|Other Names||Dual specificity protein phosphatase 5, Dual specificity protein phosphatase hVH3, DUSP5, VH3|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8448b was selected from the C-term region of human DUSP5. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues. The highest relative activity is toward ERK1.|
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The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. 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. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1, is expressed in a variety of tissues with the highest levels in pancreas and brain, and is localized in the nucleus.
Mandl, M., et al., Mol. Cell. Biol. 25(5):1830-1845 (2005).Ueda, K., et al., Oncogene 22(36):5586-5591 (2003).Kwak, S.P., et al., J. Biol. Chem. 270(3):1156-1160 (1995).Ishibashi, T., et al., J. Biol. Chem. 269(47):29897-29902 (1994).Martell, K.J., et al., Genomics 22(2):462-464 (1994).
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