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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

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5 MG
€434.00
10 MG
€802.00
25 MG
€1,010.00

€434.00

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5 MG
€434.00
10 MG
€802.00
25 MG
€1,010.00

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

€434.00

In StockDetails

type

Type II

Quality Level

200

form

essentially salt-free, lyophilized powder

specific activity

100-300 units/mg solid

storage temp.

−20°C

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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 [1]. Rhodanese is used to study sulfur energy metabolism [2].

Biochem/physiol Actions

Rhodanese (RHOD) is the principal enzyme involved in hydrogen sulphide (H2S) detoxication in the colonic luman [1].

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

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Certificates of Analysis (COA)

Lot/Batch Number
086K7455
108H7830
102H9530
021K7450

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Girish C Melkani et al.
Bioscience reports, 32(3), 299-303 (2012-01-26)
The chaperonin GroEL binds to non-native substrate proteins via hydrophobic interactions, preventing their aggregation, which is minimized at low temperatures. In the present study, we investigated the refolding of urea-denatured rhodanese at low temperatures, in the presence of ox-GroEL (oxidized
Clément Aussignargues et al.
The Journal of biological chemistry, 287(24), 19936-19948 (2012-04-13)
How microorganisms obtain energy is a challenging topic, and there have been numerous studies on the mechanisms involved. Here, we focus on the energy substrate traffic in the hyperthermophilic bacterium Aquifex aeolicus. This bacterium can use insoluble sulfur as an
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
Eda Koculi et al.
Protein science : a publication of the Protein Society, 20(8), 1380-1386 (2011-06-03)
Nuclear magnetic resonance (NMR) observation of the uniformly (2) H,(15) N-labeled stringent 33-kDa substrate protein rhodanese in a productive complex with the uniformly (14) N-labeled 400 kDa single-ring version of the E. coli chaperonin GroEL, SR1, was achieved with the
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
View All Related Papers

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