| Description: | Thioredoxin/TXN Protein participates in diverse redox reactions, using its active center dithiol for reversible oxidation and disulfide bond formation. It catalyzes crucial dithiol-disulfide exchanges and plays a pivotal role in S-nitrosylation of cysteine residues, responding to intracellular nitric oxide. Thioredoxin regulates caspase-3 activity by nitrosylating CASP3's active site cysteine. It also influences FOS/JUN AP-1 DNA binding and augments interleukin-2 receptor expression, showcasing its multifaceted cellular role beyond redox regulation. Thioredoxin/TXN Protein, Human is the recombinant human-derived Thioredoxin/TXN protein, expressed by E. coli, with tag free. The total length of Thioredoxin/TXN Protein, Human is 105 a.a., with molecular weight of ~14 kDa. |
