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Documenti fondamentali

SRP6082

Sigma-Aldrich

TRXB from Escherichia coli

recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

Sinonimo/i:

TRXR, Thioredoxin reductase

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About This Item

Codice UNSPSC:
12352200
NACRES:
NA.32

Origine biologica

Escherichia coli

Ricombinante

expressed in E. coli

Saggio

≥90% (SDS-PAGE)

Stato

liquid

PM

34.6 kDa

Confezionamento

pkg of 100 μg

N° accesso NCBI

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

Escherichia coli ... TRXB(949054)

Descrizione generale

Thioredoxin reductase (TrxR) is encoded by TRXB gene. TrxR is one of the member of flavoprotein family of pyridine nucleotide-disulphide oxidoreductases, which also includes lipoamide dehydrogenase, glutathione reductase and mercuric ion reductase. Escherichia coli TrxR is a 70-kDa homodimeric flavoprotein, each monomer of this protein contains a FAD prosthetic group, an NADPH domain and an active site with redox-active disulphide. The catalytic site (-Cys-Ala-Thr-Cys-) in Escherichia coli TrxB is localized on the NADPH domain, whereas in humans TrxB catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) is part of the FAD domain.

Azioni biochim/fisiol

Thioredoxin reductase (TRXB) catalyzes the reduction of oxidized thioredoxin using nicotinamide adenine dinucleotide phosphate (NADPH). In thioredoxin pathway, this reduced thioredoxin reduce disulfide bonds in proteins localized in the cytoplasm and is implicated in the recycling of an essential enzyme ribonucleotide reductase. TrxR is essentially involved in protection against oxidation stress, cell growth and transformation, and the recycling of ascorbate from its oxidized form.

Stato fisico

1 mg/mL solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol and 1mM DTT.

Nota sulla preparazione

Centrifuge the vial prior to opening.

Altre note

MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K.

Pittogrammi

Exclamation mark

Avvertenze

Warning

Indicazioni di pericolo

Classi di pericolo

Eye Irrit. 2

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Characterization of two active site mutations of thioredoxin reductase from Escherichia coli.
Prongay AJ
The Journal of Biological Chemistry, 264(5), 2656-2664 (1989)
Thioredoxin reductase
Debbie MUSTACICH and Garth POWIS
The Biochemical Journal, 346, 1-8 (2000)
E S Arnér et al.
European journal of biochemistry, 267(20), 6102-6109 (2000-09-30)
Thioredoxin, thioredoxin reductase and NADPH, the thioredoxin system, is ubiquitous from Archea to man. Thioredoxins, with a dithiol/disulfide active site (CGPC) are the major cellular protein disulfide reductases; they therefore also serve as electron donors for enzymes such as ribonucleotide

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