G3664
Glutathione Reductase from baker′s yeast (S. cerevisiae)
ammonium sulfate suspension, 100-300 units/mg protein (biuret)
Sign Into View Organizational & Contract Pricing
All Photos(1)
Synonym(s):
GR, NAD(P)H:oxidized-glutathione oxidoreductase
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.47
Recommended Products
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)
Looking for similar products? Visit Product Comparison Guide
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.
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.
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
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).
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
Product No.
Description
Pricing
related product
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
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)
Yan-Guang Wu et al.
Cell research, 17(8), 722-731 (2007-08-08)
Selecting oocytes that are most likely to develop is crucial for in vitro fertilization and animal cloning. Brilliant cresyl blue (BCB) staining has been used for oocyte selection in large animals, but its wider utility needs further evaluation. Mouse oocytes
Jing Wang et al.
Acta ophthalmologica, 88(7), 779-785 (2010-01-28)
To investigate the evolution of cataract development and glutathione redox balance in the rat lens after in vivo close-to-threshold dose exposure to ultraviolet radiation (UVR) around 300 nm. Three groups of 10 Sprague-Dawley rats were unilaterally exposed to 8 kJ/m²
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
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service