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Merck

G9297

Sigma-Aldrich

Glutathione Reductase human

buffered aqueous solution, ≥10 units/mg protein, recombinant, expressed in E. coli

Sinónimos:

GR, Glutathione-disulfide reductase, NADPH:oxidized glutathione oxidoreductase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

recombinant

expressed in E. coli

Quality Level

form

buffered aqueous solution

specific activity

≥10 units/mg protein

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... GSR(2936)

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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Descripción
Precios

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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C C Bohme et al.
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
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Plant physiology and biochemistry : PPB, 71, 226-234 (2013-08-27)
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