I. Technical Specifications
- Molecular Formula: C_10H_17N_3O_6S
- Molecular Weight: 307.32 g/mol
- CAS Number: 70-18-8
- Sequence: \gamma-L-Glutamyl-L-cysteinyl-glycine
- Appearance: White Lyophilized Powder
- Solubility: Highly soluble in Water or Bacteriostatic Water
II. Compound Overview
Glutathione (GSH)
is the most abundant low-molecular-weight thiol in eukaryotic cells, known in research as the “Master Antioxidant.”
Its unique structure features a \gamma-peptide bond between the amine group of cysteine and the carboxyl group of the glutamate side chain, a modification that protects the molecule from degradation by standard cellular peptidases. In laboratory models, Glutathione is essential for maintaining the cellular redox state
, protecting organelles from reactive oxygen species (ROS). Taurus Peptides provides this compound in a high-concentration 1500mg
format, vacuum-sealed to prevent premature oxidation into its disulfide form (GSSG).
III. Mechanism of Action (The “Science” Section)
Current literature suggests that Glutathione
functions primarily through its reactive thiol (-SH) group
on the cysteine residue, which acts as a potent electron donor. Researchers observe two primary pathways:
- Direct Antioxidant Defense: GSH directly neutralizes pro-oxidants and free radicals. In this process, two GSH molecules are oxidized to form a disulfide-linked dimer known as Glutathione Disulfide (GSSG). The enzyme Glutathione Reductase then utilizes NADPH to reduce GSSG back to GSH, completing the redox cycle.
- Enzymatic Cofactor: GSH is a mandatory cofactor for Glutathione Peroxidase (GPx), which detoxifies lipid hydroperoxides, and Glutathione S-Transferases (GST), which facilitate the conjugation and excretion of xenobiotics and electrophilic toxins.
Furthermore, researchers are increasingly focused on S-glutathionylation
, a post-translational modification where GSH covalently binds to protein cysteines. This mechanism is thought to protect critical proteins from irreversible oxidation and serve as a “redox switch” for signaling pathways involved in apoptosis and cell cycle regulation.
IV. Observed Research Outcomes
- Redox Buffer Dynamics: Studies observed that the ratio of GSH to GSSG is a definitive biomarker for oxidative stress levels in both in-vitro and animal models.
- Ferroptosis Inhibition: Research indicates that GSH levels are the primary defense against ferroptosis (iron-dependent programmed cell death), as it is required for GPx4 activity to prevent lethal lipid peroxidation.
- Mitochondrial Protection: When evaluated in mitochondrial research, GSH was found to be critical for maintaining the integrity of mitochondrial DNA and the efficiency of the Electron Transport Chain.
V. Storage & Handling
- Storage: Store at -20^\circ C for long-term stability. Lyophilized Glutathione is stable at room temperature for shipping but should be refrigerated or frozen upon receipt. Once reconstituted, use within 7–10 days.
- Handling: Glutathione is sensitive to air (oxidation). Minimize the time the vial remains open and reconstitute with a sterile, pH-neutral diluent. Allow the lyophilized “cake” to reach room temperature before adding liquid to avoid condensation and ensure a clear solution.
