Anti-DUSP19

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], Protein function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins. [The UniProt Consortium] Recommended dilutions: Western Blot: 1/500 - 1/2000. Immunofluorescence: 1/200 - 1/1000. ELISA: 1/20000. Not yet tested in other applications.. Cellular localization: