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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| Size/SKU | Availability | Price |
|---|---|---|
100 units | Estimated to ship TODAYfromSAINT LOUIS | $64.20 |
500 units | Estimated to ship TODAYfromSAINT LOUIS | $147.00 |
2500 units | Estimated to ship TODAYfromSAINT LOUIS | $486.00 |
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.47
EC Number:
MDL number:
Specific activity:
100-300 units/mg protein (biuret)
form
ammonium sulfate suspension
Quality Segment
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)
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:
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.
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.
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This Item | |||
|---|---|---|---|
| description ammonium sulfate suspension, 100-300 units/mg protein (biuret) | description Type VII, ammonium sulfate suspension, ≥200 units/mg protein | description lyophilized powder, ≥2.0 units/mg protein | description Type XV, lyophilized powder, 200-400 units/mg protein (modified Warburg-Christian) |
| specific activity 100-300 units/mg protein (biuret) | specific activity ≥200 units/mg protein | specific activity ≥2.0 units/mg protein | specific activity 200-400 units/mg protein (modified Warburg-Christian) |
| Gene Information bakers yeast ... GLR1(856014) | Gene Information Saccharomyces cerevisiae ... ZWF1(855480) | Gene Information - | Gene Information - |
| form ammonium sulfate suspension | form ammonium sulfate suspension | form lyophilized powder | form lyophilized powder |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. −20°C | storage temp. −20°C |
| UniProt accession no. | UniProt accession no. - | UniProt accession no. - | UniProt accession no. - |
| mol wt 118 kDa | mol wt 128 kDa | mol wt 228 kDa | mol wt 128 kDa |
Signal Word
Danger
Hazard Codes
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
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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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