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Glutathione (GSH)

Glutathione (γ-L-glutamyl-L-cysteinylglycine, GSH, CAS 70-18-8) is the most abundant endogenous intracellular antioxidant, a tripeptide with a molecular weight of approximately 307.3 Da and formula C₁₀H₁₇N₃O₆S. Synthesized in virtually all mammalian cells through two sequential ATP-dependent enzymatic reactions (γ-glutamylcysteine synthetase and glutathione synthetase), GSH exists at millimolar concentrations (1–10 mM) in the cytosol. It is a fundamental research tool in redox biology, oxidative stress, and cellular detoxification mechanisms.

Technical Specifications

Property Value
CAS Number 70-18-8
Molecular Formula C₁₀H₁₇N₃O₆S
Molecular Weight ~307.3 Da
Purity ≥99% (HPLC-verified)
Appearance Lyophilized white powder
Solubility Highly soluble in sterile water and aqueous buffers
Storage -20°C (lyophilized), 2–8°C (reconstituted)

Mechanism of Action

Glutathione functions as the principal cellular redox buffer through reversible oxidation of its cysteinyl thiol group. Reduced glutathione (GSH) donates electrons to neutralize reactive oxygen species (ROS) — including superoxide (O₂⁻), hydrogen peroxide (H₂O₂), and hydroxyl radicals (·OH) — either directly or through its role as a co-substrate for glutathione peroxidase (GPx) enzymes. The resulting oxidized glutathione (GSSG) is recycled back to GSH by glutathione reductase using NADPH as the electron donor, maintaining the crucial GSH:GSSG ratio (typically >100:1) that defines cellular redox status. Beyond direct antioxidant defense, GSH serves as a cofactor for glutathione S-transferase (GST)-mediated detoxification of xenobiotics, electrophilic compounds, and lipid peroxidation products through conjugation reactions. GSH also maintains the reduced state of protein thiols through glutaredoxin-mediated deglutathionylation, regulates cell proliferation and apoptosis via redox-sensitive transcription factors (NF-κB, AP-1, Nrf2), and participates in leukotriene and prostaglandin biosynthesis as a co-substrate. The γ-glutamyl bond (rather than the standard α-peptide bond) confers resistance to intracellular peptidases.

Research Applications

  • Primary: Redox biology — oxidative stress, GSH/GSSG ratio, cellular antioxidant defense
  • Secondary: Xenobiotic detoxification and GST-mediated conjugation, apoptosis and cell death signaling, mitochondrial redox homeostasis
  • Model Systems: In vitro (all mammalian cell types, isolated mitochondria, GSH depletion models using BSO), in vivo (oxidative stress models, acetaminophen-induced hepatotoxicity, ischemia-reperfusion)

Quality Control & Analytical Methods

  • HPLC: ≥99% purity verification at 214/220 nm (C18 reversed-phase column)
  • Mass Spectrometry: ESI-MS for molecular weight confirmation (~307.3 ±1.0 Da)
  • Peptide Content: Amino acid analysis (AAA) for net peptide content determination
  • Endotoxin: <1 EU/mg (LAL assay)
  • TFA Content: <1% (ion chromatography)

Stability & Storage

Condition Stability
-20°C (lyophilized) 24 months
4°C (lyophilized) 6 months
25°C (lyophilized) 1 month
Reconstituted (4°C) 7 days
Reconstituted (-20°C) 30 days

Key Research References

  • Meister & Anderson (1983) — Glutathione. Annu Rev Biochem. PMID: 6137189
  • Forman et al. (2009) — Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med. PMID: 18712089
  • Lu (2013) — Glutathione synthesis. Biochim Biophys Acta. PMID: 22995213

Source & Purchase

For researchers requiring research-grade GLUTATHIONE with full analytical documentation including HPLC, LC-MS, and Certificate of Analysis, visit the HK Peptides product page for specifications, bulk pricing, and ordering.

View GLUTATHIONE Product →

FAQ

Q: What purity level is standard for Glutathione? A: HK Peptides supplies Glutathione at ≥99% purity by HPLC with full COA documentation.

Q: How should Glutathione be stored for research use? A: Lyophilized Glutathione should be stored at -20°C, protected from moisture. Reconstituted solutions at 4°C for short-term use (up to 7 days). Note: GSH slowly oxidizes to GSSG in solution at neutral pH.