GLUTATHIONE

Glutathione is the tripeptide γ-glutamyl-cysteinyl-glycine, and its odd γ-link joins glutamate through its side chain rather than its backbone, which sets it apart from ordinary peptides. The cysteine's free thiol (–SH) is the working part: it donates electrons to neutralize oxidants and to power glutathione peroxidases. That's why the ratio of reduced to oxidized l glutathione is a standard readout of oxidative stress, and why the form in the vial sets the baseline for the whole experiment.

Here's how it goes wrong. In the presence of oxygen and moisture, two GSH molecules link through their sulfur atoms to form GSSG, and a partly oxidized powder can still look perfectly clean. GSSG isn't an impurity in the usual sense; it's glutathione after the reaction your study might be measuring. Titan Core's glutathione is made in the USA as reduced L-glutathione and tested at an independent lab by HPLC, which separates GSH from GSSG, so the starting ratio is measured rather than assumed. The report carries the same LOT number as your vial, and a single LOT covers repeated assays. It's for laboratory research only, not a supplement or cosmetic, and not for human or veterinary use.

Research Highlights

• Mitochondrial import — Loss of the carrier SLC25A39 cut glutathione import into mitochondria without changing total cellular levels, and paired SLC25A40 loss disrupted iron-sulfur proteins (Nature, 2021).
• A built-in feedback loop — The protease AFG3L2 normally degrades SLC25A39; when glutathione runs low, the carrier is spared and mitochondrial uptake rises (Science, 2023).
• Tumor cysteine supply — Extracellular glutathione was abundant around tumors and rescued cancer cells in cystine-deficient conditions through γ-glutamyltransferase activity (Nature, 2026).
• Protein damage repair — LanCL enzymes attach glutathione to damaged dehydroamino acids in proteins, switching off aberrantly activated MEK1 (Cell, 2021).
• Immune positioning — S-geranylgeranyl-L-glutathione was identified as the ligand for receptor P2RY8, which keeps B cells confined in germinal centers (Nature, 2019).
• Ferroptosis control — Ferroptosis had been thought to depend on the glutathione enzyme GPX4 alone; FSP1 was then identified as a glutathione-independent suppressor (Nature, 2019).

FORM: Lyophilized powder (reduced form, GSH)
PURITY: ≥99% (HPLC verified)
SEQUENCE: γ-Glu-Cys-Gly (γ-L-glutamyl-L-cysteinyl-glycine)
MOLECULAR FORMULA: C₁₀H₁₇N₃O₆S
MOLECULAR WEIGHT: 307.3 g/mol
CAS NUMBER: 70-18-8
PRESENTATION: 1500mg
LOT: TC-077-JZ
STORAGE: Keep sealed at 2–8°C (–20°C for long-term), protected from light and moisture.