G3664
Glutathione Reductase from baker′s yeast (S. cerevisiae)
ammonium sulfate suspension, 100-300 units/mg protein (biuret)
Synonyme(s) :
GR, NAD(P)H:oxidized-glutathione oxidoreductase
Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme
About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.47
Produits recommandés
Forme
ammonium sulfate suspension
Niveau de qualité
Activité spécifique
100-300 units/mg protein (biuret)
Poids mol.
118 kDa
Numéro d'accès UniProt
Activité étrangère
G-6-PDH, 6-PGDH, and NADPH oxidase ≤0.01%
lipoamide dehydrogenase ≤0.1%
Température de stockage
2-8°C
Informations sur le gène
bakers yeast ... GLR1(856014)
Vous recherchez des produits similaires ? Visite Guide de comparaison des produits
Description générale
Glutathione reductase (GLR1) exists in mitochondrial and cytoplasmic isoforms. It shares sequence and structural homology to thioredoxin reductase, and is a flavin-containing oxidoreductase. Its active site is composed of a redox-active disulphide, and it requires NADPH for its catalytic activity. It is a widely present enzyme and is found in plants, bacteria, yeast, mice and humans.
Application
Glutathione Reductase (GR) from baker′s yeast has been used:
- in the glutathione assay to determine glutathione concentration.
- as a standard in the generation of calibration curve.
- as an antigen to measure plasma activity of GR.
Glutathione reductase (GR) from baker′s yeast (Saccharomyces cerevisiae) has been used-
- for quantifying the myocardial tissue glutathione content using a glutathione reductase-5,5′-dithiobis (2-nitrobenzoic acid)-based enzymatic recycling assay
- for the quantification of reduced glutathione (GSH) in the oocytes, using a slightly modified microglutathione assay, obtained from prepubertal gilts
- for the preparation of total GSSG (glutathione disulphide) + GSH measurement, where all available GSSG was reduced to GSH, in rat lens
- for the quantification of intracellular reduced glutathione (GSH) in the oocytes obtained from rats
Actions biochimiques/physiologiques
Glutathione (γ-glutamylcysteinylglycine) is a ubiquitous tripeptide thiol which plays a crucial role in oxidative stress defence mechanism of the cell. Glutathione reductase (GLR1) is responsible for the reduction of the glutathione disulfide (GSSG) to reduced glutathione (GSH).
Glutathione reductase IGR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the process is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, citrate synthase, EF hands, hemoglobins, lipocalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems.
Définition de l'unité
One unit will reduce 1.0 μmole of oxidized glutathione per min at pH 7.6 at 25 °C.
Forme physique
Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol
Notes préparatoires
Purified by affinity chromatography
Inhibiteur
Réf. du produit
Description
Tarif
Produit(s) apparenté(s)
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
Déjà en possession de ce produit ?
Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Les clients ont également consulté
Caryn E Outten et al.
The Journal of biological chemistry, 279(9), 7785-7791 (2003-12-16)
To combat oxidative damage, eukaryotic cells have evolved with numerous anti-oxidant factors that are often distributed between cytosolic and mitochondrial pools. Glutathione reductase, which regenerates the reduced form of glutathione, represents one such anti-oxidant factor, yet nothing is known regarding
Kristin K Brown et al.
Free radical biology & medicine, 45(4), 494-502 (2008-05-27)
Isothiocyanates are phytochemicals with anti-cancer properties that include the ability to trigger apoptosis. A substantial body of evidence suggests that reaction of the electrophilic isothiocyanate moiety with cysteine residues in cellular proteins and glutathione accounts for their biological activity. In
Tünde Pusztahelyi et al.
Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS), 30, 96-101 (2014-12-20)
Selenium deficiency is a major health problem worldwide for about 1 billion people. Bacterial cells usually possess low tolerance to selenite stress and also low ability to reduce high concentrations of toxic selenite. Here, high tolerance to selenite and selenium
Yan-Guang Wu et al.
Cell research, 17(8), 722-731 (2007-08-08)
Selecting oocytes that are most likely to develop is crucial for in vitro fertilization and animal cloning. Brilliant cresyl blue (BCB) staining has been used for oocyte selection in large animals, but its wider utility needs further evaluation. Mouse oocytes
Jing Wang et al.
Acta ophthalmologica, 88(7), 779-785 (2010-01-28)
To investigate the evolution of cataract development and glutathione redox balance in the rat lens after in vivo close-to-threshold dose exposure to ultraviolet radiation (UVR) around 300 nm. Three groups of 10 Sprague-Dawley rats were unilaterally exposed to 8 kJ/m²
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
Contacter notre Service technique