T9698

Sigma-Aldrich

Thioredoxin Reductase from rat liver

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

Synonym(s):
Thioredoxin: NADP+ Oxidoreductase, NADPH:Oxidised Thioredoxin Oxidoreductase
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.32

Quality Level

biological source

rat liver

assay

≥90% (GE)

form

buffered aqueous glycerol solution

specific activity

≥100 units/mg protein (Bradford)

application(s)

activity assay: suitable

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

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.

Packaging

50 μg in glass bottle

Biochem/physiol Actions

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 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 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.

Unit Definition

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.

Physical form

Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol.

storage_class_code

12 - Non Combustible Liquids

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Certificate of Analysis

Certificate of Origin

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...
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...
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...
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...
Anne-Sophie Bohrer et al.
Journal of experimental botany, 63(18), 6315-6323 (2012-10-26)
In plants, thioredoxins (TRX) constitute a large protein disulphide oxidoreductase family comprising 10 plastidial members in Arabidopsis thaliana and subdivided in five types. The f- and m-types regulate enzymes involved mainly in carbon metabolism whereas the x, y, and z...
Articles
Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.
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