Thioredoxin 1 Yeast (rec.)

CHF 366.00
In stock
YIF-LF-P00360.5 mgCHF 366.00
More Information
Product Details
Product Type Protein
Properties
Source/Host E. coli
Crossreactivity Yeast
Biological Activity

32.7U/mg (One unit will cause a ΔA650 of 1.0 in 1 min at 25°C in the insulin reduction assay)

Purity ≥95% (SDS-PAGE)
Formulation Lyophilized from 20mM HEPES, pH 7.4.
Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability After reconstitution, store at -80°C.
Documents
MSDS No
Product Specification Sheet
Datasheet Download PDF

Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide -isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-κB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7).

Product References

1) Andoh, T. et al. (2002) J.Biol.Chem. 277, 9655-9660. (General)
2) Arner, E. S. and Holmgren, A. (2000) Eur. J. Biochem. 267, 6102-6109. (General)
3) Lundstrom, J. and Holmgren, A. (1990) J. Biol. Chem. 265, 1994-9120. (General)
4) Nordberg, J. and Arner, E. S. J. (2001) Free Radic. Biol. Med. 31, 1287-1312. (General)
5) Matthews, J. R. et al. (1992) Nucleic Acids Res. 20, 3821-3830. (General)
6) Wei, S. J. (2000) Cancer Res. 60, 6688-6695. (General)
7) Chae, H. Z. (1999) Methods Enzymol. 300, 219-226. (General)

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