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G9297 Sigma

Glutathione Reductase human

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

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



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.

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.

Price and Availability

All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 
Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers


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