L(-)-Glutatione (forma ridotta)

Supplier: Merck

L(-)-Glutatione (forma ridotta), Supelco®

Supplier: Enzo Life Sciences

L(-)-Glutatione (forma ridotta)

Supplier: VWR Chemicals

L(-)-Glutatione (forma ridotta) ≥98%, purissimo

Supplier: Cayman Chemical

L(-)-Glutatione (forma ridotta)

Supplier: Cayman Chemical

L(-)-Glutatione (forma ridotta)

Supplier: Abcam

Reduced Glutathione (GSH), Endogenous antioxidant. Achieve your results faster with highly validated, pure and trusted compounds.

Supplier: Thermo Fisher Scientific

L(-)-Glutatione (forma ridotta) 98% per analisi, reduced

Supplier: PanReac AppliChem

L(-)-Glutatione (forma ridotta)

Supplier: Thermo Fisher Scientific

L(-)-Glutatione (forma ridotta) ≥97%

Supplier: Apollo Scientific

L(-)-Glutatione (forma ridotta)

Supplier: Apollo Scientific

L-Glutathione reduced

Supplier: Thermo Fisher Scientific

L(-)-Glutatione (forma ridotta) ≥98%

Supplier: Merck Millipore (Calbiochem‎)

L(-)-Glutatione (forma ridotta), Millipore®

Supplier: MERCK PRODUCTION CHEMICALS

L(-)-Glutatione (forma ridotta) 98.0-101.0% (by iodometry), EMPROVE® EXPERT Ph. Eur. per la produzione biofarmaceutica, SAFC®

Supplier: MP Biomedicals

Storage: Store at +4 °C, store under nitrogen
Glutathione is the major low molecular weight thiol compound of the living plant or animal cell. It is a tripeptide with a gamma peptide linkage between the amine group of cysteine (which is attached by normal peptide linkage to a glycine) and the carboxyl group of the glutamate side-chain. It is an antioxidant, preventing damage to important cellular components caused by reactive oxygen species such as free radicals and peroxides. The sulfhydryl (thiol) group (SH) of cysteine serves as a proton donor and is responsible for the biological activity of glutathione.
Glutathione suppresses human immunodeficiency virus expression in chronically infected monocytic cells. It is a useful tripeptide involved in many aspects of metabolism, including transport of g-glutanyl amino acids and reductive cleavage of disulfide bonds.
Endogenous antioxidant that plays a major role in reducing reactive oxygen species formed during cellular metabolism and the respiratory burst. Glutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer agents.

Supplier: MP Biomedicals

Glutathione suppresses human immunodeficiency virus expression in chronically infected monocytic cells. It is a useful tripeptide involved in many aspects of metabolism, including transport of g-glutamyl amino acids and reductive cleavage of disulphide bonds.