Thioredoxin, Human, Recombinant, E. coli

Recombinant, human thioredoxin expressed in E. coli. A ubiquitous protein with two redox-active half-cysteine residues that function as a general disulfide reductant. Works efficiently on model compounds (e.g. Ellman′s reagent, Cat. No. 322123) and protein disulfides. Plays an essential role in cellular protection against oxidative stress and cell death. Inhibits apoptosis in Jurkat T-cells and human PBL blasts. Occurs as a single polypeptide chain.

Recombinant, human thioredoxin expressed in E. coli. A ubiquitous protein with two redox-active half-cysteine residues. Functions as a general disulfide reductant. Works efficiently on model compounds (e.g. Ellman’s reagent, Cat. No. 322123) and protein disulfides. Plays an essential role in cellular protection against oxidative stress and cell death. Inhibits apoptosis in Jurkat T cells and human PBL.

Toxicity: Standard Handling (A)

One unit (insulin reduction unit) is calculated by measuring the change in absorbance at 650 nm with 330 µM DTT as the reductant at 25°C, pH 6.5.

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.

Reconstitute in physiological buffer containing 3 mM EDTA and 1-5 mM DTT.

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Buchanon, B.B., et al. 1994. Arch. Biochem. Biophys. 314, 257.

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