Recombinant Human Glutathione Peroxidase 1 protein is a Human Full Length protein, in the 1 to 203 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis (PubMed:11115402, PubMed:36608588). Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides (PubMed:11115402, PubMed:36608588). In platelets catalyzes the reduction of 12-hydroperoxyeicosatetraenoic acid, the primary product of the arachidonate 12-lipoxygenase pathway (PubMed:11115402).
Glutathione peroxidase 1, GPx-1, GSHPx-1, Cellular glutathione peroxidase, Phospholipid-hydroperoxide glutathione peroxidase GPX1, GPX1
Recombinant Human Glutathione Peroxidase 1 protein is a Human Full Length protein, in the 1 to 203 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 30% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.04% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab113603 was purified using conventional chromatography techniques.
Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis (PubMed:11115402, PubMed:36608588). Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides (PubMed:11115402, PubMed:36608588). In platelets catalyzes the reduction of 12-hydroperoxyeicosatetraenoic acid, the primary product of the arachidonate 12-lipoxygenase pathway (PubMed:11115402).
Belongs to the glutathione peroxidase family.
During periods of oxidative stress, Sec-49 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.
Glutathione Peroxidase 1 (GPx1) also known as GSH peroxidase is a selenium-containing enzyme with a mass of approximately 22 kDa. It plays an important role in reducing hydrogen peroxide to water using glutathione as a substrate therefore protecting cells from oxidative damage. GPx1 is widely expressed in many tissues but is found in high concentrations in the liver and erythrocytes. Researchers use antibodies specific to GPx1 often obtained from specialized suppliers to study and quantify this enzyme in various biological samples.
The enzyme guards cellular components by neutralizing free radicals. GPx1 is not part of a large complex but functions as a homotetramer. Its activity is essential for preserving the redox balance within the cell preventing cellular damage from reactive oxygen species (ROS). Enzyme-linked immunosorbent assays (ELISA) often measure GPx1 activity to assess oxidative stress levels in research and clinical settings.
GPx1 is important in the glutathione metabolism and cellular antioxidant defense pathways. Within these pathways GPx1 works closely with proteins like glutathione reductase to maintain reduced glutathione levels. This interplay with other antioxidant proteins ensures cellular protection against oxidative damage. Studies focus on GPx1's role in these pathways as it underpins many critical cellular processes maintaining cell health.
Decreased GPx1 activity links to neurodegenerative diseases and cardiovascular disorders. In neurodegenerative diseases such as Alzheimer's the oxidative stress overwhelms the antioxidant defenses including GPx1. Similarly in cardiovascular disorders a diminished GPx1 activity correlates with increased oxidative stress contributing to disease progression. Researchers also investigate connections between GPx1 and other oxidative stress-related proteins like superoxide dismutase to fully understand GPx1's role in disease mechanisms.
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15% SDS-PAGE showing ab113603 (3 μg) at approximately 24.2 kDa.
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