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Key Documents

U7752

Sigma-Aldrich

Urease from Canavalia ensiformis (Jack bean)

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

Canavalia ensiformis

Niveau de qualité

Forme

solid

Poids mol.

hexamer 545 kDa
trimer ~272 kDa

Contient

~20% dithiothreitol

Adéquation

suitable for marker for electrophoresis (non-denaturing PAGE)

Température de stockage

−20°C

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Description générale

Subunit molecular weight: ~90,770
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)

Actions biochimiques/physiologiques

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.

Autres remarques

Contains approx. 1 mg protein

Pictogrammes

Health hazardExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1


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Consulter la Bibliothèque de documents

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
Suchithra Menon et al.
Cell, 156(4), 771-785 (2014-02-18)
mTORC1 promotes cell growth in response to nutrients and growth factors. Insulin activates mTORC1 through the PI3K-Akt pathway, which inhibits the TSC1-TSC2-TBC1D7 complex (the TSC complex) to turn on Rheb, an essential activator of mTORC1. However, the mechanistic basis of how
Muhammad Ajmal Rana et al.
PloS one, 16(10), e0258568-e0258568 (2021-10-15)
Urea is the most popular and widely used nitrogenous fertilizer. High soil urease activity rapidly hydrolyses applied urea to ammonia which contributes to soil nitrogen (N) losses and reduces N use efficiency of crop plants. The ammonia losses can be
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
Keith J Mickolajczyk et al.
eLife, 11 (2022-02-12)
Catch bonds are a form of mechanoregulation wherein protein-ligand interactions are strengthened by the application of dissociative tension. Currently, the best-characterized examples of catch bonds are between single protein-ligand pairs. The essential AAA (ATPase associated with diverse cellular activities) mechanoenzyme

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