Key Takeaways
- Glutathione (GSH) is a 307.33 Da tripeptide thiol built from glutamate, cysteine and glycine. Glutamate is joined to cysteine through its side-chain gamma-carboxyl rather than a standard peptide bond.
- Sourcing specification: ≥99% purity by HPLC. Measured purity is reported on the lot's Certificate of Analysis where one is on file.
- Third-party Certificates of Analysis are published where on file. Same-day US shipping.
Glutathione Specifications
Glutathione is studied in in-vitro and animal models via Two-step ATP-dependent biosynthesis. This section covers molecular identity and specification data. Analytical standard: not stated in this reference profile. Stocked material is for laboratory research use only. Identity, structure, and handling values come from the existing profile.
- Compound Name
- Glutathione (reduced form, GSH)
- Compound Class
- Gamma-glutamyl tripeptide thiol
- Molecular Formula
- C10H17N3O6S
- Molecular Weight
- ~307.33 Da
- IUPAC Name
- (2S)-2-amino-5-[[(2R)-1-(carboxymethylamino)-1-oxo-3-sulfanylpropan-2-yl]amino]-5-oxopentanoic acid
- SMILES
- C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N
- Residue Count
- 3 residues
- Residue Composition
- L-glutamate (gamma-linked), L-cysteine, glycine
- Glutamyl Linkage
- Glutamate side-chain gamma-carboxyl bonded to the cysteine amine
- Redox-Active Group
- Free cysteine thiol (sulfhydryl)
- Oxidised Counterpart
- Glutathione disulfide (GSSG)
- Physical Form
- Lyophilized powder
- Solubility
- Freely soluble in water
- Purity Standard
- ≥99% by HPLC
- Purity Testing
- Third-party HPLC analysis per batch
- Storage (Lyophilized)
- -20°C, sealed, desiccated, protected from light
- Storage (In Solution)
- 2-8°C for same-day use, or single-use aliquots at -20°C or colder
- Oxidation Sensitivity
- Thiol oxidises to GSSG in solution, faster at neutral to alkaline pH
- Documentation
- Batch Certificate of Analysis (CoA)
- Intended Use
- In-vitro laboratory research only
- Human Use
- Not for human or veterinary use
Glutathione molecular identity and purity specifications
Glutathione Mechanism of Action
Glutathione is studied in in-vitro and animal models via Two-step ATP-dependent biosynthesis. This section covers the reported mechanism and its evidence limits. Analytical standard: not stated in this reference profile. Stocked material is for laboratory research use only. Identity, structure, and handling values come from the existing profile.
Two-step ATP-dependent biosynthesis. Cells build glutathione in two ATP-dependent steps. Glutamate-cysteine ligase first joins the gamma-carboxyl of glutamate to cysteine, and glutathione synthetase then adds glycine. A 2024 review in Current Medicinal Chemistry by Gasmi and colleagues summarises this pathway together with downstream glutathione metabolism and its proposed functions, and describes cysteine supply and the first ligase step as the usual limits on synthesis rate.
At the bench, the gamma linkage is the structural detail that matters most. Most intracellular peptidases cleave alpha-peptide bonds and leave glutathione intact, so turnover depends instead on gamma-glutamyl transpeptidase, which sits on the outer face of the plasma membrane in many tissues.
This arrangement is one reason the fate of glutathione added to culture medium is debated. Some fraction may be broken down outside the cell into its constituent amino acids before any intact uptake occurs, and the balance between those two routes has not been established across cell types.
Synthesis rate and intracellular concentration differ by tissue and model. GSH and GSSG redox cycling. In its reduced form (GSH), the cysteine thiol donates electrons. Two oxidised molecules then join through a disulfide bond to form glutathione disulfide (GSSG). Glutathione peroxidases use GSH to reduce hydrogen peroxide and lipid hydroperoxides, and glutathione reductase regenerates GSH from GSSG using NADPH.
Weinbergová described the reductase's part in this oxidation-reduction cycle in 1970. In a 1989 review, Sies placed glutathione within the wider biochemistry of thiol groups. Because the cycle couples back to NADPH, the GSH:GSSG ratio is widely used as a readout of overall cellular redox state rather than as a direct measure of any single oxidant.
That reading has limits. In a 2017 perspective in Chemical Research in Toxicology, Boysen argued that the amounts of glutathione cells form do not match, stoichiometrically, the oxidative loads it is assumed to neutralise. The argument challenges the simple picture of glutathione as a one-for-one radical sink.
Whether direct scavenging or enzyme-coupled peroxide reduction dominates in a given model remains contested. Conjugation through glutathione S-transferases. Glutathione S-transferases attach glutathione to electrophilic compounds, and the mercapturic acid pathway then processes the conjugates toward excretion. Conjugation is usually framed as detoxification, but the literature records clear exceptions.
In 1983, Varghese characterised glutathione conjugates of the radiosensitiser misonidazole. In 1988, Vamvakas and colleagues reported that S-conjugates of hexachloro-1,3-butadiene were mutagenic in the Ames test, and they tied that compound's kidney carcinogenicity to activation by the same mercapturic acid pathway.
Some transferases also act outside catalysis. A 2022 review by Niitsu and colleagues describes glutathione S-transferase P1 acting as a chaperone for CRAF in MAPK signalling, a role separate from conjugation chemistry. In a separate 2003 enzymology report, Miller and colleagues found that glutathione, S-substituted glutathiones and leukotriene C4 served as substrates for peptidylglycine alpha-amidating monooxygenase.
The C-terminal glycine of glutathione therefore makes it a substrate for enzymes outside the redox network. Compartments and membrane transport. Glutathione is synthesised in the cytosol, yet it is also found in mitochondria, the endoplasmic reticulum and the nucleus, so transport must fill those separate pools.
Oestreicher and Morgan's 2019 review in Biochemistry and Cell Biology covers this subcellular distribution and the membrane transport routes proposed for it. The identity and regulation of several organelle carriers are still not fully established, so compartment-specific measurements need cautious interpretation.
No dedicated receptor mediates the antioxidant or conjugation activities of glutathione. In experimental systems those effects follow from thiol chemistry and from its use as an enzyme cofactor, which is why concentration and redox state, rather than binding affinity, are the variables to control.
Glutathione Research Applications
Glutathione is studied in in-vitro and animal models via Two-step ATP-dependent biosynthesis. This section covers the model systems and analytical readouts. Analytical standard: not stated in this reference profile. Stocked material is for laboratory research use only. Identity, structure, and handling values come from the existing profile.
GSH and GSSG quantification: McBeth and colleagues published a 2024 ortho-phthalaldehyde protocol that measures reduced and oxidised glutathione separately in cultured mammalian cells, calibrated against authentic glutathione standards.
Assay selection: a 2005 review by Rousar and colleagues surveyed glutathione assay chemistries, which helps when choosing between enzymatic recycling, fluorometric and chromatographic readouts.
Cell-free redox buffering: defined GSH and GSSG mixtures set thiol redox potential in protein refolding and enzyme assays, although optimal ratios are system specific and not standardised.
Drug resistance: Gouyette's 1994 review linked activity of the glutathione system to anticancer drug resistance in tumour cells.
Chemosensitisation in vitro: Nakanishi and colleagues reported in 1997 that glutathione derivatives enhanced adriamycin cytotoxicity in a human lung adenocarcinoma cell line.
Analogue design: Wu and Batist reviewed glutathione and synthetic glutathione analogues as experimental agents in 2013.
Glutathione Storage Requirements
Glutathione is studied in in-vitro and animal models via Two-step ATP-dependent biosynthesis. This section covers the material's structure-specific handling requirements. Analytical standard: not stated in this reference profile. Stocked material is for laboratory research use only. Identity, structure, and handling values come from the existing profile.
Reduced glutathione dissolves readily in water, but its thiol oxidises to GSSG in solution, faster at neutral to alkaline pH and in the presence of trace transition metals. Your preparation choices decide how much of the vial is still GSH when the assay begins.
Reconstitution and handling guidance: Let the sealed vial reach room temperature before opening so that condensation does not wet the powder. Record the batch number and read the HPLC purity figure on the matching Certificate of Analysis before calculating molar concentrations.
Choose a solvent suited to the assay. Sterile water or a degassed buffer suits most cell-free work, while bacteriostatic water adds benzyl alcohol, which may be unwanted in cell culture. Sparge the solvent with nitrogen or argon when oxidation must be minimised, because dissolved oxygen drives conversion of GSH to GSSG.
Add the solvent slowly down the vial wall and swirl gently until the powder dissolves. Vigorous vortexing introduces oxygen without improving solubility. Check the pH. Dissolved glutathione free acid gives an acidic solution, and raising it to physiological pH speeds thiol oxidation, so neutralise immediately before use.
Where the assay tolerates it, add a metal chelator such as EDTA to the buffer to slow metal-catalysed oxidation of the thiol. Divide the stock into single-use aliquots. Keep them at 2-8°C for same-day work or freeze them at -20°C or colder, and avoid repeated freeze-thaw cycles.
When the experiment depends on the reduced fraction, confirm the GSH:GSSG content of the working stock with a method such as an ortho-phthalaldehyde assay.
Glutathione at Peptide.Express
Glutathione is sourced against a ≥99% HPLC purity specification. Third-party Certificates of Analysis are listed by batch where on file. Same-day US shipping on orders before 2 PM EST. For laboratory research use only. Not for human or veterinary use.
Glutathione Frequently Asked Questions
What is glutathione?
Glutathione is a 307.33 Da tripeptide of glutamate, cysteine and glycine, with formula C10H17N3O6S. Glutamate is attached through its gamma-carboxyl. The free cysteine thiol lets glutathione cycle between a reduced form (GSH) and a disulfide-linked oxidised form (GSSG). That cycling makes glutathione the main small-molecule thiol redox buffer studied in cell biology and a cofactor for peroxidases and transferases.
What is the molecular weight of glutathione?
Reduced glutathione has a molecular weight of approximately 307.33 Da and the molecular formula C10H17N3O6S.
What does research say about glutathione benefits?
The evidence for glutathione benefits is strongest for its biochemistry inside cells and weakest for what added glutathione does in people. Its intracellular functions are well characterised. These include enzyme-coupled reduction of peroxides through glutathione peroxidases, conjugation of electrophiles through glutathione S-transferases, and maintenance of the GSH:GSSG ratio by NADPH-dependent glutathione reductase. Published work also links glutathione levels to conditions under investigation, such as brain aging in a 2022 review, hypertension in a 2016 review, and schizophrenia in a 2021 observational study of plasma glutathione. Association is not intervention, though. Few of these papers test whether supplying glutathione changes an outcome, and human trial data for exogenous glutathione remain limited. Glutathione supplied by Peptide.Express is intended for in-vitro research only.
How does a glutathione supplement differ from research-grade glutathione?
A glutathione supplement is a consumer product made to dietary supplement standards for oral use. Research-grade glutathione is a laboratory reagent specified by analytical purity, here a standard of ≥99% by HPLC, and comes with a batch Certificate of Analysis so that molar concentrations in assays can be calculated reliably. The two are not interchangeable, and research material is not for consumption.
What purity standard applies to Peptide.Express glutathione?
Peptide.Express sources glutathione to a standard of ≥99% purity by HPLC. Each batch is documented with a Certificate of Analysis that reports the measured result for that lot.
Is glutathione a peptide?
Glutathione is a peptide in the chemical sense: a tripeptide of three amino acid residues. Its glutamate-cysteine bond uses the glutamate side chain rather than the alpha-carboxyl, so most peptidases do not cleave it.
Are glutathione injections FDA approved?
Glutathione injections are not FDA-approved drugs for any indication in the United States. Glutathione is sold as a dietary supplement ingredient, and the FDA has publicly raised concerns about compounding sterile injectables from dietary-ingredient glutathione after receiving reports of adverse events. Research-grade glutathione from Peptide.Express is supplied for in-vitro laboratory use only and is not intended for injection or any human use.
What is the difference between GSH and GSSG?
GSH is reduced glutathione, a single 307.33 Da molecule with a free cysteine thiol. GSSG is glutathione disulfide, formed when two GSH molecules are oxidised and joined by a disulfide bond. Glutathione reductase converts GSSG back to GSH using NADPH, and the GSH:GSSG ratio is a common readout of cellular redox state.
How is glutathione measured in cell culture?
Glutathione in cell culture is usually measured as separate reduced (GSH) and oxidised (GSSG) fractions. Ortho-phthalaldehyde derivatisation is one published approach: a 2024 protocol by McBeth and colleagues quantified both forms in cultured mammalian cells. Enzymatic recycling assays and chromatographic methods are alternatives. Because sample handling can oxidise GSH artefactually, quenching and thiol-blocking steps matter as much as the detection chemistry.
Why is glutathione linked to chemotherapy resistance?
Glutathione is linked to chemotherapy resistance because tumour cells can use glutathione conjugation and redox buffering to inactivate or tolerate some anticancer drugs. Gouyette's 1994 review described resistance associated with the glutathione system. The relationship cuts both ways in experimental models. Nakanishi and colleagues reported in 1997 that glutathione derivatives enhanced adriamycin cytotoxicity in a human lung adenocarcinoma cell line, and 2022 preclinical nanoparticle studies have either exploited or depleted tumour glutathione deliberately. None of this work establishes a clinical application.
References
- Gasmi A, Nasreen A, Lenchyk L, et al. "An Update on Glutathione's Biosynthesis, Metabolism, Functions, and Medicinal Purposes." Current medicinal chemistry, 2024. Read the Gasmi 2024 record on PubMed: An Update on Glutathione's Biosynthesis, Metabolism, Functions, and Medicinal Purposes
- Weinbergová O. "[Glutathione reductase and glutathione-insulin-transhydrogenase and their participation in the oxydation-reduction transformation of glutathione]." Ceskoslovenska fysiologie, 1970. Read the Weinbergová 1970 record on PubMed: [Glutathione reductase and glutathione-insulin-transhydrogenase and their participation in the oxydation-reduction transformation of glutathione]
- Sies H. "[Biochemistry of thiol groups: the role of glutathione]." Die Naturwissenschaften, 1989. Read the Sies 1989 record on PubMed: [Biochemistry of thiol groups: the role of glutathione]
- Boysen G. "The Glutathione Conundrum: Stoichiometric Disconnect between Its Formation and Oxidative Stress." Chemical research in toxicology, 2017. Read the Boysen 2017 record on PubMed: The Glutathione Conundrum: Stoichiometric Disconnect between Its Formation and Oxidative Stress
- Varghese AJ. "Glutathione conjugates of misonidazole." Biochemical and biophysical research communications, 1983. Read the Varghese 1983 record on PubMed: Glutathione conjugates of misonidazole
- Vamvakas S, Kordowich FJ, Dekant W, et al. "Mutagenicity of hexachloro-1,3-butadiene and its S-conjugates in the Ames test--role of activation by the mercapturic acid pathway in its nephrocarcinogenicity." Carcinogenesis, 1988. Read the Vamvakas 1988 record on PubMed: Mutagenicity of hexachloro-1,3-butadiene and its S-conjugates in the Ames test--role of activation by the mercapturic acid pathway in its nephrocarcinogenicity
- Niitsu Y, Sato Y, Takayama T. "Implications of glutathione-S transferase P1 in MAPK signaling as a CRAF chaperone: In memory of Dr. Irving Listowsky." Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2022. Read the Niitsu 2022 record on PubMed: Implications of glutathione-S transferase P1 in MAPK signaling as a CRAF chaperone: In memory of Dr. Irving Listowsky
- Miller LA, Baumgart LE, Chew GH, et al. "Glutathione, S-substituted glutathiones, and leukotriene C4 as substrates for peptidylglycine alpha-amidating monooxygenase." Archives of biochemistry and biophysics, 2003. Read the Miller 2003 record on PubMed: Glutathione, S-substituted glutathiones, and leukotriene C4 as substrates for peptidylglycine alpha-amidating monooxygenase
- Oestreicher J, Morgan B. "Glutathione: subcellular distribution and membrane transport (1)." Biochemistry and cell biology = Biochimie et biologie cellulaire, 2019. Read the Oestreicher 2019 record on PubMed: Glutathione: subcellular distribution and membrane transport (1)
- McBeth C, Brown D, Pokorski P, et al. "Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro." Journal of visualized experiments : JoVE, 2024. Read the McBeth 2024 record on PubMed: Rapid Quantification of Oxidized and Reduced Forms of Glutathione Using Ortho -phthalaldehyde in Cultured Mammalian Cells In Vitro
- Rousar T, Cervinková Z, Muzáková V, et al. "[Glutathione and glutathione assays]." Acta medica (Hradec Kralove). Supplementum, 2005. Read the Rousar 2005 record on PubMed: [Glutathione and glutathione assays]
- Gouyette A. "[Resistance associated with the glutathione system]." Bulletin du cancer, 1994. Read the Gouyette 1994 record on PubMed: [Resistance associated with the glutathione system]
- Nakanishi Y, Matsuki H, Takayama K, et al. "Glutathione derivatives enhance adriamycin cytotoxicity in a human lung adenocarcinoma cell line." Anticancer research, 1997. Read the Nakanishi 1997 record on PubMed: Glutathione derivatives enhance adriamycin cytotoxicity in a human lung adenocarcinoma cell line
- Wu JH, Batist G. "Glutathione and glutathione analogues; therapeutic potentials." Biochimica et biophysica acta, 2013. Read the Wu 2013 record on PubMed: Glutathione and glutathione analogues; therapeutic potentials
- Dong S, Zhang Y, Guo X, et al. "Glutathione Pulse Therapy: Promote Spatiotemporal Delivery of Reduction-Sensitive Nanoparticles at the "Cellular Level" and Synergize PD-1 Blockade Therapy." Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2022. Read the Dong 2022 record on PubMed: Glutathione Pulse Therapy: Promote Spatiotemporal Delivery of Reduction-Sensitive Nanoparticles at the "Cellular Level" and Synergize PD-1 Blockade Therapy
- Liang B, Qiao B, Yu K, et al. "Mitochondrial Glutathione Depletion Nanoshuttles for Oxygen-Irrelevant Free Radicals Generation: A Cascaded Hierarchical Targeting and Theranostic Strategy Against Hypoxic Tumor." ACS applied materials & interfaces, 2022. Read the Liang 2022 record on PubMed: Mitochondrial Glutathione Depletion Nanoshuttles for Oxygen-Irrelevant Free Radicals Generation: A Cascaded Hierarchical Targeting and Theranostic Strategy Against Hypoxic Tumor
- Iskusnykh IY, Zakharova AA, Pathak D. "Glutathione in Brain Disorders and Aging." Molecules (Basel, Switzerland), 2022. Read the Iskusnykh 2022 record on PubMed: Glutathione in Brain Disorders and Aging
- Raffa M, Bel Hadj Youssef I, Ben Othman L, et al. "[Plasmatic glutathione levels and their relationships with clinical and therapeutic features in patients with schizophrenia]." L'Encephale, 2021. Read the Raffa 2021 record on PubMed: [Plasmatic glutathione levels and their relationships with clinical and therapeutic features in patients with schizophrenia]
- Robaczewska J, Kedziora-Kornatowska K, Kozakiewicz M, et al. "Role of glutathione metabolism and glutathione-related antioxidant defense systems in hypertension." Journal of physiology and pharmacology : an official journal of the Polish Physiological Society, 2016. Read the Robaczewska 2016 record on PubMed: Role of glutathione metabolism and glutathione-related antioxidant defense systems in hypertension
- Stanescu C, Chiscop I, Boev M, et al. "Glutathione in Skin Aging and Tissue Regeneration: A Systematic Review of Molecular Mechanisms, Redox Modulation, and Biomedical Implications." Molecules (Basel, Switzerland), 2026. Read the Stanescu 2026 record on PubMed: Glutathione in Skin Aging and Tissue Regeneration: A Systematic Review of Molecular Mechanisms, Redox Modulation, and Biomedical Implications
- Fu Z, Yao Y, Haq MZU, et al. "Glutathione's role in mitigating cadmium stress in Pogostemon cablin: Insights from combined transcriptomic and metabolomic approaches." Journal of hazardous materials, 2025. Read the Fu 2025 record on PubMed: Glutathione's role in mitigating cadmium stress in Pogostemon cablin: Insights from combined transcriptomic and metabolomic approaches
- Johnson JS, Jarvis NR, Martinez AM, et al. "Intravenous Glutathione and Vitamin Supplementation Causing Stevens-Johnson Syndrome: A Case Report." Journal of burn care & research : official publication of the American Burn Association, 2025. Read the Johnson 2025 record on PubMed: Intravenous Glutathione and Vitamin Supplementation Causing Stevens-Johnson Syndrome: A Case Report
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