Thiosulfate sulfurtransferase (TST), also known as Rhodanese, is a mitochondrial enzyme that involved in cyanide detoxification and the modification of sulfur-containing enzymes. This protein contains two highly conservative domains, known as rhodanese homology domains. In mammals, most cyanide is converted to thiocyanate by this enzyme. TST also has weak mercaptopyruvate sulfurtransferase activity. Recombinant TST protein was expressed in E. coli and purified by using conventional chromatography techniques.
Source:Recombinant corresponding to human TST, expressed in E. coli.
Enzyme Activity:Not determined. This product is recommended for use in applications that do not require a catalytically active form of the protein.
Storage and Stability:Aliquot to avoid repeated freezing and thawing and freeze at -70°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 6 months.
仕様
Size：100ug
Source Antigen：Recombinant, E. coli
Grade：Affinity Purified
Purity：~95% (SDS-PAGE) Purified by immunoaffinity chromatography.
Form：Supplied as a liquid in 20mM Tris-HCl, pH 8.0, 10% glycerol.
