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Glutathione
1200 mg
$99.99
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Glutathione (GSH) is the tripeptide gamma-glutamyl-cysteinyl-glycine and the most abundant low-molecular-weight thiol in mammalian cells. The reactive thiol on its cysteine residue drives its redox chemistry, making GSH a standard reference compound for researchers studying oxidative-stress balance, the GSH:GSSG ratio, and glutathione-dependent enzyme systems in non-human laboratory models. This 1200mg lyophilized vial is prepared for controlled reconstitution.
Products sold by KÖLD are for Research Use Only. Not intended for human or animal consumption, diagnosis, treatment, or prevention of disease.
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Compounds for studying cellular signaling, repair mechanisms, and longevity-related pathways.
Product Features
Glutathione (GSH) is a tripeptide of L-glutamate, L-cysteine, and glycine. The glutamate joins the cysteine through an unusual gamma-glutamyl bond that resists most peptidases, while the cysteine and glycine are linked by a standard peptide bond. The free thiol on the cysteine residue makes GSH the principal intracellular thiol antioxidant in mammalian cells, typically present at millimolar concentrations. Researchers use it as a reference substrate and electron donor when studying redox homeostasis, glutathione-S-transferase conjugation pathways, and the selenium-dependent glutathione peroxidase system. For in vitro and non-human laboratory research only.
What form of glutathione does KÖLD supply, and what is its structure? KÖLD supplies reduced glutathione (GSH), the tripeptide gamma-glutamyl-cysteinyl-glycine (C10H17N3O6S, about 307 g/mol). Its glutamate connects to cysteine through a gamma-carboxyl bond, and the free cysteine thiol is the reactive site researchers study in redox and conjugation experiments.
How is the GSH:GSSG ratio used in research? Researchers track the ratio of reduced glutathione (GSH) to its oxidized disulfide form (GSSG) as an index of redox state in non-human models. A high ratio indicates a reduced intracellular environment; a falling ratio is a widely cited readout of oxidative stress.
Which enzyme systems is glutathione studied alongside? GSH acts as the electron-donating substrate for selenium-dependent glutathione peroxidase, which reduces peroxides, and as the conjugating thiol for glutathione-S-transferases in detoxification studies. Glutathione reductase then regenerates GSH from GSSG using NADPH, closing the cycle.
Before Reconstitution
Store sealed vial in a freezer at -20°C (–4°F)
Keep away from light and humidity
After Reconstitution
Store at 4°C (39°F)
Use within 14 days
Avoid repeated freeze-thaw cycles
This compound is supplied as a lyophilized powder.
Use KÖLD Solution (sterile, lab-grade solvent) if your protocol requires reconstitution.
Reconstitute only when ready to begin your study.
For research use only. Not for human or animal use.
Not intended to diagnose, treat, cure, or prevent any disease.
“The level of trust and transparency behind this research material is unmatched. It gives me confidence in every study I run.”
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KÖLD peptides
Glutathione
$99.99
Availability: In stock