Anti-DUSP10

In 1X PBS, pH 7.4, with 0.09% sodium azide. 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. Protein function: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38. [The UniProt Consortium]