| Product Name | Phosphoserine phosphatase Human, Recombinant |
|---|---|
| Description | Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+ General references: -dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated by local rearrangement of the alpha-helical bundle domain, is important to substrate recognition and hydrolysis. Recombinant human hPSP was overexpressed in E. coli and purified by conventional chromatography. |
| Synonyms | PSPH, Phosphoserine phosphatase Human, PSPase, PSP, EC 3.1.3.3, O-phosphoserine phosphohydrolase, L-3-phosphoserine phosphatase, Phosphoserine phosphatase, L 3 phosphoserine phosphatase, O phosphoserine phosphohydrolase, Phosphoserine phosphatase deficiency, included, |
| Host | E. coli |
| Molecular Weight | 84 kDa (750 aa) |
| Amino Acid Sequence | MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 40mM Tris pH 8.0, 100mM NaCl, 4mM MgCl2, 2mM DTT, 40% glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 95% 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 | Moro-Furlani., AM., et al. (1980) Ann. Hum. Genet. 43, 323-333 Collet JF., et al. (1997) FEBS Lett. 408, 281-284 Kim HY, et al. (2002) J Biol Chem. 277, 46651-8. |
| Background | Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+ General references: -dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated by local rearrangement of the alpha-helical bundle domain, is important to substrate recognition and hydrolysis. Recombinant human hPSP was overexpressed in E. coli and purified by conventional chromatography. |
| Supplier | ARP |
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