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MAK120

Sigma-Aldrich

Urease Activity Assay Kit

sufficient for 100 colorimetric tests

Synonym(s):

Urea Amidohydrolase Activity Assay Kit

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About This Item

UNSPSC Code:
12161503
NACRES:
NA.84

usage

sufficient for 100 colorimetric tests

application(s)

environmental

detection method

colorimetric

relevant disease(s)

gastrointestinal diseases

storage temp.

2-8°C

General description

Urease is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia. Urease is found in bacteria, yeast, and certain higher plant species. Urease activity is found in environmental and fecal samples.

Application

Urease Activity Assay Kit has been used to measure urease activity.

Features and Benefits

Compatible with high-throughput handling systems. Can be adapted for use with cuvettes.

Suitability

Suitable for the detection of Urease activity in biological and environmental samples.

Principle

In this assay, urease catalyzes the hydrolysis of urea resulting in the production of ammonia. The ammonia is determined by the Berthelot method resulting in colorimetric product measure at 670 nm, proportionate to the urease activity present in the sample. One unit of urease is the amount of enzyme that catalyzes the formation of 1.0 μmole ammonia per minute at pH 7.0.

Signal Word

Danger

Hazard Statements

Hazard Classifications

Aquatic Acute 1 - Aquatic Chronic 2 - Eye Dam. 1 - Met. Corr. 1 - Muta. 2 - Skin Corr. 1B

Supplementary Hazards

Storage Class Code

8B - Non-combustible corrosive hazardous materials

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Chelsea M Heveran et al.
Scientific reports, 9(1), 14721-14721 (2019-10-13)
We demonstrate for the first time that the morphology and nanomechanical properties of calcium carbonate (CaCO3) can be tailored by modulating the precipitation kinetics of ureolytic microorganisms through genetic engineering. Many engineering applications employ microorganisms to produce CaCO3. However, control
Ureases I. Functional, catalytic and kinetic properties: A review
Barbara K.
Journal of Molecular Catalysis. B, Enzymatic, 59(1-3), 9-21 (2009)
Isolation, partial purification, characterization and inhibition of urease (EC 3.5. 1.5) enzyme from the Cajanus cajan seeds.
Sujoy B and Aggarwal A
Asian Journal of Bio Science, 7(2), 203-209 (2012)
Ah-Young Jee et al.
Journal of the American Chemical Society, 141(51), 20062-20068 (2019-11-30)
The concept that catalytic enzymes can act as molecular machines transducing chemical activity into motion has conceptual and experimental support, but experimental support has involved oligomeric enzymes, often studied under conditions where the substrate concentration is higher than biologically relevant
Ah-Young Jee et al.
Proceedings of the National Academy of Sciences of the United States of America, 117(47), 29435-29441 (2020-11-11)
Molecular agitation more rapid than thermal Brownian motion is reported for cellular environments, motor proteins, synthetic molecular motors, enzymes, and common chemical reactions, yet that chemical activity coupled to molecular motion contrasts with generations of accumulated knowledge about diffusion at

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