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Reduced L-glutathione, high-purity reference standard for in vitro laboratory research and analysis.
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Price
$44.96
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Quantity
In Stock · 85 Units Available
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- Third-party HPLC tested. Every lot ships with a batch-linked certificate of analysis naming the laboratory, the method and the measured result. Browse certificates
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Certificate of Analysis & Specifications
HPLC Purity
99.99% HPLC
Area Normalization
Assay Content
1498.96mg
Quantitative Target
Testing Lab
KMD Analytical
Lot Number
KRSGLU-1500-260827-01
Tested Sep 3, 2026
Storage
36°F to 46°F
Retest Date
Sep 2, 2028
Released COA Library
Published Certificates of Analysis for Glutathione. All released analytical records are preserved here. Pending and in-testing lots are reachable only through the QR printed on the vial.
1500mg1 released lot
- View COA
Lot KRSGLU-1500-260827-01
Tested Sep 3, 2026 · KMD Analytical · HPLC 99.99% · Assay 1498.96
Related research materials
Research Data
Chemical & Structural Identifiers
![2D chemical structure of (2S)-2-amino-5-[[(2R)-1-(carboxymethylamino)-1-oxo-3-sulfanylpropan-2-yl]amino]-5-oxopentanoic acid ($\gamma$-L-glutamyl-L-cysteinylglycine)](/structures/glutathione.svg)
- Chemical Name (IUPAC)
- (2S)-2-amino-5-[[(2R)-1-(carboxymethylamino)-1-oxo-3-sulfanylpropan-2-yl]amino]-5-oxopentanoic acid (γ-L-glutamyl-L-cysteinylglycine)
- CAS Registry Number
- 70-18-8 (Reduced monomer form; distinct from oxidized GSSG: 27025-41-8).
- PubChem CID
- 124886
- Molecular Formula
- C10H17N3O6S
- Molecular Weight
- 307.08 Da (307.32 g/mol average).
- Sequence
- H-γ-Glu-Cys-Gly-OH (Isopeptide γ-linkage between Glu and Cys; single-letter: ECG).
- SMILES
- C(CC(=O)N[C@@H](CS)C(=O)NCC(=O)O)[C@@H](C(=O)O)N
- InChIKey
- RWSXRVCMGQZWBV-WDSKDSINSA-N
- Salt / Counter-Ion
- Supplied as a high-purity crystalline free acid or lyophilized reduced zwitterionic solid.
- Synonyms
- Glutathione (reduced), GSH, L-Glutathione, γ-Glu-Cys-Gly, Glutinal.
Analytical & COA Specifications
- Analytical Purity (RP-HPLC)
- ≥ 98.5% by area normalization under UV detection at λ = 214 nm.
- Identity Confirmation (RP-HPLC RT + UV vs. reference)
- Main peak retention time and UV spectrum conform to the reference standard.
- Physical Characterization
- Pure white crystalline powder or lyophilized cake.
Handling & Stability
Storage. Store dry solid desiccated at -20°C to -80°C, protected from atmospheric moisture, ambient air, and direct light.
Solubility. Readily soluble in sterile deoxygenated deionized water (≥ 50 mg/mL) and sterile degassed Phosphate-Buffered Saline (PBS, pH 7.4, ≥ 30 mg/mL) for in vitro assay application.
- Thiol Autoxidation Safeguards: The active cysteinyl sulfhydryl (-SH) group spontaneously oxidizes to form glutathione disulfide (GSSG) in basic or aerated aqueous solutions; prepare assay stock solutions using degassed/nitrogen-sparged buffers, avoid exposure to trace transition metal catalysts (Fe3+, Cu2+), and aliquot into single-use fractions under inert gas at -80°C to eliminate freeze-thaw degradation.
Mechanism & Literature
Atypical Isopeptide Architecture: A non-ribosomal linear tripeptide synthesized enzymatically via glutamate-cysteine ligase (GCL) and glutathione synthetase (GS). The distinct γ-glutamyl linkage links the γ-carboxylate of glutamate to the amino group of cysteine, conferring enzymatic resistance to standard intracellular aminopeptidases and restricting hydrolysis to the membrane-bound enzyme γ-glutamyl transpeptidase (GGT).
Cellular Pathways Investigated: Evaluated across diverse in vitro cellular models (such as primary hepatocytes, cortical neurons, and endothelial cultures) to quantify intracellular redox buffer dynamics (the reduced-to-oxidized GSH:GSSG ratio), co-substrate kinetics with Glutathione Peroxidase (GPx) in lipid hydroperoxide reduction, enzymatic cycling via NADPH-dependent Glutathione Reductase (GR), and Phase II electrophilic metabolite conjugation via Glutathione S-Transferase (GST) isoforms.
References (3)
- Meister, A., & Anderson, M. E. (1983). Glutathione. Annual Review of Biochemistry, 52(1), 711–760.
- Forman, H. J., et al. (2009). Glutathione: overview of its protective roles, measurement, and biosynthesis in vitro. Molecular Aspects of Medicine, 30(1-2), 1–12.
- Lu, S. C. (2013). Glutathione synthesis in cell cultures and regulation of cellular redox signaling. Biochimica et Biophysica Acta (BBA) - General Subjects, 1830(5), 3143–3153.
Technical Laboratory FAQs
Why does Glutathione contain an atypical γ-glutamyl peptide bond?
The γ-carboxyl linkage prevents standard cellular endopeptidases and aminopeptidases from cleaving the N-terminal glutamate residue, rendering GSH stable inside cell assay systems until cleaved by specific γ-glutamyl transpeptidase (GGT) enzymes.
How do laboratory assays monitor the conversion between GSH and GSSG?
Assays utilize enzymatic recycling methods (DTNB/Ellman's reagent coupled with glutathione reductase) or RP-HPLC with electrochemical detection to quantify the concentration of free thiol monomer (GSH) relative to the disulfide dimer (GSSG).
What buffer conditions prevent autoxidation of reduced Glutathione in vitro?
Using deoxygenated, nitrogen-purged buffers at neutral to slightly acidic pH (pH 6.5--7.0) and adding low concentrations of a metal-chelating agent (such as EDTA) prevents transition-metal-catalyzed oxidation to GSSG.
For Research Use Only. Not for human or animal administration. Not intended to diagnose, treat, cure, or prevent any disease. Sold for laboratory research purposes only.