Skip to Content
Merck
All Photos(1)

Documents

Safety Information

R1756

Sigma-Aldrich

Rhodanese from bovine liver

Type II, essentially salt-free, lyophilized powder, 100-300 units/mg solid

Synonym(s):

Thiosulfate Sulfur Transferase, Thiosulfate:cyanide sulfurtransferase

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

CAS Number:
9026-04-4
Enzyme Commission number:
2.8.1.1 (BRENDA, IUBMB)
MDL number:
MFCD00132178
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type II

form

essentially salt-free, lyophilized powder

specific activity

100-300 units/mg solid

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

Application

Rhodanese (RHOD) is an enzyme that converts cyanide to thiocyanate. RHOD may be useful in ulcerative colitis (UC) research as it has been shown to have detoxifying properties in the colon . Rhodanese is used to study sulfur energy metabolism .

Biochem/physiol Actions

Rhodanese (RHOD) is the principal enzyme involved in hydrogen sulphide (H2S) detoxication in the colonic luman .

Unit Definition

One unit will convert 1.0 μmole of cyanide to thiocyanate per min at pH 8.6 at 25°C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

R1756-5MG:
R1756-VAR:
R1756-25MG:
R1756-BULK:
R1756-10MG:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Tomohiro Mizobata et al.
PloS one, 6(10), e26462-e26462 (2011-10-27)
The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is responsible for a specific role in the functional mechanism. Here, we have used circular permutation to study the structural and functional
Yoshihiro Sasaki et al.
Macromolecular bioscience, 11(6), 814-820 (2011-03-09)
Cell-free protein synthesis is a promising technique for the rapid production of proteins. However, the application of the cell-free systems requires the development of an artificial chaperone that prevents aggregation of the protein and supports its correct folding. Here, nanogel-based
Piotr Sura et al.
Comparative biochemistry and physiology. Toxicology & pharmacology : CBP, 154(3), 180-186 (2011-05-25)
The effect of mercury ions on the level of cysteine, glutathione, sulfane sulfur, and on the activity of rhodanese, 3-mercaptopyruvate sulfurtransferase (MPST) and γ-cystathionase in brain, heart muscle, liver, kidneys, testes and skeletal muscle of adult Xenopus laevis was investigated.
Hossein Tayefi-Nasrabadi et al.
TheScientificWorldJournal, 2012, 648085-648085 (2012-05-26)
Cyanide is one of the most toxic substances present in a wide variety of food materials that are consumed by animals. Rhodanese, a ubiquitous enzyme, can catalyse the detoxification of cyanide by sulphuration reaction. In this study, rhodanese was partially
Avinash Kale et al.
The Journal of biological chemistry, 286(24), 21254-21265 (2011-04-29)
The PEB4 protein is an antigenic virulence factor implicated in host cell adhesion, invasion, and colonization in the food-borne pathogen Campylobacter jejuni. peb4 mutants have defects in outer membrane protein assembly and PEB4 is thought to act as a periplasmic
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service