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Research Use Only. This product is intended exclusively for laboratory research purposes. Not for human consumption, medical use, or veterinary use. No dosing or administration instructions are provided.
Glutathione (L-Glutathione Reduced, GSH) | Research Grade | 600mg
$69.99
L-Glutathione Reduced (GSH) — endogenous tripeptide (γ-Glu-Cys-Gly) and primary cellular redox buffer designed for laboratory research into oxidative stress, antioxidant defense, and redox signaling. ≥99% purity, HPLC-verified, with independent third-party Certificate of Analysis. For laboratory research use only. Not for human consumption.
50 in stock
≥99% PURE (HPLC)
THIRD-PARTY TESTED
COA INCLUDED
USA MANUFACTURED
THIRD-PARTY TESTED
COA INCLUDED
USA MANUFACTURED
Product Overview
Glutathione (GSH, L-Glutathione Reduced) is an endogenous tripeptide composed of γ-glutamyl-cysteinyl-glycine. As the principal low-molecular-weight thiol redox buffer in eukaryotic cells, glutathione serves as a fundamental biological research tool for investigating oxidative stress responses, antioxidant enzyme systems, and cellular redox homeostasis in controlled laboratory settings.
Supplied as the biologically active reduced form (GSH) containing a free sulfhydryl (-SH) group. Every order is accompanied by an independent third-party verified Certificate of Analysis with a unique authentication key for direct lab verification.
Research Applications
Glutathione is intended for use in qualified laboratory research environments, including:
- Oxidative stress and cellular redox balance modeling
- Glutathione peroxidase (GPx) and reductase (GR) enzyme kinetics
- Phase II xenobiotic metabolism and GST conjugation studies
- Redox signaling and reversible protein S-glutathionylation
- Mitochondrial redox homeostasis and cell death cascade research
Mechanism of Action
Glutathione (GSH) functions as the principal cellular redox buffer, maintaining intracellular redox potential by cycling between its monomeric reduced state (GSH) and its dimeric oxidized state (GSSG). GSH serves as an essential electron donor for glutathione peroxidase enzymes (GPx1-GPx8), reducing hydrogen peroxide and organic hydroperoxides to water and corresponding alcohols. NADPH-dependent glutathione reductase (GR) continuously regenerates GSH from GSSG, maintaining a high physiological GSH:GSSG ratio (>100:1). GSH also acts as a nucleophilic substrate for glutathione S-transferase (GST) enzymes, facilitating Phase II conjugation of electrophilic xenobiotics for cellular efflux. Additionally, GSH modulates redox signaling via reversible S-glutathionylation of protein cysteine residues, acting as a dynamic post-translational switch in signal transduction.
Product Specifications
| Specification | Value |
|---|---|
| Compound | L-Glutathione Reduced (GSH) |
| Compound Name | γ-L-Glutamyl-L-cysteinyl-glycine |
| CAS Number | 70-18-8 |
| Structure | Tripeptide (γ-Glu-Cys-Gly) |
| Molecular Formula | C₁₀H₁₇N₃O₆S |
| Molecular Weight | 307.32 g/mol |
| Form | Reduced (GSH, free thiol) — not oxidized (GSSG) |
| Purity | ≥99% (HPLC-verified) |
| Physical Form | Lyophilized powder |
| Appearance | White to off-white crystalline powder |
| Net Content | 600mg |
| Manufacturing | USA-manufactured |
Quality & Testing
Every batch undergoes independent third-party laboratory testing to verify purity, identity, and quality. Each order includes:
- Certificate of Analysis (COA) with unique batch number
- Independent third-party verification key — verifiable directly through the testing laboratory’s online portal
- HPLC purity analysis
- Mass spectrometry identity confirmation
- Endotoxin and microbial contamination screening
“Trust is the most important compound in our catalog.” Every claim about purity, identity, and quality is independently verifiable — not just stated on a label.
Storage & Handling
- Product is supplied in a sterile vial — maintain sterility until use
- Store lyophilized material at -20°C upon receipt
- Protect from moisture and direct light — GSH is hygroscopic and oxidation-sensitive
- Keep vials tightly sealed; exposure to air causes auto-oxidation to GSSG
- Allow vial to equilibrate to room temperature before opening
- Handle in accordance with your institution’s laboratory safety protocols
Frequently Asked Questions
What is glutathione?
Glutathione (GSH, L-Glutathione Reduced) is an endogenous tripeptide composed of γ-glutamic acid, cysteine, and glycine. It is the principal low-molecular-weight thiol redox buffer in eukaryotic cells and a cofactor for multiple antioxidant enzyme systems.
What is the CAS number for glutathione?
The CAS registry number for L-glutathione reduced (GSH) is 70-18-8.
Is glutathione a peptide?
Yes. Glutathione is a tripeptide — a chain of three amino acids (γ-glutamyl-cysteinyl-glycine) linked by peptide bonds. The γ-carboxyl bond between glutamic acid and cysteine is an unusual isopeptide bond.
What is the difference between GSH and GSSG?
GSH (reduced glutathione) is the monomeric active form containing a free sulfhydryl (-SH) group. GSSG (glutathione disulfide) is the oxidized dimeric form created when two GSH molecules donate electrons to neutralize peroxides. The GSH:GSSG ratio is a key indicator of cellular redox status.
How should glutathione be stored?
Store the lyophilized material at -20°C upon receipt. GSH is hygroscopic and oxidation-sensitive — keep vials tightly sealed and protected from direct light and atmospheric humidity to prevent auto-oxidation to GSSG.
Is a Certificate of Analysis included?
Yes. Every order includes a batch-specific Certificate of Analysis with an independent third-party verification key, verifiable directly through the testing laboratory’s online portal.
For laboratory research use only. Not for human consumption.
This product is a laboratory research reagent and is not intended for human consumption, therapeutic use, diagnostic procedures, or veterinary applications. This product has not been evaluated by the FDA. It is not intended to diagnose, treat, cure, or prevent any disease. Researchers must ensure compliance with all applicable institutional, local, and federal regulations prior to use. Must be 21 or older to purchase.
| Weight | 0.1 lbs |
|---|---|
| Dimensions | 4 × 2 × 2 in |
| CAS Number | 70-18-8 |
| Purity | ≥99% |
| Net Content | 600mg |
| Form | Lyophilized |
| Storage Temperature | -20°C |
Certificate of Analysis
COA data for the current batch is being processed. Please check back shortly or contact us with the lot number from your packaging.
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Product Disclaimer
For laboratory research use only. Not for human consumption, medical use, or veterinary use. These products have not been evaluated by the FDA. They are not intended to diagnose, treat, cure, or prevent any disease.
PepperCo Research products are manufactured and tested in accordance with industry standards. All products are accompanied by a Certificate of Analysis (COA) verifying purity and identity. Products are sold without instructions for use, administration, or preparation.
By purchasing, the buyer confirms they are 21 years of age or older and accepts full responsibility for the safe and proper handling of all materials in a laboratory research setting.
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