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Background: DUSP3 belongs to the dual specificity protein phosphatase subfamily which inactivates their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. DUSP3 negatively regulate members of the mitogen-activated protein kinase superfamily that are related to cellular proliferation and differentiation. DUSP3 is expressed in both breast and ovarian tissues and displays activity both for tyrosine-protein phosphate and serine-protein phosphate, but exhibits a strong preference toward phosphotyrosines, specifically dephosphorylates and inactivates ERK1 and ERK2. In vitro studies showed that DUSP3 is a negative regulator of ERK and JNK pathways in several cell lines. On the other hand, DUSP3 is implicated in human cancer. It has been alternatively described as having tumor suppressive and oncogenic properties.
Dual specificity phosphatise 3 (DUSP3) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (1-185) and having a molecular mass of 22.6 kDa.
DUSP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Protein Quality:
Protein concentration (Bradford with BSA as standard) 1.0 mg/ml
Purity > 95% by SDS PAGE
Form liquid
Specific activity >1,750 units/mg*
Storage buffer: 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 10% glycerol.
* Enzymatic activity was confirmed by measuring the amount of enzyme hydrolyzing 1 nmole of p-nitrophenyl phosphate (pNPP) per minute at 37C, pH7.5 using 10mM of substrate.
Ordering information: shipped on dry ice
Ishibashi T., Bottaro D.P., Chan A., Miki T., Aaronson S.A.(1992) "Expression cloning of a human dual-specificity phosphatase." Proc. Natl. Acad. Sci. U.S.A. 89:12170-12174
Todd J.L., Tanner K.G., Denu J.M.(1999) "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. Biol. Chem. 274:13271-13280
Schumacher M.A., Todd J.L., Rice A.E., Tanner K.G., Denu J.M.(2002) "Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase." Biochemistry 41:3009-3017
Pavic K1, Duan G1, Köhn M1.(2015) ”VHR/DUSP3 phosphatase: structure, function and regulation.” FEBS J. 2015 May;282(10):1871-90.
Amand M, Erpicum C, Bajou K, Cerignoli F, Blacher S, Martin M, Dequiedt F, Drion P, Singh P, Zurashvili T, Vandereyken M, Musumeci L, Mustelin T, Moutschen M, Gilles C, Noel A, Rahmouni S1. (2014) “DUSP3/VHR is a pro-angiogenic atypical dual-specificity phosphatase.” Mol Cancer. 2014 May 15;13:108.
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