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For laboratory research. Sold in 500mg and 5000mg kit sizes.
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For research use only. Not for human consumption.
Glutathione (GSH) is a tripeptide composed of glutamic acid, cysteine, and glycine that functions as the primary endogenous antioxidant in mammalian cells. It is synthesized intracellularly and exists in both reduced (GSH) and oxidized (GSSG) forms, with the ratio of these states serving as a key indicator of cellular redox balance that researchers use to assess oxidative stress in experimental systems.
In laboratory research, glutathione is extensively studied for its roles in phase II xenobiotic metabolism, where it conjugates with reactive electrophiles via glutathione S-transferase enzymes. Researchers also investigate its function in maintaining protein thiol homeostasis, regulating enzyme activity through protein glutathionylation, and serving as a cofactor for glutathione peroxidase enzymes that neutralize lipid peroxides and hydrogen peroxide.
Beyond its antioxidant functions, glutathione has been investigated as a signaling molecule involved in immune cell regulation, mitochondrial function, and apoptotic pathway modulation. Its depletion in tissue culture or animal models is used as an experimental tool to investigate oxidative stress mechanisms, while supplementation studies explore how restoration of GSH levels affects cellular function in research contexts.
The areas where this compound appears in the published research literature.
Glutathione levels in research samples are typically quantified using the DTNB (Ellman's reagent) colorimetric assay, HPLC with electrochemical or fluorescence detection, or mass spectrometry-based metabolomic panels. Researchers measure both total GSH and the GSH/GSSG ratio to characterize the redox environment of cells or tissue under experimental conditions.
Functional studies deplete cellular glutathione using buthionine sulfoximine (BSO), an inhibitor of gamma-glutamylcysteine synthetase, to create controlled oxidative stress models. Restoration experiments then introduce exogenous glutathione or precursors and measure recovery of redox markers, enzyme activity, and viability parameters, establishing causal relationships between GSH levels and cellular outcomes.
In vivo research uses animal models with targeted deletion of glutathione synthesis enzymes (e.g., Gclc knockout mice) or pharmacological depletion to study systemic consequences of GSH deficiency. Researchers use liquid chromatography-mass spectrometry to profile the glutathione metabolome (GSH, GSSG, protein-glutathione mixed disulfides, and metabolites) across tissues of interest.
Lyophilized glutathione (reduced form) is hygroscopic and should be stored at -20°C in a tightly sealed container under inert atmosphere or desiccant to prevent oxidation. Exposure to air will convert GSH to GSSG; researchers should minimize headspace and handle with inert gas when possible.
Reconstituted glutathione solutions are chemically unstable in aqueous conditions at room temperature due to oxidation. Working solutions should be prepared fresh immediately before use or stabilized with EDTA (to chelate trace metals that catalyze oxidation) and stored at 4°C for a maximum of 24 hours. Long-term storage of solutions is not recommended in laboratory practice.
Glutathione (GSH) for sale from Optimum ReGen Peptides, a US research-peptide company with a storefront in Medford, Oregon. It is in stock, priced from $80. Every order ships 2-Day Priority Air, a $13 flat rate anywhere in the US, with tracking, or can be picked up at the store.
The current batch has a published third-party certificate of analysis, shown above. Glutathione is supplied as lyophilized powder, for laboratory and research use only, not for human consumption.
