Glutathione Reductase (GR) Fluorescent Activity Kit determines GR activity by the amount of GSH generated from the reduction of GSSG with a non-fluorescent molecule, ThioStar�, that covalently binds the free thiol group on GSH to yield a highly fluorescent product. The most widely used procedure to measure GR is to monitor the oxidation of NADPH as a decrease in absorbance at 340nm. However many biological molecules absorb light at 340 nm, plus the detection system gives very low OD readings. The Glutathione Reductase Fluorescent Activity kit overcomes these problems of measuring GR activity by the direct detection of the GSH formed from oxidized glutathione.
Glutathione reductase (GR) plays an indirect but essential role in the prevention of oxidative damage within the cell by helping to maintain appropriate levels of intracellular glutathione (GSH). GSH, in conjuction with the enzyme glutathione peroxidase (GP), is the acting reductant responsible for minimizing harmful hydrogen peroxide cellular levels. The regeneration of GSH is catalyzed by GR. GR is an ubiquitous 100-120 kDa dimeric flavoprotein that catalyzes the reduction of oxidized glutathione (GSSG) to reduced glutathione, using ��-nicotinamide dinucleotide phosphate (NADPH) as the hydrogen donor. Molecules such as NADPH act as hydride donors in a variety of enzymatic processes. NADPH has been suggested to also act as an indirectly operating antioxidant, given its role in the re-reduction of GSSG to GSH and thus maintaining the antioxidative power of glutathione.
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