Glutathion hætteglas 1500 mg

Glutathion (GSH) er et naturligt forekommende tripeptid, kemisk set et thiolholdigt γ-glutamylpeptid. I videnskabelig forskning studeres det som en modelforbindelse til redoxbiokemi og enzymologi og som en referencestandard i analytisk arbejde. Denne forbindelse tilbydes som et frysetørret pulver på 1500 mg pr. hætteglas, udelukkende til laboratorie- og forskningsformål.

Hvad er glutathion?

Glutathion (γ-L-glutamyl-L-cysteinyl-glycin) er et tripeptid sammensat af aminosyrerne glutaminsyre, cystein og glycin med sekvensen γ-Glu-Cys-Gly. Det er karakteriseret ved en usædvanlig γ-peptidbinding: glutamatresten er bundet til cystein via dens sidekæde i stedet for α-carboxylgruppen, hvilket gør molekylet resistent over for de fleste almindelige aminopeptidaser. Den frie thiolgruppe i cysteinresten danner den reaktive kerne. Det er netop denne kombination af en atypisk peptidbinding og en fri sulfhydryl, der gør glutathion til et meget anvendt modelmolekyle inden for peptidkemi og thiolbiokemi.

I forskningsmodeller spiller forbindelsen en central rolle i GSH/GSSG redox-parret: in vitro kan to GSH-molekyler danne en disulfidbro til den oxiderede dimer GSSG, som derefter omdannes tilbage til den reducerede form af NADPH-afhængig glutathionreduktase. Derudover fungerer glutathion i cellemodeller som en cofaktor for glutathionperoxidaser og som et substrat for glutathion S-transferaser, som kobler thiolgruppen til ikke-polære elektrofiler. Biosyntesen forløber i to ATP-afhængige trin via glutamatcysteinligase og glutathionsyntetase, der tilsammen danner kernen i γ-glutamylcyklussen. Derfor anvendes glutathion som modelforbindelse og referencestof i videnskabelig forskning.

Forskningsområder

I laboratoriesammenhæng forekommer glutathion blandt andet inden for følgende forskningsområder:

• Enzymologisk undersøgelse af glutathionperoxidaser, glutathionreduktase og glutathion S-transferaser og deres substratspecificitet in vitro.
• Modelstudier af GSH/GSSG redoxparret og bestemmelse af det intracellulære redoxpotentiale i isolerede cellekultursystemer.
• Forskning i S-glutathionylering af cysteinrester i proteiner som en posttranslationel modifikation i cellemodeller.
• Biokemiske studier af γ-glutamylcyklussen, glutamat-cysteinligase og kinetikken af ​​totrinsbiosyntese.
• Analytical method development and validation (HPLC, LC-MS, thiol varitization) using glutathione as the reference standard.
• Stability and solubility studies of thiol-containing peptides and their oxidation behavior under controlled conditions.

Hver af disse anvendelser involverer kontrolleret laboratorie- eller præklinisk modelforskning.

Glutathione in our research assortment

Glutathione falls under the category of freeze-dried research peptides in vial form within our range. Researchers working with this category frequently combine the compound with other peptides studied via their own biochemical targets. While Glutathione focuses on thiol chemistry and redox-dependent enzyme systems, other components within the same product line have been specifically chosen to cover receptor-linked or signal-mediated targets. These compounds share the freeze-dried vial form but differ fundamentally in amino acid composition and investigated mechanism.

Specifikationer

Form, håndtering og opbevaring

Glutathione is supplied as a freeze-dried powder in a sealed glass vial containing a standardized quantity of 1500 mg. Unlike a solid tablet form, this lyophilisate is intended to be dissolved in a suitable solvent in a laboratory setup before analytical work takes place. The free thiol group is susceptible to oxidation to GSSG in solution; therefore, the compound is offered in freeze-dried form.

Store the vial refrigerated, protected from direct light and moisture, in the original packaging and with the seal intact. Handle the connection with standard laboratory precautions: work in a clean environment, use appropriate personal protective equipment, and prevent cross-contamination with other research materials. Avoid repeated temperature changes and keep the packaging out of reach of unauthorized persons.

Sammensætning og laboratorieresultater

The lyophilisate contains glutathione with a controlled purity of ≥ 99% (HPLC). The vial contains exclusively the freeze-dried compound, without added excipients or preservatives.

Du kan finde en oversigt over den tilgængelige analytiske dokumentation på vores side med laboratorieresultaterRapporterne samles centralt der, så du kan integrere dataene i dine egne forskningsregistre.

Ofte stillede spørgsmål

To which class of substances does glutathione belong?
Glutathione is a tripeptide composed of glutamic acid, cysteine, and glycine. Due to the γ-peptide bond between glutamate and cysteine, it is classified as a γ-glutamyl peptide and not as an ordinary linear peptide.

What is the difference between GSH and GSSG in research?
GSH is the reduced form with a free thiol group; GSSG is the oxidized dimer in which two molecules are linked via a disulfide bridge. The ratio of both forms is used in cell models as a measure of the redox state.

I hvilken form leveres forbindelsen?
As a freeze-dried powder in a sealed vial with 1500 mg per unit. The lyophilized form limits oxidation of the thiol group during storage and transport.

Hvordan opbevarer jeg hætteglasset?
Refrigerated, protected from light and moisture, preferably in the original packaging with the seal intact.