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G3664
Glutathione Reductase from baker′s yeast (S. cerevisiae)
ammonium sulfate suspension, 100-300 units/mg protein (biuret)
Synonym(s):
GR, NAD(P)H:oxidized-glutathione oxidoreductase
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1 G
CN¥1,006.32
5 G
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CN¥11,849.43
CN¥1,006.32
List PriceCN¥1,597.73Save 37%Available to ship onApril 27, 2025Details
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1 G
CN¥1,006.32
5 G
CN¥3,242.74
25 G
CN¥11,849.43
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.47
CN¥1,006.32
List PriceCN¥1,597.73Save 37%Available to ship onApril 27, 2025Details
Request a Bulk Order
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form
ammonium sulfate suspension
Quality Level
specific activity
100-300 units/mg protein (biuret)
mol wt
118 kDa
UniProt accession no.
foreign activity
G-6-PDH, 6-PGDH, and NADPH oxidase ≤0.01%
lipoamide dehydrogenase ≤0.1%
storage temp.
2-8°C
Gene Information
bakers yeast ... GLR1(856014)
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This Item | D0632 | 43816 | D5545 |
|---|---|---|---|
| grade for molecular biology | grade - | grade for molecular biology | grade - |
| assay ≥99.5% (RT) | assay ≥98% (HPLC), ≥99.0% (titration) | assay 900-1100 mmol/L (Titration molarity) | assay ≥99.0% (titration) |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
| product line BioUltra | product line - | product line BioUltra | product line BioXtra |
| form powder | form powder | form liquid | form powder |
| mp 41-44 °C (lit.) | mp 41-44 °C (lit.) | mp - | mp 41-44 °C (lit.) |
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.[1]
Application
Glutathione Reductase (GR) from baker′s yeast has been used:
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[3]
- for the quantification of reduced glutathione (GSH) in the oocytes, using a slightly modified microglutathione assay, obtained from prepubertal gilts[2]
- for the preparation of total GSSG (glutathione disulphide) + GSH measurement, where all available GSSG was reduced to GSH, in rat lens[6]
- for the quantification of intracellular reduced glutathione (GSH) in the oocytes obtained from rats[7]
Biochem/physiol Actions
Glutathione (γ-glutamylcysteinylglycine) is a ubiquitous tripeptide thiol which plays a crucial role in oxidative stress defence mechanism of the cell. Glutathione reductase (GLR1) is responsible for the reduction of the glutathione disulfide (GSSG) to reduced glutathione (GSH).[1]
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.
Unit Definition
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
inhibitor
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Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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I P Gontar et al.
Bulletin of experimental biology and medicine, 150(6), 765-769 (2012-01-12)
The proposed method of emulsive polymerization provides the possibility of modifying and obtaining insoluble forms of superoxide dismutase (SOD), glutathione reductase, and streptolysin-O preserving nanoobjects (conformationally active centers and antigenic determinants) in their native states. Apart from enzymatic and immunological
Feng Gao et al.
The Journal of pharmacology and experimental therapeutics, 301(2), 543-550 (2002-04-19)
The present experiment determined the effects of glutathione and ascorbic acid, the two most important hydrophilic antioxidants, on myocardial ischemia-reperfusion injury and evaluated their relative therapeutic values. Isolated rat hearts were subjected to ischemia (30 min) and reperfusion (120 min)
Tünde Pusztahelyi et al.
Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS), 30, 96-101 (2014-12-20)
Selenium deficiency is a major health problem worldwide for about 1 billion people. Bacterial cells usually possess low tolerance to selenite stress and also low ability to reduce high concentrations of toxic selenite. Here, high tolerance to selenite and selenium
Caryn E Outten et al.
The Journal of biological chemistry, 279(9), 7785-7791 (2003-12-16)
To combat oxidative damage, eukaryotic cells have evolved with numerous anti-oxidant factors that are often distributed between cytosolic and mitochondrial pools. Glutathione reductase, which regenerates the reduced form of glutathione, represents one such anti-oxidant factor, yet nothing is known regarding
Kristin K Brown et al.
Free radical biology & medicine, 45(4), 494-502 (2008-05-27)
Isothiocyanates are phytochemicals with anti-cancer properties that include the ability to trigger apoptosis. A substantial body of evidence suggests that reaction of the electrophilic isothiocyanate moiety with cysteine residues in cellular proteins and glutathione accounts for their biological activity. In
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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