Glutathione (γ-L-glutamyl-L-cysteinyl-glycine, GSH) is a tripeptide composed of glutamate, cysteine, and glycine with a molecular weight of approximately 307.32 Da and the molecular formula C₁₀H₁₇N₃O₆S. As the most abundant low-molecular-weight thiol in mammalian cells, glutathione serves as the principal intracellular redox buffer and has been the subject of extensive investigation in oxidative stress, detoxification, and cellular homeostasis research.
The biochemistry of glutathione centers on the reactive sulfhydryl group of its cysteine residue, which enables participation in thiol-disulfide exchange reactions. The GSH/GSSG (reduced/oxidized glutathione) ratio serves as a critical indicator of cellular redox status in experimental systems. In cell culture models, perturbation of this ratio has been associated with activation of redox-sensitive transcription factors including Nrf2, NF-κB, and AP-1. Glutathione peroxidase (GPx) enzymes utilize GSH as a co-substrate for the reduction of hydrogen peroxide and lipid hydroperoxides, positioning glutathione at the center of enzymatic antioxidant defense research.
Phase II detoxification research represents a major application area. Glutathione S-transferases (GSTs) catalyze the conjugation of GSH to electrophilic substrates, facilitating their elimination in hepatocyte and other cell models. In vitro studies using primary hepatocyte cultures and HepG2 cell lines have demonstrated that intracellular GSH concentration directly influences xenobiotic conjugation capacity. These findings are central to toxicology and drug metabolism research.
Additional research applications include mitochondrial function studies, where a distinct mitochondrial glutathione pool (mGSH) has been identified as essential for electron transport chain integrity and mitochondrial membrane potential maintenance. In neuronal cell models, GSH depletion has been used to model oxidative stress conditions relevant to neurodegeneration research. Immune cell function studies have demonstrated that lymphocyte proliferation and cytokine production are sensitive to intracellular GSH concentrations in PBMC culture systems.
Erosyn Labs provides glutathione in its reduced form (GSH) as a lyophilized powder at ≥99% purity verified by HPLC. Each lot includes a comprehensive Certificate of Analysis documenting purity, identity by mass spectrometry, and thiol content quantification. Reconstitution in sterile water or phosphate-buffered saline (pH 6.5–7.0) is recommended; acidic pH helps maintain the reduced state. Store lyophilized material at -20°C, protected from light and moisture. Reconstituted solutions should be aliquoted, stored at -20°C, and used promptly, as GSH is susceptible to auto-oxidation in aqueous solution.
For research and laboratory use only. Not for human consumption.
