T8690
Thioredoxin human
≥90% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal histidine tagged), essentially salt-free, lyophilized powder, ≥5 U/mg
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About This Item
Produits recommandés
Source biologique
human
Niveau de qualité
Produit recombinant
expressed in E. coli (N-terminal histidine tagged)
Pureté
≥90% (SDS-PAGE)
Forme
essentially salt-free, lyophilized powder
Activité spécifique
≥5 U/mg
Poids mol.
14 kDa
Technique(s)
activity assay: suitable
Solubilité
water: soluble 0.50—0.60 mg/mL, clear to slightly hazy, colorless to faint yellow or tan
Adéquation
suitable for molecular biology
Numéro d'accès UniProt
Application(s)
cell analysis
Température de stockage
−20°C
Informations sur le gène
human ... TXN(7295)
Description générale
Cloned from Jurkat cell cDNA. Identical to the ADF/Trx (GenBank® Accession Number X77584) and the thioredoxin from human placenta (GenBank® Accession Number AF085844).
Thioredoxin (TXN) is a 12 kDa ubiquitous protein. The gene is located on human chromosome 9q31.3. TXN is mainly located in the cytoplasm.Thioredoxin contains a redox-active dithiol in the active site. Itexists in several forms, the most prevalent ones being the cytosolic (TRX1) andmitochondrial (TRX2) forms.
Application
Thioredoxin human can be used for in vitro thioredoxin assay. The product can also be used for assessing Thioredoxin reductase (TRXR) enzyme activity.
Thioredoxin human has been used:
- in mitogen-activated protein kinase kinase 4 (MKK4) in vitro kinase assay
- to study its role in transcription regulation, RNA processing and nuclear pore function in human cells
- in proteomics identification of Trx1 reduction target proteins from the hearts of cardiac specific transgenic (Tg)-Trx1 mice
Actions biochimiques/physiologiques
Human Thioredoxin is a recombinant, N-terminal histidine tagged protein. The product induces proliferation in lymphoid cells, fibroblasts as well as in numerous human solid tumor cell lines.The product also stimulates growth in normal as well as leukemic B cell, modifies the transcriptional activity of AP-1and inhibits the apoptosis signal-regulating kinase 1 (ASK1).Thioredoxin (TRX) plays a role in protecting the cells fromelectrophiles, a cytotoxic agent.
Thioredoxin (TXN) has disulfide-reducing activity. It acts as a cytokine to reduce inflammation. TXN functions as a scavenger for reactive oxygen intermediates (ROIs), which are produced in various oxidative stress. Thioredoxin induces cellular proliferation to decrease oxidative stress. TXN is a prognostic biomarker for various cancers, such as lung, pancreatic and hepatocellular carcinoma. It contributes to protein reduction, tissue development and redox regulation.
Mediates the reduction of disulfide bonds in proteins.
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)
Certificats d'analyse (COA)
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Les clients ont également consulté
Cexiong Fu et al.
Molecular & cellular proteomics : MCP, 8(7), 1674-1687 (2009-05-07)
Thioredoxin 1 (Trx1) is a key redox modulator that is functionally conserved across a wide range of species, including plants, bacteria, and mammals. Using a conserved CXXC motif, Trx1 catalyzes the reduction of cysteine disulfides and S-nitrosothiols. In contrast to
TXN (thioredoxin)
Chen Z, et al.
Atlas of Genetics and Cytogenetics in Oncology and Haematology (2010)
Thioredoxin activates MKK4-NFkappaB pathway in a redox dependent manner to control manganese superoxide dismutase gene expression in endothelial cells
Kundumani-Sridharan V, et al.
The Journal of Biological Chemistry, jbc-M115 (2015)
Walter H Watson et al.
Toxicological sciences : an official journal of the Society of Toxicology, 78(1), 3-14 (2003-12-24)
Thioredoxins (Trx) are members of an evolutionarily conserved family of redox-active proteins containing a conserved active site dithiol motif. Trx supports diverse reduction reactions, including several of direct toxicologic interest, but relatively little information is available concerning the roles of
Christopher J Boehler et al.
PloS one, 8(8), e71525-e71525 (2013-08-13)
Thioredoxin reductase-1 (TRXR-1) is the sole selenoprotein in C. elegans, and selenite is a substrate for thioredoxin reductase, so TRXR-1 may play a role in metabolism of selenium (Se) to toxic forms. To study the role of TRXR in Se
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