L-Glutathione is a naturally occurring tripeptide composed of three amino acids: cysteine, glycine, and glutamic acid.  Supplied in its reduced form (GSH), it functions as the cell’s primary intracellular antioxidant and redox regulator. As a research compound, it is widely used in oxidative stress modeling, phase II detoxification pathway studies, protein purification workflows, and mitochondrial function research.

GSH is among the most studied small molecules in cell biology. Its central role in maintaining intracellular redox balance makes it a foundational reference compound across a broad range of research disciplines, from basic biochemistry to molecular toxicology.

What makes GSH particularly versatile as a laboratory tool is its dual utility. On one hand, it is a direct participant in antioxidant defense mechanisms, neutralizing reactive oxygen and nitrogen species through its free sulfhydryl (-SH) group on the cysteine residue. It is a critical reagent in recombinant protein purification workflows; specifically in the elution of GST-tagged fusion proteins from glutathione-immobilized resin columns, where it is typically applied in the 10–40 mM concentration range.

Its involvement in phase II conjugation pathways, mitochondrial integrity, and protein folding regulation further extends its relevance across preclinical and biochemical research settings.

• CAS Number: 170-18-8
• Molecular Weight: 307.32 g/mol
• Purity: ≥99%
• Also Known As: GSH, Reduced Glutathione, gamma-L-Glutamyl-L-cysteinylglycine, L-gamma-Glutamyl-L-cysteinylglycine
• Chemical Formula: C₁₀H₁₇N₃O₆S

In cell-based models, GSH exerts its antioxidant activity primarily through its sulfhydryl group, which donates electrons to neutralize reactive oxygen species (ROS) and reactive nitrogen species (RNS). This process converts GSH to its oxidized disulfide form (GSSG), which can be recycled back to GSH by glutathione reductase in the presence of NADPH, a redox cycling mechanism studied extensively in cellular oxidative stress models.

GSH also acts as a co-substrate for glutathione peroxidase enzymes, which catalyze the reduction of hydrogen peroxide and lipid peroxides in membrane and cytosolic preparations. In phase II detoxification research, GSH conjugates with electrophilic compounds via glutathione S-transferase (GST) enzymes, facilitating the study of xenobiotic metabolism and cellular detoxification pathways.

In protein biochemistry workflows, reduced glutathione competes with GST-tagged fusion proteins for binding sites on glutathione-immobilized resin, enabling selective elution of recombinant proteins under mild, non-denaturing conditions — a standard technique in affinity chromatography protocols.

• Oxidative Stress Modeling
• Redox Biology Research
• Phase II Detoxification Studies
• Protein Purification Workflows
• Antioxidant Enzyme Studies
• Xenobiotic Metabolism Research