Longevity · Lyophilized Powder
L-Glutathione (Reduced, GSH) - 600mg Vial
CAS: 70-18-8 | Sequence: Tripeptide γ-Glu-Cys-Gly | Purity: ≥99.2%
49.99 / vial
Pre-Order - First Batch in Final QC
- Cold Storage −20 °C lyophilized
- Reconstituted 2–8 °C · 28 days
- HPLC ≥99.2% third-party verified
SKU PT-GSH-600 · HPLC + MS tested every batch · Insulated cold-pack shipping
What Is Glutathione?
L-Glutathione in its reduced form (GSH) is an endogenous tripeptide of 307.32 g/mol built from γ-L-glutamate, L-cysteine and glycine. It is the dominant intracellular thiol antioxidant, present at millimolar concentrations in most cell types, and the GSH/GSSG ratio is the conventional measure of a cell's redox state.
Its defining structural feature is the γ-glutamyl linkage: the glutamate joins through its side-chain carboxyl rather than its α-carboxyl. That makes glutathione invisible to ordinary peptidases, so its degradation runs through a dedicated extracellular enzyme, γ-glutamyl transpeptidase. The free cysteine thiol does the redox and conjugation chemistry.
Supplied as 600 mg of white lyophilized powder at ≥99.2% HPLC purity with a batch-specific third-party COA. The thiol oxidizes in air, so prepare solutions fresh. The first production batch is in final QC; request the certificate below.
Request the Full HPLC Report
The first production batch of Glutathione is in final QC. Ask for the complete HPLC and mass-spec package and we will email it the moment the certificate is released.
For laboratory research use only. We do not provide dosing guidance or medical advice.
Glutathione Scientific Documentation
Technical reference data and a summary of published preclinical literature, provided for educational purposes.
| Name | L-Glutathione, reduced (GSH) |
|---|---|
| Synonyms | GSH, reduced glutathione, γ-glutamylcysteinylglycine |
| CAS Number | 70-18-8 |
| Molecular Formula | C10H17N3O6S |
| Molecular Weight | 307.32 g/mol |
| Sequence (3-letter) | γ-L-Glutamyl-L-cysteinyl-glycine |
| Sequence (1-letter) | γE-C-GThe glutamate is linked through its γ-carboxyl, not the usual α-carboxyl — which is why standard peptidases do not cleave it and why it is written γ-Glu rather than Glu. |
| Structure Class | Endogenous tripeptide with an unusual γ-glutamyl peptide bond and a free, redox-active cysteine thiol |
| Form | White lyophilized powder |
| Purity | ≥99.2% (RP-HPLC); identity confirmed by LC-MS |
| Content per Vial | 600 mg net peptide |
| Solubility | Freely soluble in water; solutions oxidize readily on standing and should be prepared fresh under low-oxygen conditions where possible |
| Storage Conditions | Lyophilized: −20 °C, desiccated and protected from light. Reconstituted: 2–8 °C, use within 28 days. The free thiol oxidizes to GSSG on air exposure; keep the vial tightly sealed and make up solutions immediately before use. |
The Cell's Principal Thiol Buffer
Glutathione is the most abundant low-molecular-weight thiol in most cells, present at millimolar concentrations. The GSH/GSSG ratio is the standard readout of intracellular redox state, and maintaining it is the job of glutathione reductase working at NADPH's expense.
The γ-Glutamyl Bond
The glutamate residue is joined through its γ-carboxyl group rather than the α-carboxyl found in ordinary peptide bonds. This single structural quirk makes glutathione resistant to normal intracellular peptidases, and its turnover instead requires γ-glutamyl transpeptidase at the cell surface.
Conjugation and Detoxification
Glutathione S-transferases conjugate GSH to electrophilic xenobiotics, forming mercapturic acid precursors for excretion. This phase II conjugation chemistry is why glutathione depletion is a standard endpoint in toxicology assays.
Analytical Handling
The free thiol oxidizes to the disulfide GSSG on exposure to air, so a purity figure is only meaningful at the time of testing. Prepare solutions immediately before use; where the GSH/GSSG ratio is the measurement, degas the buffer and work quickly.
Limitations
Reported bioavailability of orally or systemically administered glutathione is a long-standing point of dispute, and much consumer-facing material overstates it. For in-vitro work this is irrelevant; for any model system it is a design consideration.
Representative literature: Meister A, Anderson ME, Annu Rev Biochem 1983;52:711-760; Lu SC, Mol Aspects Med 2009;30:42-59; Forman HJ, Zhang H, Rinna A, Mol Aspects Med 2009;30:1-12.
Bacteriostatic Water Ratio Chart (600 mg Vial)
| Diluent Added | Concentration | Per 0.1 mL Aliquot |
|---|---|---|
| 1.0 mL | 600.0 mg/mL | 60 mg |
| 2.0 mL | 300.0 mg/mL | 30 mg |
| 2.5 mL | 240.0 mg/mL | 24 mg |
| 3.0 mL | 200.0 mg/mL | 20 mg |
| 5.0 mL | 120.0 mg/mL | 12 mg |
Reconstitution Procedure
Allow the vial to reach room temperature. Introduce sterile or bacteriostatic water slowly down the inner glass wall — do not inject directly onto the powder cake. Swirl gently until fully dissolved; do not shake or vortex, as this can promote aggregation.
Temperature Stability
| State | Condition | Typical Stability |
|---|---|---|
| Lyophilized | −20 °C, desiccated | 24+ months |
| Lyophilized | 2–8 °C | Up to 12 months |
| Lyophilized | Room temp (≤25 °C) | Several weeks (transit) |
| Reconstituted | 2–8 °C | Up to 28 days |
| Reconstituted | −20 °C aliquots | Avoid repeated freeze–thaw |
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