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T8690

Sigma-Aldrich

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

Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

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Source biologique

human

Niveau de qualité

Produit recombinant

expressed in E. coli (N-terminal histidine tagged)

Essai

≥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.[1]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.[2]

Application

Thioredoxin human can be used for in vitro thioredoxin assay.[3] The product can also be used for assessing Thioredoxin reductase (TRXR) enzyme activity.[4]
Thioredoxin human has been used:
  • in mitogen-activated protein kinase kinase 4 (MKK4) in vitro kinase assay[5]
  • to study its role in transcription regulation, RNA processing and nuclear pore function in human cells[6]
  • in proteomics identification of Trx1 reduction target proteins from the hearts of cardiac specific transgenic (Tg)-Trx1 mice[7]

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.[8]The product also stimulates growth in normal as well as leukemic B cell,[9] modifies the transcriptional activity of AP-1[10]and inhibits the apoptosis signal-regulating kinase 1 (ASK1).[11]Thioredoxin (TRX) plays a role in protecting the cells fromelectrophiles, a cytotoxic agent.[2]
Mediates the reduction of disulfide bonds in proteins.
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.[1] It contributes to protein reduction, tissue development and redox regulation.[5]

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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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
Identification of novel nuclear targets of human thioredoxin 1
Wu C, et al.
Molecular and Cellular Proteomics, mcp-M114 (2014)

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