U7752
Urease from Canavalia ensiformis (Jack bean)
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About This Item
Productos recomendados
biological source
Canavalia ensiformis
Quality Level
form
solid
mol wt
hexamer 545 kDa
trimer ~272 kDa
contains
~20% dithiothreitol
suitability
suitable for marker for electrophoresis (non-denaturing PAGE)
storage temp.
−20°C
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General description
Subunit molecular weight: ~90,770
Composed of six subunits with total molecular weight: ~544,620
Composed of six subunits with total molecular weight: ~544,620
Urease is a multi-subunit nickel-dependent metalloenzyme. It is found abundantly in fungi, yeast, plants, and bacteria. It belongs to the superfamily of amidohydrolases and phosphotriesterases. Urease is also found in leguminous seeds.
Application
Urease from Canavalia ensiformis (Jack bean) has been used:
- as a component of the molecular mass standard in electrophoresis
- as a component of the standard in size-exclusion chromatography
- as a reference in native-polyacrylamide gel electrophoresis (PAGE)
Biochem/physiol Actions
Urease is an essential enzyme of the nitrogen cycle. It plays a role in degrading urea into ammonia and carbamate. Urease provides a source of nitrogen for growth to various organisms. It also plays a major role in seed germination and seed chemical defense.
Other Notes
Contains approx. 1 mg protein
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
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Paweł Kafarski et al.
Journal of advanced research, 13, 101-112 (2018-08-11)
Urease is a nickel-dependent metalloenzyme found in plants, some bacteria, and fungi. Bacterial enzyme is of special importance since it has been demonstrated as a potent virulence factor for some species. Especially it is central to Helicobacter pylori metabolism and
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Anuradha Balasubramanian et al.
Journal of molecular biology, 400(3), 274-283 (2010-05-18)
Urease, a nickel-dependent metalloenzyme, is synthesized by plants, some bacteria, and fungi. It catalyzes the hydrolysis of urea into ammonia and carbon dioxide. Although the amino acid sequences of plant and bacterial ureases are closely related, some biological activities differ
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