G9297
Glutathione Reductase human
buffered aqueous solution, ≥10 units/mg protein, recombinant, expressed in E. coli
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GR, Glutathione-disulfide reductase, NADPH:oxidized glutathione oxidoreductase
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General description
Research area: Cell signaling. Glutathione Reductase belongs to the homodimericFAD−disulfide oxidoreductases family. is made up of highly conserved domains such as two Rossmann fold domains, where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain. It favors its accumulation in the regions of high electron flux in cells where reactive species are generated.
Application
Human glutathione reductase has been used in:
- glutathione reductase activity assay
- oxidative stress analysis
- redox assays
Biochem/physiol Actions
Glutathione reductase enzyme is a homodimeric enzyme containing 1 FAD molecule and 1 NADPH binding domain per subunit. Both human GR (hGR) and Plasmodium falciparum GR (PfGR) are essential for the survival of the malaria parasite within the human erythrocyte. Thus, this enzyme may be used for studies of candidate anti-malaria reagents.
Glutathione reductase is a ubiquitous flavoenzyme involved in the protection from cell stress. Glutathione reductase catalyzes the reduction of oxidized glutathione (GSSG) to glutathione (GSH). It is essential for the glutathione redox cycle that maintains adequate levels of reduced cellular GSH, which serves as an antioxidant reacting with free radicals and organic peroxides. Glutathione is also an electron donor for glutathione peroxidases and a substrate for glutathione S-transferases contributing to the detoxification and elimination of toxic electrophilic metabolites and xenobiotics.
Human glutathione reductase is suitable as cytostatic and antimalarialagent. It may also be used to protect against malaria by mimicking favism by blockingthe enzyme with specific inhibitors.
Unit Definition
1 unit will reduce 1.0 μmole of DTNB to TNB per minute at 25 °C at pH 7.5.
Physical form
Solution containing 25 mM Tris-HCl, pH 7.4, 1 mM EDTA, and 50% (v/v) glycerol.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Plant physiology and biochemistry : PPB, 71, 173-183 (2013-08-14)
Seed germination and growth of seedlings are critical phases of plant life that are adversely affected by various environmental cues. Water availability is one of the main factors that limit the productivity of many crops. This study was conducted to
Dietary methionine can sustain cytosolic redox homeostasis in the mouse liver
Nature Communications (2014)
The Journal of biological chemistry, 275(48), 37317-37323 (2000-09-02)
The homodimeric flavoenzyme glutathione reductase (GR) maintains high intracellular concentrations of the antioxidant glutathione (GSSG + NADPH + H(+) <--> 2 GSH + NADP(+)). Due to its central function in cellular redox metabolism, inhibition of GR from the malarial parasite
Definition of transcriptome-based indices for quantitative characterization of chemically disturbed stem cell development: introduction of the STOP-Toxukn and STOP-Toxukk tests.
Archives of Toxicology, 91(2) (2017)
Free radical biology & medicine, 95, 27-42 (2016-03-01)
In this review article we examine the role of glutathione reductase in the regulation, modulation and maintenance of cellular redox homoeostasis. Glutathione reductase is responsible for maintaining the supply of reduced glutathione; one of the most abundant reducing thiols in
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