Description
Product Characteristics:
Glutathione peroxidase (GPx) enzymes are generally selenium-containing tetrameric glycoproteins that help prevent lipid peroxidation of cell membranes. GPx enzymes reduce lipid hydroperoxides to alcohols, and reduce free hydrogen peroxide to water. GPx members are among the few proteins known in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA. There are eight GPx homologs (GPx-18). GPx-1 plays an important role in the antioxidant defense of the vascular wall and neural cells in response to oxidative stress. GPx-2 is the major isoform in the lungs and its basal or inducible expression is dependent on Nrf2. GPx-3 is under regulation by hypoxic stress and the expression and deficiency of GPx-3 is associated with cardiovascular disease and stroke. GPx-5 is selenium-independent, it is bound to the acrosome of sperm, where it may protect sperm from premature acrosome reaction in the epididymis.
Subcellular location: Cytoplasm
Synonyms: Gastrointestinal glutathione peroxidase, GI GPx, Glutathione peroxidase 2 gastrointestinal, Glutathione peroxidase 2, Glutathione peroxidase gastrointestinal, Glutathione peroxidase related protein 2, Glutathione peroxidase-gastrointestinal, Glutathione peroxidase-related protein 2, GPRP, GPRP-2, GPx 2, GPx-2, GPx-GI, GPX2, GPX2_HUMAN, GSHPx 2, GSHPx GI, GSHPx-2, GSHPx-GI.
Target Information: This gene is a member of the glutathione peroxidase family and encodes a selenium-dependent glutathione peroxidase that is one of two isoenzymes responsible for the majority of the glutathione-dependent hydrogen peroxide-reducing activity in the epithelium of the gastrointestinal tract. The protein encoded by this locus contains a selenocysteine (Sec) residue encoded by the UGA codon, which normally signals translation termination. Alternatively spliced transcript variants have been described. [provided by RefSeq, Feb 2012]