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Human Carbonic Anhydrase IV / CA4 Protein (His Tag)

CAIV,Car4,RP17

Catalog Number P10472-H08H
Organism Species Human
Host Human Cells
Synonyms CAIV,Car4,RP17
Molecular Weight The recombinant human CA4 consists of 276 amino acids after removal of the signal peptide and has a predicted molecular mass of 31.7 kDa. In SDS-PAGE under reducing conditions, rh CA4 migrates as an approximately 30 kDa band.
predicted N Ala 19
SDS-PAGE
Purity > 96 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human CA4 (NP_000708.1) (Met1-Lys283) without the pro peptide was expressed, fused with a polyhistidine tag at the C-terminus.
Bio-activity Measured by its esterase activity . The specific activity is >2 pmoles/min/μg.
Research Area Cancer |Signal transduction |Metabolism |Mitochondrial
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background 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 IV (CAIV) is a membrane-associated enzyme anchored to plasma membrane surfaces by a phosphatidylinositol glycan linkage. CAIV is a high-activity isozyme in CO2 hydration comparable to that of CAII. Furthermore, CAIV is more active in HCO3- dehydration than is CAII. However, the esterase activity of CAIV is decreased 150-fold compared to CAII.
Reference
  • 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.
  • Baird TT, et al. (1997) Catalysis and Inhibition of Human Carbonic Anhydrase IV. Biochemistry. 36 (9): 2669-78.