GPX2 (human, recombinant)

Glutathione peroxidase 2 (GPX2) is a selenocysteine-containing glutathione peroxidase that protects cells from oxidative damage. It is a homotetramer and has an active site containing selenocysteine, glutamine, asparagine, and tryptophan. mRNA encoding GPX2 has been found predominantly in the liver and gastrointestinal tract and is localized to the nucleus and cytosol, and GPX2 can reduce organic peroxides, such as hydrogen-, tert-butyl-, or cumene hydroperoxide. It catalyzes the reduction of these reactive oxygen species (ROS) to water or their corresponding non-toxic lipid alcohols by converting glutathione (GSH) to oxidized glutathione (GSSH), reducing intracellular oxidative stress. GPX2 knockout increases inflammation and tumor growth in a dextran sulfate sodium (DSS) mouse model of inflammation-associated colon carcinogenesis. Its levels are increased in undifferentiated basal cells, but absent in lineage-restricted luminal progenitors and luminal cells, in normal human breast tissue. GPX2 levels are decreased in triple-negative- and HER2+ breast cancers, but not in luminal breast cancers, and are negatively correlated with patient survival. Cayman's GPX2 (human, recombinant) protein can be used for enzyme activity assays.Synonyms: Glutathione Peroxidase 2 (Gastrointestinal), GSHPX2, GSHPX-GI. Purity: >95% estimated by SDS-PAGE. Source: Active recombinant human GPX2 expressed in E. coli. Amino Acids: 190 residues. Formulation: (Request formulation change), 25 mM Tris-HCl, pH 8.0, with 250 mM sodium chloride, 2 mM 2-mercaptoethanol, and 10% glycerol.