Sigma-Aldrich Thioredoxin from Escherichia coli. 1 mg

Research area: Cell Signaling

Thioredoxin from Escherichia coli is a monomeric, globular protein. It has a central β-sheet surrounded by α-helices.[1]

Thioredoxin from Escherichia coli has been used in thioredoxin reductase assay, peroxidase-coupled thioredoxin system assay and peroxiredoxin assay.[2][3][4] It has also been used to study its effects on photoreceptor death in a mouse model of retinitis pigmentosa (RP) and its potential to modify retinal oxidative stress, glial changes, and vascular changes during the progression of the disease.[5]

Mediates the reduction of disulfide bonds in proteins.

Thioredoxin from Escherichia coli catalyzes REDOX reactions and has a role in various biological processes. It modulates the structure and activity of many proteins. The enzyme thioredoxin reductase catalyzes the reduction of thioredoxin. Thioredoxin also has a role in oxidative stress response.[1][6][7]Thioredoxin, known as both adult T cell leukemia-derived factor (ADF) and a cellular redox enzyme, functions as a cytokine or chemokine, facilitating cell-to-cell communication.[8] Additionally, it plays a role in regulating cell growth and apoptosis.[9]

GenBank^® Accession Number M26133.

One unit will cause a ΔA₆₅₀ of 1.0 in 1 min at 25 °C in the insulin reduction assay.

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