Glutathione 1500mg

What is Glutathione 1500mg?

Glutathione (γ-L-glutamyl-L-cysteinyl-glycine) represents the first line of antioxidant defense. This tripeptide, present in millimolar concentrations in cells, functions as the primary reducing agent that neutralizes reactive oxygen species before they damage proteins, lipids, or DNA. The peptide's cysteine thiol group (-SH) provides the reducing power—glutathione oscillates between reduced (GSH) and oxidized (GSSG) forms, with the GSH/GSSG ratio serving as a key indicator of cellular redox status.

Beyond direct antioxidant action, glutathione serves as a cofactor for glutathione peroxidases (which reduce hydrogen peroxide) and glutathione S-transferases (which detoxify electrophilic compounds and xenobiotics). This higher-dose preparation enables concentration-dependent studies and research requiring substantial glutathione supplementation in experimental models.

Mechanism of Action

Glutathione (GSH) functions as the primary intracellular reducing agent through its reactive cysteine thiol group (-SH). This thiol directly reduces reactive oxygen species including hydrogen peroxide, lipid peroxides, and peroxynitrite, becoming oxidized to glutathione disulfide (GSSG) in the process. The GSH/GSSG ratio serves as the major indicator of cellular redox status—healthy cells maintain ratios >100:1, which decline during oxidative stress. Glutathione reductase regenerates GSH from GSSG using NADPH, completing the redox cycle.

Beyond direct ROS scavenging, GSH serves as cofactor for glutathione peroxidases (GPx enzymes that reduce H2O2 and lipid peroxides) and glutathione S-transferases (GSTs that conjugate electrophilic toxins and xenobiotics for excretion). The peptide also maintains cysteine residues on proteins in reduced state, preventing aberrant disulfide bond formation. During oxidative stress, GSH can be exported from cells to maintain extracellular redox balance. Intracellular GSH concentration (1-10 mM) far exceeds other antioxidants, positioning it as the first line of defense against oxidative damage.

Key Research Findings

• Maintains intracellular concentrations of 1-10 mM in hepatocytes, 100-1000 fold higher than other antioxidants [Meister & Anderson, 1983]
• Demonstrates GSH/GSSG ratio decline from >100:1 (healthy) to <10:1 during severe oxidative stress [Schafer & Buettner, 2001]
• Reduces oxidative DNA damage by 72% in cells supplemented with glutathione vs depleted controls [Dröge, 2002]
• Shows KM of 1.2 mM for glutathione peroxidase and 0.6 mM for glutathione S-transferase [Hayes et al., 2005]
• Protects mitochondria from oxidative damage with 58% reduction in cardiolipin peroxidation in GSH-supplemented models [Marí et al., 2009]

Research Applications

• Redox biology
• Oxidative stress models
• Glutathione peroxidase studies
• Cellular detoxification pathways
• Thiol biochemistry
• Xenobiotic metabolism
• GSH/GSSG ratio studies
• Antioxidant defense mechanisms

Reconstitution & Use

Reconstitute with bacteriostatic water for laboratory use. For detailed reconstitution instructions and concentration ratios for your specific research application, see our reconstitution guide.

Storage & Handling

Store lyophilized at -20°C protected from light and oxidizing conditions. Upon reconstitution with sterile water, use promptly or store at 2-8°C for up to 30 days. Glutathione oxidizes over time; fresh solutions provide optimal reducing capacity.