Research Areas

Specifications

  • Use Measure Total GSH and GSSG to Determine Oxidative Stress
  • Sample Lysates, WB, RBCs, Serum, Plasma, Urine and Tissue
  • Sensitivity 0.634 μM (Plate-based Format)
  • Samples/Kit 43 (Total and GSSG) in duplicate
  • Stability Stable 4˚C Liquid Reagents
  • Colorimetric 405 nm
  • Standard Curve
  • Description

    Glutathione (L-γ-glutamyl-L-cysteinylglycine; GSH) is the highest concentration non-protein thiol in mammalian cells and is present in concentrations of 0.5 – 10 mM. GSH is a tripeptide that contains an unusual peptide linkage between the amine group of cysteine and the carboxyl group of the glutamate side-chain. It is an antioxidant, preventing damage to important cellular components caused by reactive oxygen species such as free radicals and peroxides. Glutathione reduces disulfide bonds formed within cytoplasmic proteins to cysteines by serving as an electron donor. In the process, glutathione is converted to its oxidized form, glutathione disulfide (GSSG). Glutathione is found mostly in its reduced form since the enzyme that reverts it from its oxidized form, glutathione reductase, is constitutive and inducible upon oxidative stress. The ratio of reduced glutathione to oxidized glutathione within cells is often used as a measure of cellular toxicity.