T9698
Thioredoxin Reductase from rat liver
buffered aqueous glycerol solution, ≥100 units/mg protein (Bradford)
Synonyme(s) :
NADPH:Oxidised Thioredoxin Oxidoreductase, Thioredoxin: NADP+ Oxidoreductase
Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme
Sélectionner une taille de conditionnement
50 μG
490.00 CHF
Sélectionner une taille de conditionnement
Changer de vue
50 μG
490.00 CHF
About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
rat liver
Niveau de qualité
Essai
≥90% (GE)
Forme
buffered aqueous glycerol solution
Activité spécifique
≥100 units/mg protein (Bradford)
Poids mol.
55—67 kDa
Technique(s)
activity assay: suitable
Impuretés
Glutathione reductase
Solubilité
water: soluble
Adéquation
suitable for molecular biology
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Informations sur le gène
rat ... Txnrd1(58819)
Description générale
Research area: Cell signaling
Application
Thioredoxin Reductase from rat liver can be used for studying the uptake and reduction of a-lipoic acid by utilizing reducing capacity of human erythrocytes.[1] The product can also be used for studying the activation mechanism of transglutaminase 2 (TG2) in the extracellular matrix by using Thioredoxin.[2]
Actions biochimiques/physiologiques
Thioredoxin Reductase is a ubiquitous enzyme that catalyzes the active site disulfide of thioredoxin by NADPH.[3] The product also reduces ubiquinone and regenerates ubiquinol, a powerful antioxidant.[4]
Thioredoxin reductase (TrxR) is a NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidized thioredoxin (Trx).
Thioredoxin reductase (TrxR) is a NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidized thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxide.
Thioredoxin reductase from mammalian sources contains a selenocysteine residue that is essential for the activity of the enzyme. It is one of the antioxidant enzymes present in the mammalian cell together with catalase, glutathione peroxidase and superoxide dismutase, and helps in removal of reactive oxygen species (ROS) from the cell. An example is the removal of excess nitric oxide (NO) by the formation of a complex with glutathione forming the S-nitroso-glutathione adduct (GS-NO). This can be cleaved directly by thioredoxin reductase. Hydrogen peroxide, another deleterious oxidant in the cell, is also reduced directly by mammalian TrxR.
Définition de l'unité
One unit will cause an increase in absorbance of 1.0 at 412 nm (when measured in a non-coupled assay containing DTNB [Sigma No. D8130] alone as substrate) per minute at pH 7.0 at 25 °C.
Forme physique
Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol.
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Faites votre choix parmi les versions les plus récentes :
Certificats d'analyse (COA)
Lot/Batch Number
Vous ne trouvez pas la bonne version ?
Si vous avez besoin d'une version particulière, vous pouvez rechercher un certificat spécifique par le numéro de lot.
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
Jianqiang Xu et al.
Nucleic acids research, 41(21), 9800-9811 (2013-08-29)
Selenoprotein expression in Escherichia coli redefines specific single UGA codons from translational termination to selenocysteine (Sec) insertion. This process requires the presence of a Sec Insertion Sequence (SECIS) in the mRNA, which forms a secondary structure that binds a unique
James M May et al.
Clinical biochemistry, 40(15), 1135-1142 (2007-08-04)
The reducing capacity of erythrocytes has been used clinically as to estimate resistance to oxidant stress. In this work we targeted the antioxidant capacity of pyridine nucleotide disulfide reductases of these cells by measuring their ability to reduce the disulfide
X Peng et al.
Cell death & disease, 4, e881-e881 (2013-10-26)
The low-molecular-weight compound APR-246 (PRIMA-1(MET)) restores wild-type conformation and function to mutant p53, and triggers apoptosis in tumor cells. We show here that APR-246 also targets the selenoprotein thioredoxin reductase 1 (TrxR1), a key regulator of cellular redox balance. APR-246
Tomas Nordman et al.
BioFactors (Oxford, England), 18(1-4), 45-50 (2003-12-30)
Ubiquinol is a powerful antioxidant, which is oxidized in action and needs to be replaced or regenerated to be capable of a sustained effort. This article summarises current knowledge of extramitochondrial reduction of ubiquinone by three flavoenzymes, i.e. lipoamide dehydrogenase
Sofiane Y Mersaoui et al.
Archives of toxicology, 96(5), 1371-1386 (2022-03-05)
Arsenic toxicity is a global concern to human health causing increased incidences of cancer, bronchopulmonary, and cardiovascular diseases. In human and mouse, inorganic arsenic (iAs) is metabolized in a series of methylation steps catalyzed by arsenic (3) methyltransferase (AS3MT), forming
Articles
Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.
Active Filters
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
