||DUSP19, 65-217aa, Human, His tag, E.coli
||Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. 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 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 (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al.
||Expressed in the heart, lung, liver, and pancreas. The expression level in the pancreas is the highest.
||>90% by SDS-PAGE
||Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.Contains 1 tyrosine-protein phosphatase domain.