Species : |
Human |
Source : |
E.coli |
Tag : |
His |
Protein Length : |
43-522 aa |
Description : |
This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. This enzyme is a homodimeric flavoprotein. It is a central enzyme of cellular antioxidant defense, and reduces oxidized glutathione disulfide (GSSG) to the sulfhydryl form GSH, which is an important cellular antioxidant. Rare mutations in this gene result in hereditary glutathione reductase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been found. |
Form : |
Liquid |
Molecular Mass : |
54.3 kDa |
Bio-activity : |
Specific activity is > 45 unit/mg. |
AASequence : |
MGSSHHHHHHSSGLVPRGSHMGSMAMACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR |
Application : |
Enzyme Activity, SDS-PAGE |
Unit Definition : |
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 μmol of NADPH per minute at 37 centigrade, pH 7.5. |
Purity : |
> 95% by SDS-PAGE |
Note : |
For research use only. This product is not intended or approved for human, diagnostics or veterinary use. |
Storage : |
Can be stored at +2 to +8 centigrade for 1 week. For long term storage, aliquot and store at -20 to -80 centigrade. Avoid repeated freezing and thawing cycles. |
Storage Buffer : |
20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol, 0.1M NaCl |
Concentration : |
1 mg/mL (determined by Bradford assay) |
Reference : |
1. Stoll V S., et al. (1997) Biochemistry. 36:6437-6447.
2. Karplus P A., et al. (1987) J Mol biol. 195:701-729. |