Recombinant Human Glutathione Reductase protein is a Human Fragment protein, in the 106 to 522 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
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| Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Maintains high levels of reduced glutathione in the cytosol.
GLUR, GRD1, GSR, GR, GRase
Recombinant Human Glutathione Reductase protein is a Human Fragment protein, in the 106 to 522 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Maintains high levels of reduced glutathione in the cytosol.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Recombinant human GSR protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Glutathione reductase also known as GSR is an enzyme that plays a mechanical role in maintaining the redox balance within cells. This enzyme reduces glutathione disulfide (GSSG) to the sulfhydryl form GSH which is essential for detoxifying reactive oxygen species. Glutathione reductase has a molecular weight of approximately 55 kDa. It is widely expressed in various tissues including the liver where it participates in detoxification processes. The enzyme operates in the cytosol and mitochondria reflecting its necessity across different cellular compartments.
The enzyme sustains a supply of reduced glutathione which is important for antioxidant defense and cellular protection against oxidative stress. As a critical player in the glutathione system it is not part of a larger complex but interacts significantly within the cellular antioxidant framework. It supports important functions like protein folding and DNA synthesis by keeping the cellular redox environment stable. The enzyme’s activity ensures that glutathione an important antioxidant with a molecular weight of 307.32 Da remains in its active form to fulfill its protective roles.
The enzyme is deeply integrated into the pentose phosphate pathway which generates NADPH necessary for the reduction of glutathione disulfide. It also connects to the glutathione metabolism pathway where it maintains homeostasis through GSH regeneration. Glutathione reductase intersects with other proteins like glutathione peroxidase (GPx) which uses GSH to reduce hydrogen peroxide displaying a coordinated effort in mitigating oxidative damage.
Deficiency or dysfunction of this enzyme links to conditions such as hemolytic anemia where reduced enzyme activity leads to higher susceptibility to oxidative damage in red blood cells. Additionally its dysfunction associates with neurodegenerative disorders where oxidative stress plays a critical role. The enzyme's function relates to proteins like superoxide dismutase (SOD) in disease pathways where both contribute to managing oxidative stress. Understanding alterations in glutathione reductase activity may offer insights into therapeutic strategies for these oxidative stress-related conditions.
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