TXNRD3NB Human

Thioredoxin reductase was first discovered during studies on the biosynthesis of deoxyribonucleotides in Escherichia coli. In 1964, Laurent and coworkers identified thioredoxin as the reducing substrate of ribonucleotide reductase, an essential enzyme for the de novo synthesis of 2′-deoxyribonucleotides. This discovery led to the identification and purification of thioredoxin reductase from E. coli and later from mammalian tissues .

Thioredoxin reductase (TrxR) is a ubiquitous enzyme that is part of the cell’s defense against oxidative stress. It is a member of the thioredoxin network, which includes thioredoxin (Trx), TrxR, and various enzymes that use Trx as a reductant, such as ribonucleotide reductase and peroxiredoxin . TrxR transfers electrons from NADPH to Trx, which in turn reduces oxidants, thereby protecting cells from oxidative damage .

There are three known isozymes of thioredoxin reductase in mammals: TrxR1, TrxR2, and TrxR3. TrxR3, also known as thioredoxin reductase 3, is particularly important in the regulation of redox homeostasis .

Thioredoxin Reductase 3 Neighbor (Human Recombinant) is a recombinant form of the human TXNRD3 protein. Recombinant proteins are produced through recombinant DNA technology, which involves inserting the gene encoding the protein into an expression system, such as bacteria or yeast, to produce the protein in large quantities. This technology allows for the production of proteins that are identical to their natural counterparts, enabling detailed studies of their structure and function.

The thioredoxin system, including Trx and TrxR, plays a significant role in cellular processes such as proliferation, differentiation, and apoptosis. It is involved in the regulation of redox-dependent signaling pathways and the maintenance of cellular redox balance . The Trx/TrxR system is also a target for cancer therapy due to its role in maintaining cell homeostasis and promoting cell survival .