TXN1 Human
Greater than 90.0% as determined by SDS-PAGE.
Description
Product Specs
Product Science Overview
Thioredoxin is a 12 kDa oxidoreductase protein characterized by a specific tertiary structure known as the thioredoxin fold. The active site of thioredoxin contains a dithiol in a CXXC motif, which includes two cysteine residues. These cysteines are essential for the protein’s ability to reduce other proteins. The reduction process begins with the attack of one cysteine residue on the oxidized group of the substrate, followed by the formation of a disulfide bond with the second cysteine, transferring two electrons to the substrate .
The primary function of thioredoxin is the reduction of oxidized cysteine residues and the cleavage of disulfide bonds. Thioredoxins act as electron donors to peroxidases and ribonucleotide reductase. They are maintained in their reduced state by the flavoenzyme thioredoxin reductase in a NADPH-dependent reaction . Thioredoxin also participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions .
Thioredoxins are essential for life in mammals and are involved in numerous critical functions. In humans, thioredoxins are encoded by the TXN and TXN2 genes. Loss-of-function mutations in either of these genes are lethal at the four-cell stage of embryonic development . Thioredoxin is also linked to the response to reactive oxygen species (ROS) and plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, contributing to the response to intracellular nitric oxide .
Recombinant human thioredoxin is produced using recombinant DNA technology, typically expressed in E. coli. The recombinant protein is often tagged with a His-tag for purification purposes. It is used in various research applications, including studies on redox biology, protein-protein interactions, and cellular signaling pathways .
