The lot-specific Certificate of Analysis provides the units per mg and mg/mL values. Using this information, prepare the glutathione reductase solution in assay buffer immediately before use. This solution should not be stored, and storage of diluted stock solutions is not recommended.
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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100 UNITS
$62.00
500 UNITS
$147.00
2500 UNITS
$486.00
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.47
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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 | P5381 | G7877 | P7634 |
|---|---|---|---|
| specific activity 100-300 units/mg protein (biuret) | specific activity ≥400 units/mg protein (biuret) | specific activity ≥200 units/mg protein | specific activity ≥500 units/mg protein |
| Gene Information bakers yeast ... GLR1(856014) | Gene Information yeast ... PGI1(852495) | Gene Information Saccharomyces cerevisiae ... ZWF1(855480) | Gene Information - |
| form ammonium sulfate suspension | form ammonium sulfate suspension | form ammonium sulfate suspension | form ammonium sulfate suspension |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| UniProt accession no. | UniProt accession no. | UniProt accession no. - | UniProt accession no. - |
| mol wt 118 kDa | mol wt tetramer 119,500 Da±600 | mol wt 128 kDa | mol wt - |
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.
Glutathione reductase is a crucial flavoenzyme in the antioxidant defense system
Physical form
Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol
Preparation Note
Purified by affinity chromatography
Other Notes
One unit will reduce 1.0 μmole of oxidized glutathione per min at pH 7.6 at 25 °C.
related product
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
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
Eugine Lee et al.
Reproduction (Cambridge, England), 134(3), 405-414 (2007-08-22)
In an effort to improve the quality of in vitro produced porcine embryos, we investigated the effect of brain-derived neurotropic factor (BDNF), a neurotropin family member, on in vitro maturation (IVM) of porcine oocytes. The expression of BDNF and truncated
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
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Related Content
QC Methods
Product Information Sheet
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If I have to prepare 1.6 U/ml of glutathione reductase then how should i prepare it (G3664)
1 answer-
Helpful?
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I recently purchased G3664 (100 units). I am wondering how much volume (mL) of the reagent is there in the bottle. Your response is highly appreciated.
1 answer-
The volume can be determined using the activity value reported on the lot specific Certificate of Analysis.
For example, if the activity is reported to be 224 units/mg protein (Biuret):
This equates to 5.2 units /mL protein (Biuret)100 units / 224 units/mg =0.446mg, that is, 100 units = 0.446 mg protein
If the protein content is 5.2 mg/ml, then 0.446mg should be approximately 0.086 ml=86 μLHelpful?
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