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L(-)-Glutathion (reduzierte Form) ≥98%, weißgraues Puder

Lieferant: MP Biomedicals

Beschreibung: 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.

L(-)-Glutathione (reduced form) ≥96%, reduziert

Artikel-Nr: (SPCMGL146-25GM)

Lieferant: Spectrum Chemical

Hersteller Artikel Nummer : GL146-25GM

Beschreibung: L-Glutathione, Reduced can also be referred to as GSH and is an organic chemical that can be traced in plants and animals alike. It is an antioxidant that prevents damage from reactive oxygen species to cellular components that are important. It can be used to raise levels of plasma and liver GSH concentrations and is thought to have some positive effects on reducing cancer development.

UOM: 1 * 25 mg

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L(-)-Glutathion (reduzierte Form) ≥98%, weißgraues Puder Reagenz für die Zellkultur

Lieferant: MP Biomedicals

Beschreibung: 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.