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VHR dual specificity phosphatase (human), (recombinant)

 
BML-SE333-0050 50 µg 299.00 USD
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Product Specification

Alternative Name:Dual specificity protein phosphatase 3, DUSP3
 
MW:20.4 kDa
 
Source:Produced in E. coli.
 
UniProt ID:P51452
 
Formulation:Liquid. In 50mM citrate, pH 6.0, containing 0.1M sodium chloride, 1mM EDTA and 1mM DTT.
 
Purity:≥95% (SDS-PAGE)
 
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.
 
Application Notes:Useful for the study of VHR dual phosphatase kinetics and substrate specificity, and to dephosphorylate pSer/Thr and pTyr phosphorylated protein substrates.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
 
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.
 
BML-SE333 SDS-PAGE
SDS-PAGE Analysis: Lane 1: MW Marker, Lane 2: 1 µg, Lane 3: 2 µg VHR dual-specificity phosphatase
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BML-SE333 SDS-PAGE

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;

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For Research Use Only. Not for use in diagnostic procedures.
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