Carbonic anhydrase II cDNA ORF Clone, Human, C-HA tag General Information
Full length Clone DNA of Human carbonic anhydrase II with C terminal HA tag.
Enhanced CMV promoter
HA Tag Sequence: TATCCTTACGACGTGCCTGACTACGCC
T7( 5' TAATACGACTCACTATAGGG 3' )
BGH( 5' TAGAAGGCACAGTCGAGG 3' )
The plasmid is confirmed by full-length sequencing.
Antibiotic in E.coli
Antibiotic in Mammalian cell
Stable or Transient mammalian expression
Storage & Shipping
Each tube contains lyophilized plasmid.
The lyophilized plasmid can be stored at ambient temperature for three months.
**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**
Carbonic anhydrase II cDNA ORF Clone, Human, C-HA tag Alternative Names
CA-II cDNA ORF Clone, Human;CAC cDNA ORF Clone, Human;CAII cDNA ORF Clone, Human;Car2 cDNA ORF Clone, Human;HEL-76 cDNA ORF Clone, Human;HEL-S-282 cDNA ORF Clone, Human
Carbonic anhydrase II Background Information
The carbonic anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The carbonic anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. Carbonic anhydrase II 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.
carbonic anhydrase II
Lehtonen J, et al. (2004) Characterization of CA XIII, a Novel Member of the Carbonic Anhydrase Isozyme Family. The Journal of Biological Chemistry. 279: 2719-27.Lindskog S. (1997) Structure and mechanism of carbonic anhydrase. Pharmacology & Therapeutics. 74(1)：1-20．Lilias A, et al. (1972) Crystal Structure of Human Carbonic Anhydrase C. Nature new biology. 235: 131-7.Li XJ, et al. (2002) Carbonic Anhydrase II Binds to and Enhances Activity of the Na+/H+ Exchanger. The Journal of Biological Chemistry. 277: 36085-91.