Glutathione

What is Glutathione (Reduced GSH)?

Glutathione (known chemically as Reduced Glutathione, GSH, or γ-L-glutamyl-L-cysteinylglycine) is the most abundant low-molecular-weight non-protein thiol tripeptide found in mammalian cells. Synthesized sequentially via γ-glutamylcysteine synthetase and glutathione synthetase, Glutathione features an atypical peptide bond between the γ-carboxyl group of glutamate and the amine group of cysteine, rendering it resistant to degradation by intracellular peptidases.

Operating as the master regulator of the intracellular redox buffer, Glutathione maintains the functional ratio between reduced GSH and oxidized glutathione disulfide (GSSG). Through enzymatic catalysis via Glutathione Peroxidase (GPx), GSH donates reducing equivalents to neutralize hydrogen peroxide (H2O2) and organic lipid hydroperoxides. Concurrently, it serves as an indispensable co-substrate for Glutathione S-Transferases (GST) during Phase II electrophilic metabolite detoxification.

Batch-verified for high analytical purity at NobleChems, Glutathione is supplied across three distinct formats tailored to specific laboratory workflows:

• 600mg Lyophilized Solid Vials

• 1500mg Lyophilized Solid Vials

• 4000mg (200mg/mL x 20mL) Aqueous Solution of 0.9% Benzyl Alcohol and Sterile Water

Researchers evaluate Glutathione alongside complementary metabolic and redox reference standards available on the site, such as S-Acetyl-L-Glutathione, NAD+, NAD+ / Carnitine Based Amino Blend, and Methylene Blue.

Chemical and Molecular Data

What are the Mechanisms of Action?

The biochemical pathways and cellular targets of Glutathione (Reduced GSH) in laboratory research include:

• Direct Free Radical Quenching & GPx Redox Cycling: GSH donates reducing hydrogen equivalents from its active cysteine sulfhydryl (-SH) group to reduce reactive oxygen species (ROS), hydroxyl radicals, and lipid hydroperoxides. Glutathione Peroxidase (GPx) couples this reaction to form oxidized glutathione disulfide (GSSG), which is subsequently regenerated back to 2 GSH molecules by NADPH-dependent Glutathione Reductase (GR).

• Phase II Xenobiotic Conjugation via GST Enzymes: Cytosolic and microsomal Glutathione S-Transferases (GST) catalyze the nucleophilic attack of the GSH thiolate anion on electrophilic compounds, xenobiotics, and peroxidized lipid breakdown products (such as 4-hydroxynonenal). This forms polar mercapturic acid precursors targeted for active cellular export.

• Protein S-Glutathionylation & Thiol Proteome Defense: Reversible formation of mixed disulfides between GSH and protein cysteine thiols (S-glutathionylation) protects sensitive structural and signaling proteins from irreversible oxidative sulfonylation, modulating enzyme activity and preserving mitochondrial membrane integrity during oxidative stress.

• Mitochondrial Membrane Potential Maintenance: Mitochondrial matrix GSH pools prevent cardiolipin oxidation and Complex I/III electron leakage, maintaining inner mitochondrial membrane potential (ΔΨm) and suppressing apoptosis-inducing cytochrome c release.

What do Preclinical & Academic Studies Show for Glutathione?

When evaluating published scientific literature and bioenergetic monographs for Glutathione (GSH):

• Intracellular Redox Homeostasis & Kinetics (PubMed): Peer-reviewed monographs on PubMed (PMID: 14988435) document how the GSH/GSSG ratio functions as the primary metabolic indicator of cellular oxidative stress, apoptosis susceptibility, and mitochondrial vitality.

• Mitochondrial Defense & Cytoprotection (PMC): Comprehensive biomedical reviews archived in PMC (PMC4684116) detail the role of mitochondrial glutathione transport in protecting neural, hepatic, and vascular endothelial cells from lipid peroxidation and ischemic insult.

• Chemical Profiling & Molecular Verification (PubChem): Official structural characterization maintained on PubChem verifies the molecular mass (307.32 g/mol), γ-glutamyl peptide geometry, and HPLC mass spectrometry profile of CAS 70-18-8.

How does Glutathione compare across formats and related compounds?

To select optimal reference standards for specific laboratory assays, researchers compare the physical formats of Glutathione alongside related thiol modulators available at NobleChems:

Lyophilized Vials (600mg / 1500mg) vs. 200mg/mL Pre-Mixed Liquid Solution (20mL)

• Lyophilized Solid Vials (600mg & 1500mg): High-purity dry cake format engineered for extended benchtop shelf life and precise gravimetric mass preparation. Ideal for long-term storage and customized concentration assay setups where solid-state stability is critical.

• 200mg/mL Pre-Solubilized Liquid Solution (20mL Vial / 4,000mg Total): High-density, ready-to-pipette aqueous solution. Provides immediate volumetric sampling and high total active mass (4,000mg) for high-throughput cell culture, multi-well microplate dosing, and high-volume enzymatic assays.

Frequently Asked Questions (FAQs)

1. Is NobleChems a reliable place to buy Glutathione?

Yes, NobleChems is a highly trusted vendor for high-purity research chemicals and reference peptides. Every batch of Glutathione (across both lyophilized solid and pre-solubilized liquid formats) undergoes strict third-party analytical testing (including HPLC and Mass Spectrometry) to verify minimum 98%+ chemical purity, correct molecular weight (307.32 g/mol), exact concentration accuracy, and complete absence of heavy metals or synthesis impurities.

2. What is Glutathione and what is its primary biological role?

Glutathione (Reduced GSH) is a tripeptide composed of glutamate, cysteine, and glycine with an atypical γ-glutamyl bond. It functions as the primary endogenous intracellular antioxidant and redox buffer in mammalian cells.

3. How does Glutathione participate in cellular redox cycling?

GSH donates electrons to reduce peroxides via Glutathione Peroxidase (GPx), forming oxidized glutathione disulfide (GSSG). Glutathione Reductase (GR) then uses NADPH to reduce GSSG back to two active GSH molecules, maintaining redox equilibrium.

4. What formats of Glutathione are available from NobleChems?

NobleChems supplies Glutathione in three distinct formats: 600mg lyophilized solid vials, 1500mg lyophilized solid vials, and a high-density 200mg/mL pre-solubilized liquid solution in a 20mL glass vial (4,000mg total active compound).

5. What role does Glutathione play in Phase II cellular detoxification?

Glutathione S-Transferases (GST) catalyze the binding of GSH’s nucleophilic sulfur atom to toxic electrophiles, xenobiotics, and oxidized lipid intermediates, converting them into water-soluble conjugates for cellular export.

6. How does Reduced Glutathione compare to S-Acetyl-L-Glutathione (SAG)?

Standard Reduced Glutathione is the native tripeptide used for direct in vitro antioxidant and enzymatic assays. S-Acetyl-L-Glutathione features an attached acetyl group that protects the thiol from oxidation and enhances passive lipid membrane permeability in cell culture models.

7. How does NobleChems verify the chemical purity and mass identity of Glutathione?

NobleChems utilizes High-Performance Liquid Chromatography (HPLC) to confirm active chemical purity exceeding 98% and Mass Spectrometry (MS) to verify exact molecular weight (307.32 g/mol) and active concentration prior to batch release.

8. What are the recommended storage parameters for Glutathione vials?

Lyophilized Glutathione vials should be stored tightly sealed in a cool, dry environment (15°C to 25°C) or refrigerated for extended shelf life. The 200mg/mL liquid solution should be kept between 2°C and 8°C (35°F – 43°F) and protected from direct light exposure to prevent auto-oxidation to GSSG.

Disclaimer: All compounds and research materials provided by NobleChems are strictly for laboratory and research professional use only. They are not approved for human or animal use nor consumption by the Food and Drug Administration (FDA). These products should not be used for any form of in vivo experimentation or for any other non-laboratory purpose. Any violation or indication of human or animal use will result in immediate removal from being able to purchase products in the future. By purchasing these products, you acknowledge that they will be used exclusively within a controlled and qualified research environment.