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Research monograph · thiol-containing tripeptide (glu-cys-gly)
L-GlutathioneResearch monograph
Oxidative Stress Studies
This monograph collects what the published literature reports about L-Glutathione — its mechanisms, the areas it is studied in, its molecular record and the sources behind them. It cycles between reduced and oxidised forms, and the ratio between them is used across the literature as a working index of cellular oxidative state — which is why it appears as a measurement as often as a subject.
For laboratory research use only — not for human or animal use
Mechanisms
How L-Glutathione works
Free Radical Scavenging
Direct Antioxidant
The free thiol group donates electrons directly to reactive species, which is how it acts as an antioxidant without requiring an enzyme to mediate.
Scavenges reactive species, radicals and peroxides directly
The cysteine thiol is the redox-active site
Protects proteins, lipids and DNA from oxidation
GPx & GST Catalysis
Enzyme Cofactor
It is also the substrate for glutathione peroxidase and S-transferase — enzymes that cannot function without it. That makes the tripeptide a cofactor as much as a scavenger.
Co-substrate for selenium-dependent GPx enzymes
GPx4 cofactor, central to ferroptosis research
Drives S-transferase detoxification reactions
Cellular Redox Homeostasis
Redox & Detox
The ratio of reduced to oxidised glutathione is used across the literature as a working index of cellular redox state, which is why the molecule appears as a measurement as often as a subject.
GSH:GSSG ratio sets redox tone, around 100:1 when healthy
Conjugates xenobiotics and electrophiles
Associated with Nrf2/HO-1 signalling
Studied applications
What L-Glutathione is researched for
REDOX BIOLOGY
Oxidative Stress & Antioxidant Defense
The reduced-to-oxidised ratio serves as the working index of cellular oxidative state across this literature.
Frontiers Pharmacol. 2014
CELL BIOLOGY
Ferroptosis & Lipid Peroxidation
Depletion is a defining step in ferroptosis, which makes the tripeptide central to that field rather than incidental to it.
Cell Death & Disease 2023
CYTOPROTECTION
Nrf2/HO-1 Pathway Signaling
Nrf2 governs the transcription of the enzymes that synthesise and use it, so the pathway and the molecule regulate each other.
Lee et al. 2019
BIOCHEMISTRY
Detoxification & Redox Defense
Conjugation by S-transferases is the mechanism, with xenobiotic clearance measured as the outcome.
Rai R. 2021
What the published work measures
The endpoints reported across the literature for this compound. The figures belong to the individual papers, not to us.
Hydrogen Peroxide Reduction
Lipid Peroxide Detoxification
Xenobiotic Conjugation
Cellular GSH:GSSG Ratio (healthy)
Reference values
L-Glutathione molecular data
Scroll for full molecular data →
Sequence
γ-L-Glutamyl-L-Cysteinyl-Glycine
Molecular weight
307.32 g/mol
Molecular formula
C₁₀H₁₇N₃O₆S
Physical form
Lyophilized powder
Documented purity
Quantified by HPLC, reported per lot
Storage
-20°C for long-term stability
Solubility
Water-soluble
Available sizes
1500mg
FAQ
Common questions about L-Glutathione
What is L-Glutathione?
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Glutathione is a tripeptide and the most abundant intracellular antioxidant in mammalian cells. It cycles between reduced and oxidised forms, and the ratio between them is used across the literature as a working index of cellular oxidative state — which is why it appears as a measurement as often as a subject.
What is L-Glutathione researched for?
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Published research on L-Glutathione concentrates on Oxidative Stress & Antioxidant Defense, Ferroptosis & Lipid Peroxidation, Nrf2/HO-1 Pathway Signaling and Detoxification & Redox Defense. Each of those areas is summarised further up this page with the citation it comes from, and the full reference list — 4 indexed publications — sits at the bottom. Study designs and concentrations vary considerably between publications, so the primary sources are worth reading directly.
How does L-Glutathione work?
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The literature describes L-Glutathione acting across Free Radical Scavenging, GPx & GST Catalysis and Cellular Redox Homeostasis, reported respectively as Direct Antioxidant, Enzyme Cofactor and Redox & Detox. Those pathways are drawn from preclinical models rather than clinical work, and they describe what has been observed rather than a settled mechanism — the individual pathway cards above cite what each one is based on.
What are the molecular specifications for L-Glutathione?
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L-Glutathione has a molecular formula of C₁₀H₁₇N₃O₆S, an average mass of 307.32 g/mol and the sequence γ-L-Glutamyl-L-Cysteinyl-Glycine. It is indexed under CAS 70-18-8. It ships as lyophilized powder. Those are nominal reference values for the parent compound. The identity of the specific material you receive is confirmed by mass spectrometry and reported on that lot's certificate.
How should L-Glutathione be stored and reconstituted?
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Store the sealed vial at -20°C, protected from light and moisture, and let it reach room temperature before opening so condensation does not form on cold powder. L-Glutathione is water-soluble; reconstitute by directing the diluent down the vial wall rather than onto the powder, then swirl to dissolve rather than shaking. Keep reconstituted solution refrigerated and avoid repeated freeze-thaw cycles — solutions are far less stable than lyophilized powder.
Is L-Glutathione approved for human use?
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No. L-Glutathione is supplied strictly for in-vitro laboratory research and development. It is not a drug, food, supplement or cosmetic, it has not been evaluated by the FDA, and it is not intended for human or animal consumption, ingestion, injection or any in-vivo use. Ordering confirms you are a qualified researcher or institution purchasing on that basis.
Cited sources
Peer-reviewed literature
Independent published research indexed from PubMed — not Routine Peptides claims.
Every production run is analyzed by an independent laboratory, and the certificate for your lot travels with the order — not a catalog-wide document, and not a summary written by us.