Glutathione Peroxidase  (Synonyms: GSH-Px; EC 1.11.1.9)

Glutathione Peroxidase (GSH-Px; EC 1.11.1.9) belongs to the peroxidase family and is commonly used in biochemical research. Glutathione Peroxidase can catalyze reduced glutathione (GSH) to form a disulfide bridge with another glutathione molecule, convert it into oxidized glutathione (GSSG), and react with hydrogen peroxide or lipid peroxide reaction, reducing it to H₂O. Glutathione Peroxidase is an effective antioxidant against oxidative stress^[1].

Glutathione peroxidase (EC 1.11.1.9) is the general name for a family of multiple isozymes that catalyze the reduction of H₂O₂ or organic hydroperoxides to water or corresponding alcohols using reduced glutathione (GSH) as an electron donor (H₂O₂ + 2GSH → GS-SG + 2H₂O). In Metazoa, some Glutathione peroxidases have a selenium-dependent glutathione peroxidase activity, with selenocysteine being encoded by an opal TGA codon. In mammalian tissues, there are four major selenium dependent Glutathione peroxidase isozymes: GPx1, GPx2, GPx3, GPx4. GPx1, 2 and 3 act as homotetramers, whereas GPx4 is functional as a monomer^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9013-66-5

Liquid

Colorless to light yellow

[Glutathione Peroxidase]

1.11.1.9

≥300U/mg protein

One unit is defined as the amount of enzyme that will catalyze the oxidation 1.0 μmole of reduced glutathione to oxidized glutathione per min at pH 7.0 at 25°C

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Regina Brigelius-Flohé, et al. Regulatory Phenomena in the Glutathione Peroxidase Superfamily. Antioxid Redox Signal. 2020 Sep 1;33(7):498-516.  [Content Brief]

  [2]. Margis R, et al. Glutathione peroxidase family-an evolutionary overview. FEBS J. 2008 Aug;275(15):3959-70.  [Content Brief]