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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
MXP 7,492.00
10 MG
MXP 15,789.00
25 MG
MXP 25,046.00

MXP 7,492.00

Estimated to ship onApril 14, 2025

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5 MG
MXP 7,492.00
10 MG
MXP 15,789.00
25 MG
MXP 25,046.00

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

MXP 7,492.00

Estimated to ship onApril 14, 2025

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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Rui Qiu et al.
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
Liming Luo et al.
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
Vicky De Preter et al.
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
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
View All Related Papers

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