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T9698

Sigma-Aldrich

Thioredoxin Reductase from rat liver

buffered aqueous glycerol solution, ≥100 units/mg protein (Bradford)

Synonyme(s) :

NADPH:Oxidised Thioredoxin Oxidoreductase, Thioredoxin: NADP+ Oxidoreductase

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About This Item

Numéro CAS:
9074-14-0
Numéro de classification (Commission des enzymes):
1.8.1.9 (BRENDA, IUBMB)
Numéro MDL:
MFCD00678149
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

rat liver

Niveau de qualité

200

Pureté

≥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

O89049

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. The product can also be used for studying the activation mechanism of transglutaminase 2 (TG2) in the extracellular matrix by using Thioredoxin.

Actions biochimiques/physiologiques

Thioredoxin Reductase is a ubiquitous enzyme that catalyzes the active site disulfide of thioredoxin by NADPH. The product also reduces ubiquinone and regenerates ubiquinol, a powerful antioxidant.
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)

Certificats d'analyse (COA)

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Luciano Oehninger et al.
Dalton transactions (Cambridge, England : 2003), 42(5), 1657-1666 (2012-11-15)
Metal complexes with N-heterocyclic carbene (NHC) ligands have been widely used in catalytic chemistry and are now increasingly considered for the development of new chemical tools and metal based drugs. Ruthenium complexes of the type (p-cymene)(NHC)RuCl(2) interacted with biologically relevant
Arun Kumar Selvam et al.
Antioxidants (Basel, Switzerland), 9(2) (2020-02-09)
Kynurenine aminotransferase 1 (KYAT1 or CCBL1) plays a major role in Se-methylselenocysteine (MSC) metabolism. It is a bi-functional enzyme that catalyzes transamination and beta-elimination activity with a single substrate. KYAT1 produces methylselenol (CH3SeH) via β-elimination activities with MSC as a
Aristi P Fernandes et al.
PloS one, 7(11), e50727-e50727 (2012-12-12)
Naturally occurring selenium compounds like selenite and selenodiglutathione are metabolized to selenide in plants and animals. This highly reactive form of selenium can undergo methylation and form monomethylated and multimethylated species. These redox active selenium metabolites are of particular biological
Kely Navakoski de Oliveira et al.
ChemMedChem, 8(2), 256-264 (2013-01-03)
Thioredoxin reductase (TrxR) is overexpressed in cancer cells and is therefore a putative cancer target. Inhibition of this enzyme is considered an important strategy for the development of new chemotherapeutic agents with a specific mechanism of action. Organotin compounds have
L Zhong et al.
The Journal of biological chemistry, 275(24), 18121-18128 (2000-06-13)
Mammalian thioredoxin reductases (TrxR) are dimers homologous to glutathione reductase with a selenocysteine (SeCys) residue in the conserved C-terminal sequence -Gly-Cys-SeCys-Gly. We removed the selenocysteine insertion sequence in the rat gene, and we changed the SeCys(498) encoded by TGA to
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Mitochondrial Stress and ROS

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

Mitochondrial Stress and ROS

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

Mitochondrial Stress and ROS

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

Mitochondrial Stress and ROS

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

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