Glutathione Reductase from baker’s yeast (S. cerevisiae)
SIGMA/G3664 - ammonium sulfate suspension, 100-300 units/mg protein (biuret)
Synonym: GR; NAD(P)
CAS Number: 9001-48-3
MDL Number: MFCD00131196
Product Type: Chemical
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| foreign activity | G-6-PDH, 6-PGDH, and NADPH oxidase ≤0.01% |
| lipoamide dehydrogenase ≤0.1% | |
| form | ammonium sulfate suspension |
| mol wt | 118 kDa |
| Quality Level | 200  |
| specific activity | 100-300 units/mg protein (biuret) |
| storage temp. | 2-8°C |
| UniProt accession no. | P41921  |
| Application: | Glutathione reductase (GR) from baker′s yeast (Saccharomyces cerevisiae) has been used- • for quantifying the myocardial tissue glutathione content using a glutathione reductase-5,5′-dithiobis (2-nitrobenzoic acid)-based enzymatic recycling assay • for the quantification of reduced glutathione (GSH) in the oocytes, using a slightly modified microglutathione assay, obtained from prepubertal gilts • for the preparation of total GSSG (glutathione disulphide) + GSH measurement, where all available GSSG was reduced to GSH, in rat lens • for the quantification of intracellular reduced glutathione (GSH) in the oocytes obtained from rats |
| Application: | Glutathione Reductase (GR) from baker′s yeast has been used: • in the glutathione assay to determine glutathione concentration. • as a standard in the generation of calibration curve. • as an antigen to measure plasma activity of GR. |
| Biochem/physiol Actions: | Glutathione (γ-glutamylcysteinylglyci |
| Biochem/physiol Actions: | Glutathione reductase IGR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the process is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, citrate synthase, EF hands, hemoglobins, lipocalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems. |
| Biochem/physiol Actions: | Glutathione reductase is a crucial flavoenzyme in the antioxidant defense system |
| General description: | Glutathione reductase (GLR1) exists in mitochondrial and cytoplasmic isoforms. It shares sequence and structural homology to thioredoxin reductase, and is a flavin-containing oxidoreductase. Its active site is composed of a redox-active disulphide, and it requires NADPH for its catalytic activity. It is a widely present enzyme and is found in plants, bacteria, yeast, mice and humans. |
| Other Notes: | One unit will reduce 1.0 μmole of oxidized glutathione per min at pH 7.6 at 25 °C. |
| Physical form: | Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol |
| Preparation Note: | Purified by affinity chromatography |
| Symbol |  GHS08 |
| Signal word | Danger |
| Hazard statements | H334 |
| Precautionary statements | P261 - P284 - P501 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 2 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: 100-300 units/mg protein (biuret) |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 1.6.4.2 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |