Anti-TST antibody produced in rabbit

Thiosulfate sulfurtransferase (rhodanese) (TST, RDS) is a mitochondrial matrix enzyme that facilitates the modification of sulfur-containing enzymes, and detoxification of H2S and cyanide. Thiosulfate sulfurtransferase converts cyanide into thiocyanide.

Synthetic peptide directed towards the middle region of human TST

Synthetic peptide located within the following region: GEHLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEP

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Anti-TST polyclonal antibody is used to tag thiosulfate sulfurtransferase/rhodanese for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of thiosulfate sulfurtransferase/rhodanese in hydrogen sulfide and cyanide detoxification.

Anti-TST polyclonal antibody reacts with human, mouse, rat, bovine, canine, and chicken thiosulfate sulfurtransferase/rhodanese enzymes.

TST is a mitochondrial matrix enzyme that is encoded by the nucleus. It may play roles in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. The product contains two highly conservative domains (rhodanese homology domains), suggesting these domains have a common evolutionary origin.The product of this gene is a mitochondrial matrix enzyme that is encoded by the nucleus. It may play roles in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. The gene product contains two highly conservative domains (rhodanese homology domains), suggesting these domains have a common evolutionary origin.

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