Glutathione

Reduced glutathione (GSH; CAS 70-18-8; MW 307.3 g/mol) is the primary intracellular antioxidant tripeptide (Glu-Cys-Gly) central to oxidative stress research, detoxification pathway investigation, immune cell function, and mitochondrial protection studies. The 1500mg vial size supports comprehensive multi-protocol research applications requiring robust antioxidant capacity.

Glutathione functions as the cell's master antioxidant, existing in high concentrations (millimolar range) within virtually all cells. Its unique gamma-glutamyl linkage provides resistance to standard peptidases, allowing it to maintain stability in the intracellular environment. The cysteine thiol group serves as the active redox center, cycling between reduced (GSH) and oxidized (GSSG) forms to neutralize reactive oxygen species (ROS) and maintain cellular redox homeostasis.

In research applications, glutathione is essential for studying oxidative stress responses, phase II detoxification enzyme activity, and cellular defense mechanisms. It serves as a critical cofactor for glutathione peroxidases and glutathione S-transferases, enzymes that detoxify peroxides and electrophilic compounds. The GSH:GSSG ratio is a widely accepted biomarker of cellular oxidative stress and redox status.

Glutathione's roles extend beyond direct ROS scavenging to include regulation of cell proliferation, apoptosis, immune function, and mitochondrial integrity. It maintains protein thiol groups in their reduced state, protecting against oxidative damage and preserving enzymatic function. The 1500mg quantity provides sufficient material for extensive research protocols examining antioxidant defense systems, redox signaling, and cytoprotective mechanisms.

The following compounds operate through distinct, non-overlapping mechanisms that complement this product's research pathways. Each is independently available from the General Peptide catalog.