Recombinant human DUSP17/DUSP19 protein

Dual specificity phosphatase 19, also known as DuSP19, is a member of the dual specificity protein phosphatase subfamily. DuSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DuSP19 is a protein phosphatase which functions as a stress-activated protein kinase pathway-regulating phosphatase. DuSP19 contains a variation of the consensus DuSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and lacks the N-terminal CH2 domain found in the MKP class of DuSPs. Recombinant human DuSP19 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.