Active • Host: E. coli • AA: 3-499 • MW: 54.5 kDa
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Thioredoxin Reductase 1 (rat, recombinant; aa 3-499)

Item No. 30586

Technical Information
Synonyms
  • NADPH-dependent Thioredoxin Reductase
  • TrxR1
  • Txnrd1
Purity
≥45% estimated by SDS-PAGE
Source
Active recombinant rat TrxR1 expressed in E. coli
Amino Acids
3-499
MW
54.5 kDa
50 mM Tris, pH 7.4, with 800 mM sodium chloride and 10% glycerol
Applications
Enzyme activity assay and Western WB
Specific Activity
batch specific
UniProt Accession №
O89049
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Thioredoxin reductase 1 (TrxR1) is an oxidoreductase encoded by the TXNRD1 gene in humans and a member of the antioxidant thioredoxin system, which is involved in the maintenance of cellular thiol redox homeostasis.1,2,3 It exists as a homodimer and contains a dimer interface domain, FAD and NADPH binding domains, an N-terminal redox catalytic site, and a C-terminal selenocysteine residue, which is essential for the catalytic activity of TrxR1.4,1 TrxR1 is ubiquitously expressed, localizes to the cytoplasm, and is regulated by the antioxidant transcription factor Nrf2.2,5 TrxR1 catalyzes the NADPH-dependent reduction of oxidized thioredoxin (Trx), restoring the disulfide reductase function of Trx, which regulates redox-sensitive transcription factors, such as NF-κB and p53, and has roles in apoptosis and cell signaling.6,3 Genome-wide deletion of Txnrd1 is embryonic lethal in mice.7 Increased serum TrxR1 activity is associated with reduced progression-free survival in patients with non-small cell lung cancer (NSCLC).8 Cayman’s Thioredoxin Reductase 1 (rat, recombinant; aa 3-499) protein can be used for enzyme activity assay and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Mustacich, D., and Powis, G. Thioredoxin reductase. Biochem. J. 346(Pt. 1), 1-8 (2000).

    2. Cebula, M., Schmidt, E.E., and Arnér, E.S.J. TrxR1 as a potent regulator of the Nrf2-Keap1 response system. Antioxid. Redox Signal. 23(10), 823-853 (2015).

    3. Watanabe, R., Nakamura, H., Masutani, H., et alAnti-oxidative, anti-cancer and anti-inflammatory actions by thioredoxin 1 and thioredoxin-binding protein-2. Pharmacol. Ther. 127(3), 261-270 (2010).

    4. Fritz-Wolf, K., Kehr, S., Stumpf, M., et alCrystal structure of the human thioredoxin reductase–thioredoxin complex. Nat. Commun. 2, 383 (2011).

    5. Li, W., Bandyopadhyay, J., Hwaang, H.S., et alTwo thioredoxin reductases, trxr-1 and trxr-2, have differential physiological roles in Caenorhabditis elegans. Mol. Cells 34(2), 209-218 (2012).

    6. Holmgren, A., and Lu, J. Thioredoxin and thioredoxin reductase: Current research with special reference to human disease. Biochem. Biophys. Res. Commun. 396(1), 120-124 (2010).

    7. Bondareva, A.A., Capecchi, M.R., Iverson, S.V., et alEffects of thioredoxin reductase-1 deletion on embryogenesis and transcriptome. Free Radic. Biol. Med. 43(6), 911-923 (2007).

    8. Chen, G., Chen, Q., Zeng, F., et alThe serum activity of thioredoxin reductases 1 (TrxR1) is correlated with the poor prognosis in EGFR wild-type and ALK negative non-small cell lung cancer. Oncotarget 8(70), 115270-115279 (2017).