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C6165

Sigma-Aldrich

Carbonic Anhydrase Isozyme II human

≥80%, powder, ≥3,000 W-A units/mg protein

Synonym(s):

Carbonate Dehydratase, Carbonate Hydrolyase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

Assay

≥80%

form

powder

specific activity

≥3,000 W-A units/mg protein

mol wt

30 kDa

color

white

pI 

~7.4

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... CA2(760)

Application

Human carbonic anhydrase isozyme II has been used to assess its gene fusion abilities for efficient expression and recovery of recombinant proteins. Human carbonic anhydrase isozyme II has also been used to investigate a new process for the synthesis of difluoromethanesulfonamides. Furthermore, CA II from Sigma has been used as a standard to measure the CA activity in lung tissue homogenates. The study analysed the possible relationship between the expression of carbonic anhydrase and non-small cell lung cancer. The product has also been used with Freund′s complete adjuvant at 1:1 ratio for antibody production. This study evaluated the quantitative and functional alterations of cytosolic CA isoenzymes in the erythrocytes of glucose-6-phosphate dehydrogenase (G6PD)-deficient individuals. The enzyme has also been used in the study of natural phenolic inhibitors of CA II.

Biochem/physiol Actions

Carbonic anhydrase is a zinc metalloenzyme that catalyzes the hydration of carbon dioxide to carbonic acid. It is involved in pathological and physiological 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 that can be used for treating various pathological conditions such as glaucoma, epilepsy and Parkinson′s disease. CAII has a molecular mass of approximately 30 kDa and is primarily present in type II pneumocytes. Due to this unique location it has been speculated that CAII is involved in pulmonary functions such as regulation of fluid secretion and CO2 elimation. Sulfonamides, sulfamates and sulfamides are potent inhibitors of CA.

Unit Definition

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.)

inhibitor

Product No.
Description
Pricing

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Ghita Ghislat et al.
Biomolecules, 10(11) (2020-11-25)
Background and purpose: Identifying the macromolecular targets of drug molecules is a fundamental aspect of drug discovery and pharmacology. Several drugs remain without known targets (orphan) despite large-scale in silico and in vitro target prediction efforts. Ligand-centric chemical-similarity-based methods for
Shinya Tsukiji et al.
Methods in molecular biology (Clifton, N.J.), 1266, 243-263 (2015-01-07)
Introducing nongenetically encoded, synthetic probes into specific proteins is now recognized as a key component in chemical biology. In particular, the ability to chemically modify specific "native" proteins in various contexts from in vitro to cellular systems is of fundamental
W L Chiang et al.
Clinica chimica acta; international journal of clinical chemistry, 314(1-2), 195-201 (2001-11-24)
This study was designed to evaluate the quantitative and activity alterations of cytosolic carbonic anhydrase (CA) isoenzymes in the erythrocytes of glucose-6-phosphate dehydrogenase (G6PD)-deficient individuals. Western Blot and CA esterase activity analysis were employed to measure cytosolic erythrocyte CA isoenzymes.
Screening and docking studies of natural phenolic inhibitors of carbonic anhydrase II
Huang HQ, et al.
Science in China. Series B, Chemistry, Life Sciences & Earth Sciences, 52(3), 332-337 (2009)
Peiwen Pan et al.
Journal of medicinal chemistry, 56(4), 1761-1771 (2013-02-09)
An α-carbonic anhydrase (CA, EC 4.2.1.1) has been identified, cloned, and characterized from the unicellular protozoan Trypanosoma cruzi, the causative agent of Chagas disease. The enzyme (TcCA) has a very high catalytic activity for the CO2 hydration reaction, being similar

Protocols

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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