Thioredoxin reductase is an enzyme that plays a crucial role in cellular redox reactions, primarily involved in maintaining the balance of thiol-disulfide status within cells. It catalyzes the reduction of thioredoxin, a small protein that acts as an electron donor in various biochemical processes, including DNA synthesis and antioxidant defense. The enzyme is characterized by its dependence on NADPH as a reducing agent, facilitating the transfer of electrons to thioredoxin. Thioredoxin reductase is typically found in various organisms, including bacteria, plants, and animals, and exists in different isoforms, each with specific functions and regulatory mechanisms. Its activity is essential for cellular processes such as cell proliferation, apoptosis, and response to oxidative stress. Additionally, thioredoxin reductase has been studied for its potential role in cancer therapy and as a target for drug development, given its involvement in redox regulation and cellular signaling pathways. The CAS number 9074-14-0 uniquely identifies this enzyme in chemical databases, aiding in research and application across various scientific fields.

thioredoxin reductase

Thioredoxin reductase (TR, TrxR) (EC 1.8.1.9) is an enzyme that reduce thioredoxin using NADPH as a co-factor, and also contains FAD. One unit of thioredoxin reductase will raise increase light absorbance by 1.0 per minute at 412nm in the presence of thioredoxin and Ellman's reagent at pH 7.0 and 25 °C.

Thioredoxin reductase from escherichia coli

Thioredoxin reductase, recombinant from Yeast

CAS 9074-14-0: thioredoxin reductase

Thioredoxin reductase from escherichia coli

Ref: 3D-JAA07414

Thioredoxin reductase, recombinant from Yeast

Ref: 54-BIB3092