| Product Name | DUSP19, 65-217aa, Human |
|---|---|
| Description | 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 |
| Host | E. coli |
| Molecular Weight | 22.6 kDa (205aa), confirmed by MALDI-TOF |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSQVGVIKP WLLLGSQDAA HDLDTLKKNK VTHILNVAYG VENAFLSDFT YKSISILDLP ETNILSYFPE CFEFIEEAKR KDGVVLVHCN AGVSRAAAIV IGFLMNSEQT SFTSAFSLVK NARPSICPNS GFMEQLRTYQ EGKESNKCDR IQENSS |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 20% glycerol, 0.15M NaCl |
| Concentration | 0.5 mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Cheng H., et al. (2003) Int J BoiChem Cell Biol. 35(2):226-34. Zama Takeru., et al. (2002) J Boil Chem. 277(26):23909-18. |
| Background | 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. |
| Supplier | ARP |
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