glutathione reductase enzyme Team:UNSW Australia/Model/Glutathione System Glutathione Reductase belongs to the homodimericFAD−disulfide oxidoreductases family Glutathione reductase catalytic cycle |
Description
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Glutathione (L--glutamyl-L-cysteinyl-glycine) is the primary intracellular antioxidant tripeptide, functioning as a substrate for glutathione peroxidase (GPx) and glutathione S-transferase (GST) enzymes in redox homeostasis and xenobiotic detoxification research models

Key Scientific Attributes High-purity Survodutide (98% by HPLC/MS, acetate salt form) Verified 29-amino-acid glucagon-based sequence with C18 diacid lipidation Lyophilized formulation for maximum long-term stability Full Certificate of Analysis (COA) with HPLC, MS, receptor-binding assays (GLP-1R/GCGR EC50), and endotoxin testing Manufactured in GMP-aligned, ISO-compliant facilities Suitable for dual-agonist receptor signaling studies and related in vitro pathway research Research Context (Based on published clinical/preclinical literature
