine-mediated signal transduction.
- PTP1B inhibition by S-nitrosylation is caused by formation of a mixed disulfide
- dynamics of the interaction between the insulin receptor and this protein in living cells
- PTP1B plays an important role in the integrin-mediated dephosphorylation of LAT in human platelets and is involved in the control of irreversible aggregation upon FcgammaRIIa stimulation
- mutation of pro387leu in PTP-1B was not associated with type 2 diabetes in Chinese
- PTP-1B appears not only to interact with and dephosphorylate the insulin-stimulated insulin receptor in a perinuclear endosome compartment but is also involved in maintaining the IR in a dephosphorylated state during its biosynthesis
- PTP1B has a role as a negative regulator of IR activation in hepatocytes
- PTP1B has a role in insulin resistance
- analysis the relative abundance of PTP1B in RBCs of different age indicated that the PTP activity undergoes oxidative inactivation that can be further differentiated into reversible and irreversible components
- Neither of the HSD3B1 or PTP1B variants were associated with hypertension
- PTP1B single nucleotide polymorphisms may interact with environmental factors to induce more severe phenotypes in morbidly obese subjects.
- protein tyrosine phosphatase 1B can be allosterically inhibited
- PTPN1 is a significant contributor to type 2 diabetes susceptibility in the Caucasian population.
- significant association with metabolic traits consistent with the proposed in vivo role for the PTP-1B protein.
- Our results provided evidence that upregulation of insulin signaling by reducing PTP1B liver with RNAi can be a potent diabetes treatment method.
- protein-tyrosine phosphatase 1B has a role in integrin signaling
- PTP1B interacts with TRPV6 in vivo and plays a role in TRPV6-mediated calcium influx in HEK293 cells
- The association of common single nucleotide polymorphisms (SNPs) and haplotypes in PTPN1 with type 2 diabetes, fasting plasma glucose, and insulin sensitivity in a large collection of subjects is reported.
- protein tyrosine phosphatase 1B (PTPN1) IVS6+G82G homozygotes showed higher levels of all measures of adiposity and G82 allele heterozygotes are potentially at higher risk for type 2 diabetes
- PTP1B was inhibited by cytochrome c and microperoxidase; a variety of redox-active metabolites and hemes can oxidatively inactivate PTPs with potentially profound implications for signal transduction
- Data show that protein-tyrosine phosphatase (PTP)-1B is an essential positive regulator of the initiation of outside-in alphaIIbbeta3 integrin signaling in platelets.
- The association between 6 single nucleotide polymorphisms and their effect on leptin, body fat, insulin sensitivity, and metabolic syndrome in female twins is reported.
- Catalytic activity of PTP1B is controlled by cell adhesion.
- PTP-1B/inhibitor complexes show a conformation-assisted inhibition mechanism as the basis for inhibitor selectivity
- PTP1B mediates of RhoA-dependent phosphorylation of p130Cas.
- findings suggest that protein tyrosine phosphatase 1B(PTP1B) plays an important role in neuroendocrine differentiation, and therefore, may possibly be involved in the progression of prostate cancer
- PTPN1 variants may modulate the lipid profile, thereby influencing susceptibility to metabolic disease
- molecular dynamics study of WPD loop movement in PTP1B
- Noonan syndrome affected individuals show heterozygous PTPN11 mutations
- PTPase activities of PTP1B or CD45 were abolished by low concentrations of (1)O(2)
- Direct interaction between ER membrane-bound PTP1B and its plasma membrane-anchored targets was demonstrated.
- C-terminal domain of protein tyrosine phosphatase-1B shows an improvement in affinity but may also provide for specificity over other phosphatases. [protein tyrosine phosphatase-1B]
- The significance of exercise-induced alterations in cytosolic SHP2 and insulin-stimulated Akt pSer(473) on the improvement in insulin sensitivity requires further elucidation.
- Single nucleotide polymorphisms are unlikely to have a major role in the aetiology of type 2 diabetes or obesity in Pima Indians.
- protein-tyrosine phosphatase 1B governs differential recruitment of signaling pathways involved in EGFR regulation of epithelial ion transport.
- case-control study in a Polish population did not confirm the reported association between polymorphisms in PTPN1 and Type 2 diabetes
- Data suggest that glucose enhances protein tyrosine phosphatase 1B transcription through Sp1 activation by protein kinase C.
- Our results from a sample of Iranian type 2 diabetes cases and controls provide evidence that the 1484insG genotype of the PTPN1 gene may be associated with insulin resistance and other cardiovascular risk factors in non-diabetic male subjects.
- The PTPN1 promoter variants -1023C>A and -51delA (which appears to be functional) were not associated with T2D or related traits in this study
- Data for PTP1B are consistent with a concept that explains the ER membrane anchor of tail-anchored proteins as a physicochemical structure.
- This study suggests that (a) PTP1B can act as an important activator of Src in colon cancer cells via dephosphorylation at Y530 of Src and (b) elevated levels of PTP1B can increase tumorigenicity of colon cancer cells by activating Src.
- It may be possible to increase proliferative activity of human corneal endothelial cells, particularly in cells from older donors, by inhibiting the activity of this important protein tyrosine phosphatase.
- Collectively, our experiments implicate a novel signaling pathway involving calpain 2, PTP1B, and Src in the regulation of invadopodia and breast cancer invasion.
- PTP1B regulates cortactin tyrosine phosphorylation by targeting Tyr446
- PTP1B is a physiological negative regulator of TLR signaling via suppression of both MyD88- and TRIF-dependent production of proinflammatory cytokine and IFN-beta in macrophages.
- IL-4 induces PTP1B mRNA expression in a phosphatidylinositol 3-kinase-dependent manner and enhances PTP1B protein stability to suppress IL-4-induced STAT6 signaling.
- PTP1B and TCPTP play distinct and non-redundant roles in the regulation of the Met receptor-tyrosine kinase
- Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation
- PTPIP51 and PTP1B, play a role in differentiation and apoptosis of the cytotrophoblast and syncytiotrophoblast, respectively.
- data indicate inactivation of receptor-associated protein tyrosine phosphatase activity by cytokine-generated reactive oxygen species is a physiologic mechanism for amplification of IL-4 receptor activation revealing a role for ROS in cytokine crosstalk
- PTP-1B constitutes a key divergent element between leptin/insulin and CNTF signaling pathways at the neuronal level.