All kit components of this kit are stable at 2 to 8°C. Any unused reconstituted standard should be discarded or frozen at -70°C. Standard can be frozen and thawed one time only without loss of immunoreactivity.
Thioredoxins(Trx) are small, multi-functional proteins with oxido-reductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide –isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1 (T1-151).Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins. Trx is a multifunctional protein and has anti-inflammatory and antiapoptotic effects, as well as antioxidative effects. It is therefore feasible to think that Trx is a potential therapy for cardiac disease. Moreover, serum Trx is a well-recognized biomarker of various diseases involving oxidative stress, and this is also the case for cardiac disorders.