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Glutathione participates in cellular redox regulation through its reversible oxidation to glutathione disulfide (GSSG), a reaction catalyzed by glutathione peroxidase (GPx) in the presence of reactive oxygen species (ROS), and its regeneration by glutathione reductase (GR) using NADPH as electron donor. Research employing glutathione as a biochemical tool has examined its role in Nrf2/Keap1 pathway regulation, mercapturic acid pathway detoxification, and the maintenance of protein thiol redox status in various cell lines. It is studied in the context of mitochondrial membrane potential maintenance, apoptosis signaling through regulation of caspase activity, and ferroptosis resistance mechanisms linked to GPx4 activity. Glutathione depletion models using this compound as a reference are common in oxidative stress research across hepatocyte, neuronal, and immune cell systems.

SKU GT1500 Category

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Technical Specifications

Product Data

CAS Number 70-18-8
Molecular Wt. 307.32 g/mol
Formula C10H17N3O6S
Purity (HPLC) ≥ 99%
Appearance White lyophilized powder
Quantity 1500 MG

Description & Application

Glutathione (GSH) is an endogenous tripeptide composed of γ-L-glutamyl-L-cysteinyl-glycine and is the most abundant low-molecular-weight thiol antioxidant found in mammalian cells. It functions as a central cofactor in cellular redox homeostasis, xenobiotic detoxification via glutathione S-transferase (GST) conjugation, and free radical scavenging through both enzymatic and non-enzymatic mechanisms. Glutathione is used extensively as a biochemical research reagent and as a reference compound in studies of oxidative stress, thiol biochemistry, and intracellular redox state quantification.

Handling & Storage Protocols

Solubility

Soluble in bacteriostatic water or appropriate solvent.

Temperature

Store refrigerated upon receipt. Long-term: -20°C.

Preparation

Reconstitute strictly under sterile lab conditions.

Integrity

Avoid repeated freeze-thaw cycles. Stable when stored correctly.

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