| Product Name | gor, 1-450aa |
|---|---|
| Description | gor, also known as Glutathione reductase, belongs to the class-I pyridine nucleotide disulfide oxidoreductase family. The main function of the protein is to maintain high levels of reduced glutathione in the cytosol. With the concomitant oxidation of NADPH, Glutathione reductase transforms oxidized glutathione to the reduced form. The active site of the protein is a redox-active disulfide bond. Recombinant E. coli gor protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | Glutathione oxidoreductase, ECK3485, gorA, JW3467 |
| Host | E. coli |
| Molecular Weight | 18.8kDa (165aa), confirmed by MALDI-TOF |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSMTKHYDY IAIGGGSGGI ASINRAAMYG QKCALIEAKE LGGTCVNVGC VPKKVMWHAA QIREAIHMYG PDYGFDTTIN KFNWETLIAS RTAYIDRIHT SYENVLGKNN VDVIKGFARF VDAKTLEVNG ETITADHILI ATGGRPSHPD IPGVEYGIDS DGFFALPALP ERVAVVGAGY IAVELAGVIN GLGAKTHLFV RKHAPLRSFD PMISETLVEV MNAEGPQLHT NAIPKAVVKN TDGSLTLELE DGRSETVDCL IWAIGREPAN DNINLEAAGV KTNEKGYIVV DKYQNTNIEG IYAVGDNTGA VELTPVAVAA GRRLSERLFN NKPDEHLDYS NIPTVVFSHP PIGTVGLTEP QAREQYGDDQ VKVYKSSFTA MYTAVTTHRQ PCRMKLVCVG SEEKIVGIHG IGFGMDEMLQ GFAVALKMGA TKKDFDNTVA IHPTAAEEFV TMR |
| Tag | His-tag |
| Reactivity | E. coli |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol, 100mM NaCl |
| Concentration | 1mg/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 | Staal G.E. et al. (1969) Biochim. Biophys. Acta 185: 63-69. Stoll V.S.. et al. (1997) Biochemistry 36: 6437-6447. |
| Background | gor, also known as Glutathione reductase, belongs to the class-I pyridine nucleotide disulfide oxidoreductase family. The main function of the protein is to maintain high levels of reduced glutathione in the cytosol. With the concomitant oxidation of NADPH, Glutathione reductase transforms oxidized glutathione to the reduced form. The active site of the protein is a redox-active disulfide bond. Recombinant E. coli gor 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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