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. AA sequence: MGSSHHHHHH SSGLVPRGSH MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD GEHLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLDRS LLKTYEQVLE NLESKRFQLV DSRSQGRFLG TEPEPDAVGL DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL SQPLIATCRK GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA 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 -70C. 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.
Molecular Weight:
35.6
Purity:
~95% (SDS-PAGE) Purified by immunoaffinity chromatography.
Form:
Supplied as a liquid in 20mM Tris-HCl, pH 8.0, 10% glycerol.
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