High-purity tripeptide antioxidant for biochemical assays, redox studies, GST elution, detoxification research & cellular oxidative stress analysis

Sigma-Aldrich L-Glutathione Reduced (GSH) is a high-quality, ≥98% pure tripeptide composed of γ-L-glutamyl-L-cysteinyl-glycine. As one of the most critical intracellular antioxidants, reduced glutathione plays a central role in cellular redox homeostasis, detoxification of electrophilic compounds, enzyme catalysis, and the regeneration of other antioxidant systems.

This reagent-grade GSH is supplied as a white lyophilized powder, highly soluble in water (50 mg/mL), and suitable for a wide variety of biochemical applications, including GST-fusion protein elution, antioxidant capacity assays, cellular redox studies, xenobiotic metabolism, and enzyme kinetics.

Its functional groups—amine, carboxyl, and thiol—enable strong nucleophilic activity and conjugation reactions, making GSH a versatile reagent for both research and industrial biochemical processes.

Key Features & Benefits

High Purity (≥98%)

• Meets analytical and biochemical research standards
• Suitable for sensitive detection and enzymatic assays
• Consistent performance in redox and detoxification studies

Biologically Relevant Tripeptide

• Natural sequence: γ-Glu-Cys-Gly
• Endogenous antioxidant found in all mammalian tissues
• Central to glutathione redox cycling (GSH/GSSG balance)

Excellent Solubility & Stability

• Soluble in water at 50 mg/mL, forming clear, colorless solution
• Stable when stored at 2–8°C
• Ideal for preparing fresh assay solutions, standards, and buffers

Essential for GST Affinity Chromatography

• Used at 5–10 mM to elute GST-fusion proteins from glutathione-agarose
• Provides high yield elution with minimal protein denaturation
• Gold standard reagent for GST-tag workflows

Chemical & Regulatory Information

Biochemical & Physiological Role

Endogenous Antioxidant

• Neutralizes reactive oxygen species (ROS)
• Maintains intracellular redox balance
• Forms GSSG upon oxidation and is recycled by glutathione reductase

Detoxification Agent

• Co-factor for glutathione S-transferases (GSTs)
• Conjugates electrophilic xenobiotics, carcinogens, and metabolites
• Critical for Phase II detox pathways

Protein Protection & Signaling

• Forms reversible disulfide bonds with cysteine residues
• Regulates protein thiol status (thiol buffer)
• Influences signaling pathways, oxidative stress responses, and apoptosis

Regeneration of Other Antioxidants

• Restores vitamin C (ascorbate) and vitamin E (tocopherol)
• Supports antioxidant networks in mammalian cells

Applications

1. Molecular Biology & Protein Purification

• Elution of GST-tagged proteins
• Preparation of redox buffers for enzyme stabilization

2. Biochemical & Cell Biology Studies

• Redox potential and ROS assessment
• Thiol/disulfide state analysis
• Antioxidant function and glutathione cycling assays

3. Toxicology & Pharmacology

• Xenobiotic conjugation studies
• ADME research (metabolism of electrophilic compounds)
• Protective agent in oxidative stress experiments

4. Analytical & Detection Workflows

• Standard curve preparation for GSH quantification assays
• Measurement of glutathione in plant, bacterial, and mammalian cells

Available Pack Sizes

Sigma-Aldrich™ L-Glutathione Reduced (GSH), ≥98%, is a high-purity biological antioxidant essential for detoxification pathways, redox biology, GST-tag protein purification, metabolic studies, toxicology, and antioxidant regeneration research. With excellent water solubility, strong nucleophilic thiol reactivity, and broad biochemical relevance, it is a core reagent for modern molecular and cellular biology laboratories.