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Recombinant human Carbonic Anhydrase 2 /CA2 Protein, 100µg  

Recombinant human Carbonic Anhydrase 2 /CA2 Protein, 100µg

Recombinant Human Carbonic Anhydrase 2 /CA2 Protein (rhCAII) Ser 2 - Lys 260 was produced in human 293 cells (HEK293)

Synonym: recombinant, human, protein CA2, CA-II, CAII, Car2

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Availability: within 7 days

300,00 €

Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes. CAs form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs rather slowly in the absence of a catalyst. One of the functions of the enzyme in animals is to interconvert carbon dioxide and bicarbonate to maintain acid-base balance in blood and other tissues, and to help transport carbon dioxide out of tissues. The active site of most carbonic anhydrases contains a zinc ion. They are, therefore, classified as metalloenzymes. There are at least five distinct CA families (α, β, γ, δ and ε). These families have no significant amino acid sequence similarity and in most cases are thought to be an example of convergent evolution. The α-CAs are found in humans.[1] Carbonic anhydrase II (CA2) also known as Carbonate dehydratase II, Carbonic anhydrase C, is one of fourteen forms of human α carbonic anhydrases. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of sodium ions in the proximal tubule. Carbonic anhydrase II has been shown to interact with Band 3 and Sodium-hydrogen antiporter 1.[2-5]

Recombinant Human Carbonic Anhydrase 2 /CA2 Protein (rhCAII) Ser 2 - Lys 260 (Accession # NP_000058.1) was produced in human 293 cells (HEK293).

Molecular Characterization
rhCAII, fused with 6×His tag at the C-terminus, has a calculated MW of 30 kDa. The predicted N-terminus is Ser 2. DTT-reduced Protein migrates as 30 kDa.

Less than 1.0 EU per μg of the rhCAII by the LAL method.

>95% purity as determined by SDS-PAGE.

Refer to data sheet

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C-8°C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).

Measured by its esterase activity for digestion of 4­Nitrophenyl Acetate(4­NPA). The specific activity is > 150 pmoles/min/μg.


(1) Badger MR, Price GD, 1994, Annu. Rev. Plant Physiol. Plant Mol. Bio. 45: 369–392.
(2) Nair, S. K. et al., 1991, The Journal of biological chemistry 266 (26): 17320–17325.
(3) Sterling, D., et al., 2001, J. Biol. Chem. (United States) 276 (51): 47886–94.
(4) Vince, J W., et al., 2000, Biochemistry (UNITED STATES) 39 (44): 13344–9.
(5) Li, Xiuju, et al., 2002, J. Biol. Chem. (United States) 277 (39): 36085–91.