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Research Overview

Glutathione: Antioxidant & Redox Research Overview

Category: Antioxidant & Redox Research

Research Use Only — Not for human or veterinary use, consumption, or administration.

Research At a Glance

Research Category
Antioxidant & Redox Research
Peptide Length
3 amino acids (Glu-Cys-Gly tripeptide)
Purity
≥ 98% (HPLC)
Published Studies
200,000+ indexed
Storage
Lyophilized: 2–8 °C, protected from light. Reconstituted: 2–8 °C, use within 30 days.
Research Use Only

Published-study figures are approximate PubMed result counts and indicate the volume of available literature only. Purity reflects third-party analytical testing on the corresponding lot; see the Quality Assurance Center for lot-matched certificates.

Overview

Glutathione (GSH) is a tripeptide composed of cysteine, glycine, and glutamate, synthesized in the cytosol of virtually all human cells and widely regarded as the body’s principal intracellular antioxidant. Its reactive thiol (sulfhydryl) group allows it to directly neutralize reactive oxygen species (ROS) and reactive nitrogen species (RNS), and to serve as a cofactor for glutathione peroxidase in reducing hydrogen peroxide and lipid peroxides. Because oxidative stress is implicated in aging, neurodegeneration, and numerous chronic disease models, GSH — and the ratio of its reduced (GSH) to oxidized (GSSG) forms — is one of the most widely used biomarkers in redox biology research.

Citation

Sies H., “Glutathione and its role in cellular functions”

History

Glutathione was first discovered in 1888 by Joseph Charles François de Rey-Pailhade, with its full tripeptide composition established in 1929 through the work of Gowland Hopkins and colleagues. Since then, it has become one of the most studied molecules in redox and aging biology, with a well-characterized synthesis pathway (via the rate-limiting enzyme glutamate-cysteine ligase) and a recognized age-related decline that has been linked to dysregulation of the Nrf2 transcriptional pathway. Research applications span cellular protection, detoxification, immune modulation, and — more recently — neurodegenerative disease research examining GSH depletion in conditions such as Alzheimer’s disease.

Citation

Hopkins F.G. (1929)

Structure

CAS #70-18-8
Molecular FormulaC10H17N3O6S
Molecular Weight307.32 g/mol
PubChem CID124886

Research Findings

Glutathione has been studied across oxidative stress, immune function, detoxification, and neurodegenerative models.

Key Areas of Research

  • Antioxidant/redox biology: Direct ROS/RNS neutralization, cofactor for glutathione peroxidase, GSH/GSSG ratio as a redox status biomarker
  • Cellular protection: Mitochondrial oxidative damage mitigation, roles in autophagy, apoptosis, and ferroptosis regulation
  • Immune function: T-cell activation, cytokine production modulation
  • Neurological: Reported protective role against oxidative damage to amyloid-beta peptide methionine residues in Alzheimer’s disease research models

Summary

Together, these findings position glutathione as a foundational molecule in redox biology research, relevant across aging, immune function, detoxification, and neurodegenerative disease models. Its central role in cellular antioxidant defense has made the GSH/GSSG ratio a standard laboratory measure of oxidative stress across many research contexts, from basic cell biology to clinical oncology studies examining chemotherapy-induced oxidative stress.

Citation

Sies H.

References

  • Sies H. Glutathione and its role in cellular functions. Free Radical Biology and Medicine.
  • Perricone C., et al. Glutathione: the master antioxidant. (review compilation).
  • Silva-Islas C.A., Maldonado P.D. (2021). Oxidative Stress: Glutathione and Its Potential to Protect Methionine-35 of Aβ Peptide from Oxidation. ACS Omega.

Certificate of Analysis

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Research Use Only. This content is for laboratory and educational research purposes only. Not a drug, food, cosmetic, or dietary supplement. Not intended for human or veterinary use, consumption, administration, or diagnostic purposes.