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Merck

T7915

Sigma-Aldrich

Thioredoxin Reductase from Escherichia coli

ammonium sulfate suspension, >25 units/mg protein (Bradford)

Synonim(y):

NADPH:oxidized thioredoxin oxidoreductase

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About This Item

Numer CAS:
Numer EC enzymu:
Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.32

pochodzenie biologiczne

Escherichia coli

Poziom jakości

Postać

ammonium sulfate suspension

aktywność właściwa

>25 units/mg protein (Bradford)

masa cząsteczkowa

70 kDa

metody

activity assay: suitable

numer dostępu UniProt

temp. przechowywania

2-8°C

informacje o genach

Escherichia coli K12 ... trxB(949054)

Opis ogólny

Research area: Cell Signaling
Thioredoxin reductases (TrxRs) belongs to family of selenium-containing pyridine nucleotide-disulphide oxidoreductases.

Zastosowanie

Thioredoxin Reductase from Escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of Cys-based thiol peroxidases.Thioredoxin Reductase from Escherichia coli has been used:
  • for determining the enzymatic activity of His6-Ahp1p.
  • to assay C. elegans TRXR using the TXN-dependent activity assay.
  • to investigate the biological reducing systems for organic hydroperoxide resistance R gene (OhrR).
  • for enzymatic targeting of auranofin to test its antimicrobial properties.
  • in thioredoxin reductase activity and peroxiredoxin assay.
  • to study the synergy between broccoli sprout extract and selenium in the upregulation of thioredoxin reductase in human hepatocytes.
Thioredoxin reductase from Escherichia coli has been used in thioredoxin reductase activity and peroxiredoxin assay.
It has also been used to study the synergy between broccoli sprout extract and selenium in the upregulation of thioredoxin reductase in human hepatocytes.

Działania biochem./fizjol.

An FAD-containing enzyme involved in the transfer of hydrogen from E. coli thioredoxin to other proteins thus providing a powerful disulfide reductase system.
Thioredoxin reductase is a FAD containing enzyme, which transfers the reducing equivalent from NADPH to the disulphide bond of the enzyme by using FAD moiety within the Cys-Ala-Thr-Cys sequence. It can also reduce Trx-S2 to Trx-(SH)2 by using NADPH.
Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised 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 well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide.

Definicja jednostki

One unit will cause an increase in absorbance of 1.0 at 412 nm (when measured in a coupled assay with E. coli thioredoxin and DTNB) per min per mL at pH 7.0 at 25 °C.

Postać fizyczna

Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA.
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Kod klasy składowania

12 - Non Combustible Liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

NR1D1 Recruitment to Sites of DNA Damage Inhibits Repair and Is Associated with Chemosensitivity of Breast Cancer
Ka NL, et al.
Journal of Separation Science, 77(9), 2453?2463-2453?2463 (2017)
Purification and characterization of ferredoxin-NAD (P)+ reductase from the green sulfur bacterium Chlorobium tepidum
Seo D, et al.
Biochim. Biophys. Acta Gen. Subj., 1597(1), 123-132 (2002)
Valérie Prouzet-Mauléon et al.
The Journal of biological chemistry, 277(7), 4823-4830 (2001-11-24)
Yeasts lacking cytoplasmic superoxide dismutase (Cu,Zn-SOD) activity are permanently subjected to oxidative stress. We used two-dimensional PAGE to examine the proteome pattern of Saccharomyces cerevisiae strains lacking Cu,Zn-SOD. We found a new stable form of alkyl hydroperoxide reductase 1 (Ahp1)
Analysis of the Organic Hydroperoxide Response of Chromobacterium violaceum Reveals That OhrR Is a Cys-Based Redox Sensor Regulated by Thioredoxin
JF da Silva Neto, et al.
PLoS ONE, 7(10), e47090-e47090 (2012)
The A to Z of modulated cell patterning by mammalian thioredoxin reductases
Dagnell M, et al.
Free Radical Biology & Medicine, 115, 484-496 (2018)

Produkty

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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