Product Details
| Alternative Name: | Dual specificity protein phosphatase 3, DUSP3 |
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| MW: | 20.4 kDa |
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| Source: | Produced in E. coli. |
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| UniProt ID: | P51452 |
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| Formulation: | Liquid. In 50mM citrate, pH 6.0, containing 0.1M sodium chloride, 1mM EDTA and 1mM DTT. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Specific Activity: | 11U/mg. One unit will hydrolyze 1µmol p-nitrophenyl phosphate (pNPP) per minute at pH 6.0 and 30°C. Reaction conditions are 50mM citrate, pH 6.0, 0.1M NaCl, 1mM EDTA and 1mM DTT, 10mM pNPP substrate. An increase in signal of 3 to 4 fold can be achieved by addition of base to a pH of approximately 9.0 at the end of an assay with pNPP. |
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| Application Notes: | Useful for the study of VHR dual phosphatase kinetics and substrate specificity, and to dephosphorylate pSer/Thr and pTyr phosphorylated protein substrates. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Handling: | Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. |
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| Scientific Background: | Dual specificity phosphatases (DUSPs) are members of the superfamily of protein tyrosine phosphatases. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. |
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| Regulatory Status: | RUO - Research Use Only |
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SDS-PAGE Analysis: Lane 1: MW Marker, Lane 2: 1 µg, Lane 3: 2 µg VHR dual-specificity phosphatase
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Product Literature References
Protein tyrosine phosphatase 1B inhibitory properties of seco-cucurbitane triterpenes obtained from fruiting bodies of Russula lepida: W. Maarisit, et al.; J. Nat. Med.
71, 334 (2017),
Abstract;
Identification and evaluation of magnolol and chrysophanol as the principle protein tyrosine phosphatase-1B inhibitory compounds in a Kampo medicine, Masiningan: T. Onoda, et al.; J. Ethnopharmacol.
186, 84 (2016),
Application(s): PTP assay,
Abstract;
General Literature References
Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway: J.L. Todd, et al.; J Biol. Chem.
274, 13271 (1999),
Abstract;
The purification and characterization of a human dual-specific protein tyrosine phosphatase: J.M Denu, et al.; J Biol. Chem.
270, 3796 (1995),
Abstract;
Transition state and rate-limiting step of the reaction catalyzed by the human dual-specificity phosphatase, VHR: Z.Y., Zhang, et al.; Biochem.
34, 16088 (1995),
Abstract;
The catalytic role of Cys124 in the dual specificity phosphatase VHR: G. Zhou et al.; J Biol. Chem.
269, 28084 (1994),
Abstract;
