L-Glutathione 1500mg is a pure, lyophilized form of the naturally occurring tripeptide γ-L-glutamyl-L-cysteinyl-glycine. It is one of the most abundant low-molecular-weight thiols in mammalian cells and functions as the primary intracellular antioxidant. It is used to study redox balance, detoxification pathways, and cellular stress responses in research settings. Glutathione also supports investigations on mitochondrial function and age-related oxidative damage. Each vial contains 600 mg of ≥99% pure reduced L-Glutathione. The product appears as a white lyophilized powder and is manufactured and analytically tested in the United States. This vial size supports in vitro assays, cell culture work, and small-animal protocols. L-Glutathione is supplied only for laboratory research use and is not intended for human consumption or therapeutic use.
Biochemical Characteristics
Glutathione (GSH) is a tripeptide composed of glutamic acid, cysteine, and glycine. It contains a γ-glutamyl bond between glutamate and cysteine, which is critical for its activity.
Key Properties
- Molecular formula: C₁₀H₁₇N₃O₆S
- Molecular weight: 307.32 Da
- CAS number: 70-18-8
- Appearance: White to off-white lyophilized powder
- Solubility: Highly soluble in water (~200 mg/mL)
- Redox pair: GSH ↔ GSSG
- Standard redox potential: ~-240 mV at pH 7
The cysteine thiol group mediates antioxidant and detoxification activity, allowing glutathione to function as a reducing agent and nucleophile.
Glutathione Research
L-Glutathione is widely used in biochemical and cellular research. Common applications include:
- Research on antioxidant defense and oxidative stress
- Glutathione S-transferase and Phase II detoxification studies
- Apoptosis pathways and mitochondrial redox balance
- Models of liver injury, aging, and neurodegeneration
- Immune response and inflammation experiments
- Cellular response to toxins and radiation
The 600 mg format allows multiple experiments with minimal material waste.
Mechanism of Action
L-Glutathione maintains redox homeostasis through multiple pathways. It directly neutralizes reactive oxygen and nitrogen species, including hydrogen peroxide, superoxide, and peroxynitrite. GSH also regenerates other antioxidants, including vitamin C, vitamin E, and coenzyme Q10, via redox cycling. It conjugates electrophilic compounds through glutathione S-transferases to form water-soluble products for cellular elimination. Glutathione regulates protein thiol status through glutathionylation cycles and supports the glutathione peroxidase system. Oxidized glutathione (GSSG) is recycled by glutathione reductase using NADPH. A disrupted GSH:GSSG ratio signals oxidative stress in research models.
Preclinical Research Overview
Preclinical studies confirm glutathione’s central role in oxidative protection. In liver injury models, GSH depletion predicts hepatotoxicity, whereas restoration reduces necrosis and supports cellular recovery. In ischemia-reperfusion studies, glutathione decreases lipid peroxidation. Glutathione also reduces the release of inflammatory mediators and is associated with mitochondrial function and cellular longevity in aging studies. It protects against amyloid-beta toxicity in vitro and dopaminergic neuronal loss in neurodegeneration models. Reproductive research shows improved spindle stability and reduced DNA damage, supporting glutathione’s role in oxidative resilience.
Form and Analytical Testing
- Form: Lyophilized powder
- Purity: ≥99% by HPLC
- Identity: Verified by mass spectrometry
- Endotoxin: <0.1 EU/μg
- Storage: 2–8°C, protected from light
- Reconstitution: Sterile or bacteriostatic water
- Stability: 24–36 months sealed; 1–2 weeks after reconstitution
Each batch undergoes third-party analytical verification.
Research Use Only Disclaimer
L-Glutathione 600 mg is sold for research use only and is not approved for human or animal consumption. No therapeutic, diagnostic, or dietary claims are made. Use only in qualified laboratory environments with institutional oversight.
Referenced Citations
- Lu SC. (2013). Glutathione synthesis. Biochimica et Biophysica Acta (BBA) – General Subjects. 1830(5):3143–3153.
- Forman HJ, et al. (2009). Targeting oxidative stress in disease: promise and limitations of antioxidant therapy. Nature Reviews Drug Discovery. 8(7):579–591.
- Pizzorno J. (2014). Glutathione! Integrative Medicine. 13(1):8–12.
- Wu G, et al. (2004). Glutathione metabolism and its health implications. Journal of Nutrition. 134(3):489–492.
- Peptide Sciences product specifications: ≥99% purity, lyophilized form, analytical data available upon request.




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