Glutathione is a tripeptide — glutamate, cysteine, glycine — and the most abundant antioxidant molecule inside cells, present at millimolar concentrations that dwarf most signaling molecules.
The Redox Ledger
Glutathione exists in two states: reduced (GSH) and oxidized (GSSG). When reactive oxygen species appear, GSH neutralizes them and converts to GSSG; enzymes then recycle GSSG back. The ratio between the two states is one of the most used laboratory markers of cellular oxidative stress — a healthy cell maintains a strongly reduced balance.
Beyond Antioxidant Duty
GSH also serves as the substrate for glutathione S-transferases — the enzymes that tag unwanted compounds for export — placing it at the center of detoxification research. And through protein S-glutathionylation, it participates in redox signaling, a growing field examining how oxidation states regulate protein function.
Research Context
Redox designs frequently pair glutathione work with mitochondrial compounds — SS-31 for membrane-level ROS, NAD+ for the connected energy axis. All are in our General Health/Wellness and Anti-Aging collections.
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