Recombinant Mouse Glutathione Peroxidase 1 (Gpx1), N-His-GST

Mouse Glutathione Peroxidase 1 (Gpx1) is a key enzyme in the antioxidant defense system, belonging to the glutathione peroxidase family. It catalyzes the reduction of hydrogen peroxide (H₂O₂) and organic hydroperoxides by glutathione, thereby protecting cells from oxidative damage. Gpx1 is a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site, which is encoded by the UGA codon. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, necessary for the recognition of UGA as a Sec codon rather than a stop signal. Gpx1 is ubiquitously expressed and localized in the cytoplasm, making it the most abundant isoform in this family. It plays a crucial role in various cellular processes, including cell adhesion, migration, and mechanical stability. Gpx1 is involved in the regulation of growth-factor mediated signal transduction, mitochondrial function, and maintenance of thiol redox-balance. Knockout mice lacking Gpx1 are highly sensitive to oxidants and develop mature cataracts due to damage to the eye lens nucleus. Gpx1 has been implicated in various diseases, including cancer, cardiovascular disease, neurodegeneration, autoimmune disease, and diabetes.