Glutathione oxidized disodium, a fundamental compound in the biomedical field, embraces paramount significance for myriad diseases and ailments. Its pivotal function lies in preserving cellular homeostasis through its antioxidative and detoxifying abilities.
CAT No: R1994
CAS No:103239-24-3
Chemical Name:disodium;(2S)-2-amino-5-[[(2R)-3-[[(2R)-2-[[(4S)-4-amino-4-carboxylatobutanoyl]amino]-3-(carboxylatomethylamino)-3-oxopropyl]disulfanyl]-1-(carboxylatomethylamino)-1-oxopropan-2-yl]amino]-5-oxopentanoate;hydron
Glutathione oxidized disodium is a biochemical compound widely recognized for its role as the disodium salt form of oxidized glutathione (GSSG), a crucial redox-active tripeptide in cellular metabolism. As the oxidized counterpart of reduced glutathione (GSH), it serves as an important indicator and modulator of oxidative stress in biological systems. Its unique redox properties and water solubility make it an essential reagent in a variety of biochemical, molecular biology, and cell-based research applications. The compound is particularly valued for its involvement in studies of redox regulation, enzymatic activity, and antioxidant defense mechanisms, underpinning its relevance across diverse fields such as biochemistry, cell biology, and pharmaceutical research.
Redox biology research: In the context of redox biology, oxidized glutathione disodium is extensively utilized to investigate the cellular redox state and thiol-disulfide exchange processes. Its presence and quantification enable researchers to assess the oxidative environment within cells and tissues, providing critical insights into the balance between oxidants and antioxidants. By manipulating intracellular levels of GSSG, scientists can model oxidative stress conditions, study the impact on redox-sensitive signaling pathways, and elucidate the mechanisms underlying cellular responses to oxidative damage.
Enzyme activity assays: The compound plays a pivotal role in enzymatic studies, particularly those involving glutathione-dependent enzymes such as glutathione reductase and glutathione peroxidase. As a substrate or product in these enzymatic reactions, oxidized glutathione disodium is used to monitor enzyme kinetics, catalytic efficiency, and inhibition profiles. Its inclusion in assay systems allows for the detailed characterization of enzyme function, supports the development of high-throughput screening protocols, and aids in the identification of novel modulators of glutathione metabolism.
Protein folding and disulfide bond formation: In protein biochemistry, GSSG disodium salt is frequently employed as an oxidizing agent to facilitate the formation of disulfide bonds during in vitro protein folding experiments. The compound's ability to promote disulfide exchange makes it invaluable for refolding recombinant proteins expressed in prokaryotic systems, where correct disulfide bond formation is essential for biological activity. By providing a controlled oxidative environment, it enables optimization of folding conditions and enhances the yield of properly folded, functional proteins.
Cell culture and oxidative stress modeling: In cell-based research, oxidized glutathione is used to modulate the redox environment of cultured cells, thereby enabling the study of oxidative stress-induced cellular responses. Treatment with GSSG can mimic pathological oxidative conditions, allowing investigation of signal transduction pathways, gene expression changes, and adaptive mechanisms activated under stress. This application is particularly relevant in the study of neurodegeneration, aging, and toxicology, where oxidative imbalance plays a central role.
Analytical chemistry and metabolomics: The compound is also incorporated into analytical methodologies for the quantification of glutathione redox status in biological samples. Its use as a calibration standard or spike-in control in high-performance liquid chromatography (HPLC), mass spectrometry, or capillary electrophoresis facilitates accurate measurement of GSSG and GSH levels. These quantitative assessments are vital for evaluating oxidative stress biomarkers, monitoring disease progression in research models, and validating the efficacy of antioxidant interventions in preclinical studies.
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