Glutathione 1200mg

Glutathione (L-Glutathione, GSH, CAS 70-18-8, MW 307.32 Da, molecular formula C₁₀H₁₇N₃O₆S) is a tripeptide (γ-Glu-Cys-Gly) and the most abundant intracellular antioxidant in human cells. Its core function is to neutralise reactive oxygen species (ROS) by donating electrons via its cysteine thiol group. It is regenerated from the oxidised form (GSSG) by glutathione reductase using NADPH — forming the glutathione redox cycle. In research, glutathione is used in oxidative stress models, detoxification assays, cell viability studies, neuroprotection experiments, immune cell function research, and as a reference compound in redox biology. It is one of the most fundamental tools in cellular biochemistry. For research use only.

GSH (reduced glutathione) is the active antioxidant form with a free thiol group (-SH) on the cysteine residue. It donates electrons to neutralise ROS and is regenerated by glutathione reductase. GSSG (oxidised glutathione) is the disulphide-linked dimer formed when two GSH molecules donate electrons. The GSH:GSSG ratio is the primary cellular redox state marker — a high ratio indicates a healthy, reduced cellular environment; a low ratio indicates oxidative stress. Our product is the reduced form (GSH). For accurate redox research, reconstituted GSH should be stored under inert conditions to minimise spontaneous oxidation to GSSG. Not for human consumption — for research use only.

GSH oxidises spontaneously when its thiol group reacts with atmospheric oxygen to form GSSG. This is accelerated by heat, light, metal ion catalysts (Cu²⁺, Fe³⁺), alkaline pH, and air exposure. To minimise oxidation: store lyophilised powder at −20°C in the dark; reconstitute only the volume needed; acidify the solution to pH 5–6 if protocol allows; store reconstituted solution under nitrogen gas if possible; avoid repeated freeze-thaw cycles. For in-vitro assays, prepare fresh working solutions on the day of the experiment. Yellowing of the reconstituted solution indicates oxidation — discard if colour has changed. Not for human consumption — for research use only.

Glutathione is used across many in-vitro and in-vivo research models: hepatocyte toxicity and drug-induced liver injury assays (DILI models); glutathione S-transferase (GST) enzyme activity assays; lymphocyte proliferation and NK cell activity studies; GSSG/GSH ratio measurement by DTNB assay or LC-MS/MS; neuronal oxidative damage models (Parkinson's, Alzheimer's preclinical models); cardiomyocyte ischaemia-reperfusion injury experiments; skin cell UV-radiation damage models; and mitochondrial glutathione (mGSH) research in ageing. It is also used as a positive control in antioxidant capacity assays (ORAC, FRAP, ABTS). Not for human consumption — for research use only.

Reconstitution: Glutathione is highly water-soluble. Draw the required volume of bacteriostatic water and inject slowly into the vial; swirl gently. For a 1200mg vial: 12mL BAC water = 100mg/mL; 24mL = 50mg/mL. Reconstituted glutathione is susceptible to oxidation — work quickly, minimise air exposure, store in the dark at 2–8°C, and use within 2 weeks. For long-term storage of reconstituted solution, aliquot into single-use volumes and freeze at −80°C under inert gas where possible. Discard if the solution has yellowed. Not for human consumption — for research use only.

Glutathione is legal to purchase in Australia for legitimate laboratory research purposes. As an endogenous tripeptide naturally produced by the body, it is not a scheduled substance when sold for research use. Purchasers must confirm research-only use. Our Glutathione 1200mg is supplied as a research compound with 99.0% HPLC purity and full COA documentation. Peptide Warehouse dispatches nationwide from our Melbourne warehouse via Australia Post. Not for human consumption in this lyophilised research form.

Glutathione (L-Glutathione, reduced) has CAS number 70-18-8, molecular formula C₁₀H₁₇N₃O₆S, and molecular weight 307.32 Da. Its structure is a tripeptide linked by a conventional peptide bond (Cys-Gly) and an unusual gamma-peptide bond (γ-Glu to α-amino of Cys). The gamma bond is resistant to most intracellular peptidases — a key reason for glutathione's stability within cells. Identity is confirmed in our batches via mass spectrometry as documented in the COA. Not for human consumption — for research use only.