Glutathione
An endogenous antioxidant tripeptide investigated in cellular redox biology and detoxification enzymology research.
View GLUTA in the storeQuick answers
What is Glutathione?
Glutathione is a tripeptide (gamma-glutamyl thiol) of 3 amino acids with a molecular weight of 307.32 g/mol and the formula C10H17N3O6S.
How much published research cites Glutathione?
The Luvaminos Glutathione record cites 21 published references, dated 1969 to 2022. Each is listed on this page with a link to its source.
Does Luvaminos test Glutathione, and where is the certificate?
Yes. Every Glutathione lot Luvaminos sells is tested by Freedom Diagnostics Testing, PLLC, an independent laboratory. The current 1500 mg lot, GLU-1500-001, measured 99.96% purity by HPLC and a net content of 1524.90 mg, tested September 5, 2026. Its certificate is published at luvaminos.com/coa/GLU-1500-001.
What modifications does Glutathione carry?
Glutathione: γ-peptide (isopeptide) bond linking the γ-carboxyl of glutamate to the α-amino group of cysteine; reactive free cysteine thiol (reduced form, GSH).
How is Glutathione powder stored?
Sealed Glutathione powder: -20°C; store desiccated; air-sensitive. Air-sensitive (thiol oxidation to GSSG); store under desiccant.
How is Glutathione different from NAD+?
Glutathione and NAD+ are different compounds: Glutathione has 3 amino acids, a molecular weight of 307.32 g/mol and formula C10H17N3O6S; NAD+ has a molecular weight of 663.43 g/mol and formula C21H27N7O14P2. Glutathione: γ-peptide (isopeptide) bond linking the γ-carboxyl of glutamate to the α-amino group of cysteine.
Molecular Profile
- Type
- Tripeptide (gamma-glutamyl thiol)
- Molecular formula
- C10H17N3O6S
- Molecular weight
- 307.32 g/mol
- CAS number
- 70-18-8
- Amino acids
- 3
- Sequence
- gamma-Glu-Cys-Gly
- Modification
- γ-peptide (isopeptide) bond linking the γ-carboxyl of glutamate to the α-amino group of cysteine; reactive free cysteine thiol (reduced form, GSH).
Mechanism & Target Class
A γ-glutamyl tripeptide bearing a reactive cysteine thiol; the unusual γ-peptide bond confers resistance to standard aminopeptidase cleavage. The thiol serves as a one- and two-electron reductant, acting as co-substrate for glutathione peroxidases (via a selenenyl-glutathione adduct in the selenol ping-pong mechanism) and for glutathione S-transferases (nucleophilic conjugation of electrophilic substrates). The compound cycles between the reduced monomeric thiol (GSH) and the oxidized disulfide dimer (GSSG); regeneration of GSH from GSSG is catalyzed by glutathione reductase, a FAD-dependent flavoenzyme, linking glutathione availability to the intracellular NADPH pool.
Storage & Handling
- Lyophilized
- -20°C; store desiccated; air-sensitive.
- Handling
- Air-sensitive (thiol oxidation to GSSG); store under desiccant.
Primary Database
References (21)
Reviews
1Bachhawat AK, Yadav S. (2018). IUBMB Life
- 2
Forman HJ, Zhang H, Rinna A. (2009). Mol Aspects Med
- 3
Lu SC. (2009). Mol Aspects Med
- 4
Townsend DM, Tew KD. (2003). Oncogene
- 5
Sheehan D, Meade G, Foley VM, Dowd CA. (2001). Biochem J
- 6
Schafer FQ, Buettner GR. (2001). Free Radic Biol Med
- 7
Sies H. (1999). Free Radic Biol Med
- 8
Meister A, Anderson ME. (1983). Annu Rev Biochem
Clinical
9Kalamkar S, et al. (2022). Antioxidants
- 10
Sekhar RV, et al. (2022). Front Aging
- 11
ClinicalTrials.gov.. ClinicalTrials.gov
- 12
Allen J, Bradley RD.. Altern Med Rev
Primary research
13Borchert A, et al. (2018). Biochim Biophys Acta Mol Cell Biol Lipids
- 14
Dixon SJ, Lemberg KM, Lamprecht MR, et al. (2012). Cell
- 15
Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW. (1999). EMBO J
- 16
Sian J, Dexter DT, Lees AJ, et al. (1994). Ann Neurol
- 17
Karplus PA, Schulz GE. (1987). J Mol Biol
- 18
Pai EF, Schulz GE. (1983). J Biol Chem
- 19
Griffith OW, Meister A. (1979). J Biol Chem
- 20
Griffith OW, Anderson ME, Meister A. (1979). J Biol Chem
- 21
Tietze F. (1969). Anal Biochem
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