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C4396
Kohlensäureanhydrase I aus Humanerythrocyten
Synonym(e):
Carbonat-Dehydratase, Carbonat-Hydro-Lyase
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About This Item
Empfohlene Produkte
Form
powder
Qualitätsniveau
Spezifische Aktivität
100-500 W-A units/mg protein
Mol-Gew.
30 kDa
Farbe
white
pI
~6.6
UniProt-Hinterlegungsnummer
Lagertemp.
−20°C
Angaben zum Gen
human ... CA1(759)
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Anwendung
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. Wirkung
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.
Einheitendefinition
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.)
Angaben zur Herstellung
chromatographically
purified.
purified.
Inhibitor
Produkt-Nr.
Beschreibung
Preisangaben
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
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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
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
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
Protokolle
Enzymatic Assay of Carbonic Anhydrase for Wilbur-Anderson Units (EC 4.2.1.1)
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