Dual specificity protein phosphatase 10, Mitogen-activated protein kinase phosphatase 5, MAP kinase phosphatase 5, MKP-5, DUSP10, MKP5
Dual specificity protein phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the MAPK superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of this family of dual specificity phosphatases show distinct substrate specificities for MAPKs, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. DUSP10 binds to and inactivates p38 and SAPK/JNK, but not MAPK/ERK. Its subcellular localization is unique, it is evenly distributed in both the cytoplasm and the nucleus. The protein is widely expressed in various tissues and organs, and its expression is elevated by stress stimuli.
Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
Target:
The synthetic peptide sequence used to generate the antibody AP8453a was selected from the N-term region of human DUSP10. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
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