Research use only · Not for human or veterinary use
Each vial ships with structural data and lot identifiers for the compound, plus a Certificate of Analysis documenting purity and identity. Ready for the bench. Synthesized via solid-phase peptide synthesis (SPPS), purified by reverse-phase HPLC, verified by mass spectrometry, and tested for sterility and endotoxin load. Every spec is documented on the signed Certificate of Analysis that ships with your vial.
Glutathione (γ-glutamylcysteinylglycine; GSH) is the most abundant intracellular antioxidant tripeptide in mammalian cells, first identified in yeast by Frederick Gowland Hopkins in 1921. It is synthesized endogenously from glutamate, cysteine, and glycine via two ATP-dependent enzymatic steps catalyzed by glutamate-cysteine ligase (GCL) and glutathione synthetase.
GSH functions as a direct scavenger of reactive oxygen species (ROS) and reactive nitrogen species (RNS), a cofactor for glutathione peroxidase (GPx) enzymes reducing hydrogen peroxide and lipid hydroperoxides, and a substrate for glutathione S-transferases (GSTs) in xenobiotic detoxification. The GSH/GSSG ratio serves as a key indicator of intracellular redox status.
All referenced findings derive from preclinical and published clinical research. This product is for laboratory research use only and is not approved by the FDA for any diagnostic, therapeutic, or preventive use.
Each vial ships with structural data and lot identifiers for the compound, plus a Certificate of Analysis documenting purity and identity. Ready for the bench. Synthesized via solid-phase peptide synthesis (SPPS), purified by reverse-phase HPLC, verified by mass spectrometry, and tested for sterility and endotoxin load. Every spec is documented on the signed Certificate of Analysis that ships with your vial.
Glutathione (γ-glutamylcysteinylglycine; GSH) is the most abundant intracellular antioxidant tripeptide in mammalian cells, first identified in yeast by Frederick Gowland Hopkins in 1921. It is synthesized endogenously from glutamate, cysteine, and glycine via two ATP-dependent enzymatic steps catalyzed by glutamate-cysteine ligase (GCL) and glutathione synthetase.
GSH functions as a direct scavenger of reactive oxygen species (ROS) and reactive nitrogen species (RNS), a cofactor for glutathione peroxidase (GPx) enzymes reducing hydrogen peroxide and lipid hydroperoxides, and a substrate for glutathione S-transferases (GSTs) in xenobiotic detoxification. The GSH/GSSG ratio serves as a key indicator of intracellular redox status.
All referenced findings derive from preclinical and published clinical research. This product is for laboratory research use only and is not approved by the FDA for any diagnostic, therapeutic, or preventive use.
Glutathione: Overview of its protective roles, measurement, and biosynthesis
PubMed · PubMed · 19161420Glutathione dysregulation and the etiology and progression of human diseases
PubMed · PubMed · 19460999At Revvd Research, quality comes first. Our peptides are produced using advanced manufacturing processes and verified through comprehensive testing protocols to deliver dependable results for research applications.
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