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. Synonyms: Dual specificity phosphatase 19, DUSP17, SKRP1, TS-DSP1. NCBI no.: NP_543152