DUSP19 Rabbit Polyclonal Antibody

Dual specificity phosphatase 19 (DUSP19) Homo sapiens 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., 2009 [PubMed 19228121]) .[supplied by OMIM, Dec 2009], catalytic activity:A phosphoprotein + H (2) O = a protein + phosphate., catalytic activity:Protein tyrosine phosphate + H (2) O = protein tyrosine + phosphate., function:Has a dual specificity toward Ser/Thr and Tyr-containing proteins., similarity:Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily., similarity:Contains 1 tyrosine-protein phosphatase domain., tissue specificity:Expressed in the heart, lung, liver, and pancreas. The expression level in the pancreas is the highest.

DUSP19; DUSP17; LMWDSP3; SKRP1; Dual specificity protein phosphatase 19; Dual specificity phosphatase TS-DSP1; Low molecular weight dual specificity phosphatase 3; LMW-DSP3; Protein phosphatase SKRP1; Stress-activated protein kinase pathway