Glutathione Peroxidase from human erythrocytes

GPX1 (glutathione peroxidase 1) belongs to the four membered family of GPXs, including GPX2, GPX3 and GPX4. It is a selenocysteine-containing protein. GPX1 is the major isoform of GPX enzyme and is ubiquitously present intracellularly.

Note: At the reported pH optimum of 8.8, we have found the activity to be approx. 10 times that at pH 7.0. However, to remain consistent with literature and avoid complications arising from non-enzymatic oxidation of GSH, our unit is defined at pH 7.0.

Glutathione peroxidase (GPX) from human erythrocytes has been used for the determination of the ability of peroxides to inactivate GPX in epithelial sheets obtained from cutaneous squamous cell carcinoma (CSCC) or solar keratoses (SK).

GPX1 (glutathione peroxidase 1) catalyzes the conversion of multiple organic and inorganic peroxides, by utilizing reduced glutathione (GSH) as an electron donor. This enzyme is also responsible for the removal of organic and inorganic peroxides.

Lyophilized powder containing 25% sucrose, 3% dithiothreitol, and sodium phosphate buffer salts

One unit will catalyze the oxidation by H₂O₂ of 1.0 μmole of reduced glutathione to oxidized glutathione per min at pH 7.0 at 25 °C.