Rhodanese Human

Thiosulfate Sulfurtransferase Human Recombinant
Cat. No.
BT13133
Source
Escherichia Coli.
Synonyms
EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Human Rhodanese produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a) and having a molecular mass of 35.6 kDa. Rhodanese is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.

Product Specs

Introduction
Rhodanese, a mitochondrial enzyme encoded in the nucleus, plays a crucial role in cyanide detoxification. This enzyme facilitates the conversion of thiosulfate and cyanide into sulfite and thiocyanate, effectively neutralizing the toxic cyanide. Beyond detoxification, Rhodanese contributes to the formation of iron-sulfur proteins and the modification of enzymes containing sulfur. Classified as a transferase, Rhodanese possesses two highly conserved rhodanese homology domains. In mammals, it primarily converts cyanide to thiocyanate and exhibits limited mercaptopyruvate sulfurtransferase activity.
Description
Recombinant Human Rhodanese, expressed in E. coli, is a single, non-glycosylated polypeptide chain with 317 amino acids (1-297 a.a) and a molecular weight of 35.6 kDa. A 20 amino acid His-Tag is fused to the N-terminus to facilitate purification via standard chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The Rhodanese protein is supplied in a solution containing 20mM Tris-HCl buffer at pH 8.0 and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the protein is determined to be greater than 95.0% by SDS-PAGE analysis.
Synonyms
EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.
Source
Escherichia Coli.
Amino Acid 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.

Product Science Overview

Gene and Protein Structure

The gene encoding thiosulfate sulfurtransferase in humans is known as TST and is located on chromosome 22q12.3 . The TST gene produces a protein that contains two rhodanese domains, which are essential for its enzymatic activity . The protein is localized to the mitochondria, where it catalyzes the conversion of thiosulfate and cyanide to thiocyanate and sulfite .

Enzymatic Function

Thiosulfate sulfurtransferase is involved in several critical biochemical processes:

  • Cyanide Detoxification: The enzyme converts toxic cyanide into less harmful thiocyanate, which can be excreted from the body .
  • Sulfur and Selenium Transport: It facilitates the transport of sulfur and selenium in biologically available forms .
  • Iron-Sulfur Cluster Formation: The enzyme plays a role in the formation and maintenance of iron-sulfur clusters, which are essential for various cellular functions .
  • Redox System Maintenance: It helps maintain the redox balance within cells .
  • Mitochondrial Import of 5S rRNA: Thiosulfate sulfurtransferase interacts with 5S ribosomal RNA and aids its import into the mitochondria .
Tissue Distribution

In humans, thiosulfate sulfurtransferase is predominantly found in the liver, kidneys, adrenals, and thyroid glands . The highest enzyme activity is observed in the kidneys, followed by the liver, lungs, brain, stomach, and muscles .

Biomedical and Biotechnological Applications

The enzyme’s ability to detoxify cyanide and its involvement in sulfur metabolism make it a valuable target for biomedical research. Thiosulfate sulfurtransferase has potential applications in treating metabolic diseases such as diabetes . Additionally, its role in maintaining redox balance and forming iron-sulfur clusters highlights its importance in cellular health and function .

Recombinant Production

Human recombinant thiosulfate sulfurtransferase is produced using genetic engineering techniques. The TST gene is cloned into an expression vector, which is then introduced into a host organism, such as bacteria or yeast. The host organism produces the enzyme, which can be purified and used for research or therapeutic purposes.

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