Glutathione Reductase human, buffered aqueous solution, >=10 units/mg protein, recombinant, expressed in E. coli

Application

Human glutathione reductase has been used in:glutathione reductase activity assayoxidative stress analysisredox assays

Biochem/physiol Actions

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.

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.

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.

Physical form

Solution containing 25 mM Tris-HCl, pH 7.4, 1 mM EDTA, and 50% (v/v) glycerol.

Unit Definition

1 unit will reduce 1.0 µmole of DTNB to TNB per minute at 25 °C at pH 7.5.