e.coli gor protein (Recombinant) (His-Tag) (STJP017546)
SPECIFICATIONS
HostE.coli
ImmunogenE.coli
General Information
| Short Description | Recombinant-e.coli gor-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications. |
| Applications | Enzyme Activity/SDS-PAGE |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Concentration | 1 mg/mL |
| Formulation | Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 10% Glycerol, 0.1M NaCl, 1mM DTT |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
| Immunoreactivity | Specific activity is > 60unit/mg. The unit definition for glutathione reductase activity may be expressed in terms of the oxidation of NADPH or the reduction of GSSG since their molar ratio is 1:1. One unit of glutathione reductase oxidizes 1 umol of |
Target Information
| Accession Number | NP_417957 |
| Immunogen | E.coli |
| Immunogen Region | 1-450aa |
| Immunogen Sequence | MGSSHHHHHH SSGLVPRGSH MGSMTKHYDY IAIGGGSGGI ASINRAAMYG QKCALIEAKE LGGTCVNVGC VPKKVMWHAA QIREAIHMYG PDYGFDTTIN KFNWETLIAS RTAYIDRIHT SYENVLGKNN VDVIKGFARF VDAKTLEVNG ETITADHILI ATGGRPSHPD IPGVEYGIDS DGFFALPALP ERVAVVGAGY IAVELAGVIN GLGAKTHLFV RKHAPLRS |
Additional Info
| 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. |
Information sourced from Uniprot.org