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C7749

Sigma-Aldrich

Carbonic Anhydrase II bovine

≥90% (SDS-PAGE), recombinant, expressed in E. coli, ≥5,000 units/mg protein, buffered aqueous solution

Synonyme(s) :

Bovine carbonic anhydrase, Carbonic anhydrase enzyme

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About This Item

Numéro de classification (Commission des enzymes):
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in E. coli

Niveau de qualité

Pureté

≥90% (SDS-PAGE)

Forme

buffered aqueous solution

Activité spécifique

≥5,000 units/mg protein

Poids mol.

~29 kDa

Conditions d'expédition

wet ice

Température de stockage

−20°C

Application

Carbonic Anhydrase II bovine has been used as a control in native gel electrophoresis and X-ray absorption spectroscopy characterization of Thalassiosira weissflogii carbonic anhydrase 1.
Carbonic anhydrase is used to create carbon dioxide capture systems and to research various purification techniques . Carbonic anhydrase is also used to study acid-base regulation in fish and carbonic anhydrase type II deficiency syndrome . Product C7749, Bovine carbonic anhydrase II (CA II), has been widely used as a model protein in the investigation of the protein folding process.

Actions biochimiques/physiologiques

Carbonic Anhydrase is a zinc-containing enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate. One of its main physiological roles is to maintain the acid-base balance in blood and other tissues. Lack of carbonic anhydrase results in carbonic anhydrase type II deficiency syndrome, which is an autosomal recessive disease that causes osteopetrosis, renal tubular acidosis and brain calcifications . Carbonic anhydrases are metalloenzymes since most active sites contain zinc. Carbonic anhydrases are widely distributed in plant and animal tissues where they are involved in diverse physiological processes, such as photosynthesis, pH homeostasis, calcification, and bone resorption. The enzymes can be localized in the cytosol or mitochondria, be membrane bound with extracellular domains, or be secreted. Bovine carbonic anhydrase II (CA II) is a cytosolic, single-chain, approximately 29 kDa enzyme.

Définition de l'unité

One unit will decrease th pH of a 20 mM tris buffer from pH 8.3 to 6.3 per minute at 0 °C.

Forme physique

Supplied as a solution in 20 mM Tris, pH 7.6, with 150 mM NaCl.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

The active site structure of Thalassiosira weissflogii carbonic anhydrase 1
Cox EH, et al.
Biochemistry, 39(40), 12128-12130 (2000)
K M Gilmour et al.
The Journal of experimental biology, 212(Pt 11), 1647-1661 (2009-05-19)
Carbonic anhydrase (CA) is the zinc metalloenzyme that catalyses the reversible reactions of CO(2) with water. CA plays a crucial role in systemic acid-base regulation in fish by providing acid-base equivalents for exchange with the environment. Unlike air-breathing vertebrates, which
Joana da Costa Ores et al.
Chemosphere, 88(2), 255-259 (2012-04-20)
This work presents a study of industrially applicable techniques to obtain a biologically supported carbon dioxide capture system, based on the extraction of carbonic anhydrase from bovine blood. Carbonic anhydrase is a metalloenzyme which catalyzes the reversible hydration of carbon
Thomas M Bosley et al.
Brain : a journal of neurology, 134(Pt 12), 3502-3515 (2011-11-29)
Carbonic anhydrase type II deficiency syndrome is an uncommon autosomal recessive disease with cardinal features including osteopetrosis, renal tubular acidosis and brain calcifications. We describe the neurological, neuro-ophthalmological and neuroradiological features of 23 individuals (10 males, 13 females; ages at
Wolfgang Maret
Advances in nutrition (Bethesda, Md.), 4(1), 82-91 (2013-01-16)
The nutritional essentiality of zinc for the growth of living organisms had been recognized long before zinc biochemistry began with the discovery of zinc in carbonic anhydrase in 1939. Painstaking analytical work then demonstrated the presence of zinc as a

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