R1756
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
Recommended Products
type
Type II
Quality Level
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
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.
Protein and peptide letters, 19(11), 1139-1143 (2012-05-17)
Yeast tRNA-thiouridine modification protein 1 (Tum1) plays essential role in the sulfur transfer process of Urm1 system, which in turn is involved in many important cellular processes. In the rhodanese-like domain (RLD), conserved cysteine residue is proved to be the
Inflammatory bowel diseases, 18(12), 2371-2380 (2012-03-22)
Defective detoxification of sulfides leads to damage to the mucosa and may play a role in the etiology of ulcerative colitis (UC). The colonic mucosal thiosulfate sulfurtransferase (TST) enzyme removes H(2) S by conversion to the less toxic thiocyanate. In
Plant molecular biology, 79(4-5), 495-508 (2012-05-31)
Rhodanese-domain proteins (RDPs) are widespread in plants and other organisms, but their biological roles are mostly unknown. Here we report on a novel RDP from Chlamydomonas that has a single rhodanese domain, and a predicted chloroplast transit peptide. The protein
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
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
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