C4396
Carbonic Anhydrase I from human erythrocytes
Synonym(s):
Carbonate Dehydratase, Carbonate Hydrolyase, Carbonic Anhydrase Isozyme I
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About This Item
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form
powder
specific activity
100-500 W-A units/mg protein
mol wt
30 kDa
color
white
pI
~6.6
UniProt accession no.
storage temp.
−20°C
Gene Information
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.
Biochem/physiol Actions
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.
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.)
Preparation Note
chromatographically
purified.
purified.
inhibitor
Product No.
Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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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
Cancer letters, 188(1-2), 199-205 (2002-10-31)
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