T0910
Thioredoxin from Escherichia coli
recombinant, expressed in E. coli, essentially salt-free, lyophilized powder, ≥3 units/mg protein
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About This Item
Produits recommandés
Source biologique
Escherichia coli
Niveau de qualité
Produit recombinant
expressed in E. coli
Essai
≥90% (SDS-PAGE)
Forme
essentially salt-free, lyophilized powder
Activité spécifique
≥3 units/mg protein
Poids mol.
11.7 kDa
Numéro d'accès UniProt
Application(s)
cell analysis
Température de stockage
−20°C
Informations sur le gène
Escherichia coli K12 ... trxA(948289)
Description générale
Thioredoxin from Escherichia coli is a monomeric, globular protein. It has a central β-sheet surrounded by α-helices.
Application
Thioredoxin from Escherichia coli has been used in thioredoxin reductase assay, peroxidase-coupled thioredoxin system assay and peroxiredoxin assay.
Actions biochimiques/physiologiques
Thioredoxin from Escherichia coli catalyzes REDOX reactions and has a role in various biological processes. It modulates the structure and activity of many proteins. The enzyme thioredoxin reductase catalyzes the reduction of thioredoxin. Thioredoxin also has a role in oxidative stress response.
Mediates the reduction of disulfide bonds in proteins.
Autres remarques
GenBank® Accession Number M26133.
Définition de l'unité
One unit will cause a ΔA650 of 1.0 in 1 min at 25 °C in the insulin reduction assay.
Informations légales
GenBank is a registered trademark of United States Department of Health and Human Services
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
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Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli.
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Proceedings of the National Academy of Sciences of the USA, 101(11), 3759-3764 (2004)
Mechanism and structure of thioredoxin reductase from Escherichia coli.
Williams CH Jr
Faseb Journal, 9(13), 1267-1276 (1995)
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