Glutathione, Reduced

Inquiry

Cat Number

PIPB-0757

CAS Number

70-18-8

If you have any other questions, please contact our experts.

Product Detail Description Scientific Support Advanced Innovations Customer Q&A

CAS Number

70-18-8

EINECS

200-725-4

Storage

Store at 2-8°C

Synonyms

L-Glutathione reduced; L-Glutathione; Glutathion; Isethion; reduced glutathione; Tathion; Glutinal

Molecular Formula

C10H17N3O6S

Molecular Weight

307.33

Smiles

C(CC(=O)N[C@@H](CS)C(=O)NCC(=O)O)[C@@H](C(=O)O)N

Appearance

White crystalline powder

Melting Point

192-195°C (dec.)

Boiling Point

754.5±60.0°C (Predicted)

Relative Density

1.4482 (rough estimate)

General Description

Reduced glutathione (GSH) is a physiologically important tripeptide (γ-L-glutamyl-L-cysteinyl-glycine) that plays many vital roles in cells. It is a major component of the cellular antioxidant defense system and is found at high concentrations in nearly all typical cells.

Mechanism of Action

GSH is a primary antioxidant that can scavenge reactive oxygen species (ROS). It acts as a cofactor for several enzymes, including glutathione reductase, glutathione peroxidases, and peroxiredoxins. Glutathione S-transferases catalyze the conjugation of GSH via its sulfhydryl group to electrophilic centers on a wide variety of substrates, making them more water-soluble for excretion. It plays a vital role in both DNA synthesis and cell repair.

Application

GSH's primary role is cytoprotective. It has been studied for a variety of conditions due to its antioxidant mechanism. Its deficiency has been implicated in neurodegenerative diseases like Parkinson's disease. Clinical applications include use as a protective agent against acute kidney injury in lung cancer patients treated with cisplatin and as a potential therapy for liver diseases to reduce oxidative stress and improve liver function. It is also being investigated for its role in conditions like cystic fibrosis and hyperthyroidism.

This study explored the role of glutathione in trained immunity. Pharmacological ROS inhibition did not affect trained immunity responsiveness in human monocytes, but modulating glutathione levels reduced pro‑inflammatory cytokine production. Single nucleotide polymorphisms in glutathione metabolism genes were associated with altered cytokine production upon trained immunity. Plasma glutathione concentrations positively correlated with ex vivo IL‑1β production in BCG‑vaccinated individuals. Glutathione metabolism is involved in trained immunity induction, warranting further investigation.

Fig. 1 Increased ROS levels of trained monocytes do not contribute to their enhanced pro-inflammatory cytokine production. (Ferreira AV, et al., 2021)

References

Ferreira AV, et al. Glutathione Metabolism Contributes to the Induction of Trained Immunity. Cells. 2021;10(5):971.

This study reveals that CHAC1, a glutathione‑degrading enzyme, is upregulated during glutathione depletion‑induced ferroptosis and acts as a key regulator of protein S‑glutathionylation. CHAC1 deficiency increased glutathione pools, enhanced protein‑SSG, and attenuated hepatocyte ferroptosis in acetaminophen‑treated mice. Quantitative redox proteomics identified ARF6 as a glutathione‑sensitive protein; its S‑glutathionylation decreased during depletion, leading to reduced lysosomal ARF6, increased TFRC membrane localization, and enhanced transferrin uptake. Targeting TFRC with GalNAc‑siTfrc mitigated acetaminophen‑induced liver injury.

Fig. 2 Reduced protein-SSG is associated with decreased glutathione pools by CHAC1 induction in multiple cell types undergoing glutathione deprivation-induced ferroptosis. (Ju Y, et al., 2025)

References

Ju Y, et al. Protein S-glutathionylation confers cellular resistance to ferroptosis induced by glutathione depletion. Redox Biol. 2025;83:103660.

Does Reduced Glutathione require protection from oxygen and light during storage?

Yes, the thiol group is highly sensitive to oxidation, forming disulfide dimers. Store in airtight, light-resistant containers under inert gas (nitrogen) at 2-8°C.

Is Reduced Glutathione stable in aqueous solution for injection or oral use?

Aqueous solutions oxidize rapidly. Use immediately after preparation. Lyophilized powder is preferred for stability.

What is the recommended packaging for Reduced Glutathione to prevent oxidation?

Use amber glass vials with PTFE-lined caps, filled to minimize headspace, and sealed under nitrogen. Aluminum foil overwraps provide additional light protection.

How is the impurity oxidized glutathione (GSSG) monitored during stability?

GSSG is quantified using a stability-indicating HPLC method with electrochemical detection or a validated enzymatic recycling assay, ensuring it remains below specified limits.