||Recombinant human DUSP19 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
||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.
||Liquid. In 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM DTT, 10% glycerol, 0.1 M NaCl.
||9.4 kDa (176 aa), confirmed by MALDI-TOF
||> 90 % by SDS-PAGE
||0.5 mg/ml (determined by Bradford assay)
|Sequences of amino acids:
||MGSSHHHHHH SSGLVPRGSH MGSQVGVIKP WLLLGSQDAA HDLDTLKKNK VTHILNVAYG VENAFLSDFT YKSISILDLP ETNILSYFPE CFEFIEEAKR KDGVVLVHCN AGVSRAAAIV IGFLMNSEQT SFTSAFSLVK NARPSICPNS GFMEQLRTYQ EGKESNKCDR IQENSS
||Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.