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C4396

Sigma-Aldrich

Carbonic Anhydrase I from human erythrocytes

Synonyme(s) :

Carbonate Dehydratase, Carbonate Hydrolyase, Carbonic Anhydrase Isozyme I

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About This Item

Numéro CAS:
9001-03-0
Numéro de classification (Commission des enzymes):
4.2.1.1 (BRENDA, IUBMB)
Numéro CE :
232-576-6
Numéro MDL:
MFCD00081467
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.25

Forme

powder

Activité spécifique

100-500 W-A units/mg protein

Poids mol.

30 kDa

Couleur

white

pl 

~6.6

Numéro d'accès UniProt

P00915

Température de stockage

−20°C

Informations sur le gène

human ... CA1(759)

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Application

Carbonic anhydrase from human erythrocytes (HCA) has been used to study the molten-globule state of carbonic anhydrase (CA). Chaperone-like α-crystallin binds to this state of the enzyme and prevents its aggregation. The enzyme from sigma has been used for the analysis of thermodynamic stability of the enzyme. Furthermore, its clinical significance has been evaluated in human non-small cell lung cancer.

Actions biochimiques/physiologiques

Carbonic anhydrase is a zinc metalloenzyme that has a molecular weight of approximately 30,000 Da. The enzyme catalyzes the hydration of carbon dioxide to carbonic acid. It is involved in vital processes such as pH and CO2 homeostasis, transport of bicarbonate and CO2, biosynthetic reactions, bone resorption, calcification, and tumorigenicity. Therefore, this enzyme is an important target for inhibitors with clinical applications in various pathologies such as glaucoma, epilepsy and Parkinson′s disease.

Définition de l'unité

One Wilbur-Anderson (W-A) unit will cause the pH of a 0.02 M Trizma buffer to drop from 8.3 to 6.3 per min at 0 °C. (One W-A unit is essentially equivalent to one Roughton-Booth unit.)

Notes préparatoires

chromatographically
purified.

Inhibiteur

Réf. du produit
Description
Tarif

C4911

Chlorothiazide, thiazide diuretic

A6011

Acetazolamide, ≥99%, powder

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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K Rajaraman et al.
The Journal of biological chemistry, 271(44), 27595-27600 (1996-11-01)
alpha-Crystallin, a multimeric protein, exhibits chaperone-like activity in preventing aggregation of several proteins. We have studied the chaperone-like activity of alpha-crystallin toward heat-induced aggregation of bovine and human carbonic anhydrase. Human carbonic anhydrase aggregates at 60 degrees C, while bovine
Whei Ling Chiang et al.
Cancer letters, 188(1-2), 199-205 (2002-10-31)
This study was designed to elucidate the possible relationship between the expression of cytosolic carbonic anhydrase (CA) and non-small cell lung cancer (NSCLC). The activity and protein expression patterns of carbonic anhydrase I (CAI) and II (CAII) of 70 NSCLC
Daumantas Matulis et al.
Biochemistry, 44(13), 5258-5266 (2005-03-30)
ThermoFluor (a miniaturized high-throughput protein stability assay) was used to analyze the linkage between protein thermal stability and ligand binding. Equilibrium binding ligands increase protein thermal stability by an amount proportional to the concentration and affinity of the ligand. Binding
Qiang Jin et al.
Biosensors & bioelectronics, 83, 193-199 (2016-04-30)
A near-infrared fluorescent probe (DDAB) for highly selective and sensitive detection of carboxylesterase 2 (CE2) has been designed, synthesized, and systematically studied both in vitro and in vivo. Upon addition of CE2, the ester bond of DDAB could be rapidly
Pavel V Shliaha et al.
Journal of proteome research, 12(6), 2323-2339 (2013-03-22)
qTOF mass spectrometry and traveling wave ion mobility separation (TWIMS) hybrid instruments (q-TWIMS-TOF) have recently become commercially available. Ion mobility separation allows an additional dimension of precursor separation inside the instrument, without incurring an increase in instrument time. We comprehensively
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Protocoles

Enzymatic Assay of Carbonic Anhydrase for Wilbur-Anderson Units (EC 4.2.1.1)

Objective: To standardize a procedure for the enzymatic assay of Carbonic Anhydrase (EC 4.2.1.1) for Wilbur-Anderson Units.

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