Active • Host: E. coli • AA: Full length • MW: 11.7 kDa
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Thioredoxin 1 (C61S/C72S mutant; human, recombinant)

Item No. 11520

Product Insert (PDF)
Technical Information
Synonyms
  • Trx1
  • TrxA
  • Txn1
Purity
≥85% estimated by SDS-PAGE
Source
Active recombinant human thioredoxin 1 (C61S/C72S mutant) expressed in E. coli
Amino Acids
Full length
MW
11.7 kDa
Formulation (Request formulation change)
Lyophilized in 50 mM Tris-HCl, pH 7.5, with 1 mM EDTA
UniProt Accession №
P10599
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    250 µg

    $252

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    Product Description

    Thioredoxin 1 (Trx1) is a thiol-disulfide oxidoreductase and part of the antioxidant thioredoxin system that is involved in the maintenance of cellular thiol redox homeostasis.1,2,3 It is ubiquitously expressed, localizes primarily to the cytoplasm with some nuclear localization, and is upregulated in and released from cells under conditions of oxidative stress.1,4,2 Trx1 contains two active site cysteine residues at positions 32 and 35 with additional cysteines at positions 62, 69, and 73.2 During the catalytic cycle, the active site cysteines are oxidized to a disulfide upon reduction of oxidized protein disulfide substrates and are subsequently restored to their reduced state by thioredoxin reductase (TrxR) and NADPH.1,2 In the human recombinant enzyme, the initiating methionine is removed, and thus the positions of the amino acids are counted without the N-terminal methionine.5 Cysteine-to-serine substitutions at Cys61 (C61S) and Cys72 (C72S) in Trx1 (Trx1C61S/C72S) prevent oxidation-induced inhibition of protein disulfide reductase activity in Trx1.6 Cayman's Thioredoxin 1 (C61S/C72S mutant; human, recombinant) protein can be used for enzyme activity assays.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Haendeler, J. Thioredoxin-1 and posttranslational modifications. Antioxid. Redox Signal. 8(9-10), 1723-1728 (2006).

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

    3. Berndt, C., Lillig, C.H., and Holmgren, A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: Implications for diseases in the cardiovascular system. Am. J. Physiol. Heart Circ. Physiol. 292(3), H1227-H1236 (2007).

    4. Raffel, J., Bhattacharyya, A.K., Gallegos, A., et al. Increased expression of thioredoxin-1 in human colorectal cancer is associated with decreased patient survival. J. Lab. Clin. Med. 142(1), 46-51 (2003).

    5. Casagrande, S., Bonetto, V., Fratelli, M., et al. Glutathionylation of human thioredoxin: A possible crosstalk between the glutathione and thioredoxin systems. Proc. Natl. Acad. Sci. USA 99(15), 9745-9749 (2002).

    6. Ren, X., Björnstedt, M., Shen, B., et al. Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by Selenodiglutathione. Biochemistry 32(37), 9701-9708 (1993).