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Mouse Carbonic Anhydrase IV / Car4 Protein (His Tag)

AW456718,Ca4,Car4,RP23-167D6.1

Catalog Number P50350-M08H
Organism Species Mouse
Host Human Cells
Synonyms AW456718,Ca4,Car4,RP23-167D6.1
Molecular Weight The secreted recombinant mouse Car4 consists of 271 amino acids and has a calculated molecular mass of 31 kDa as estimated in SDS-PAGE under reducing conditions.
predicted N Glu 18
SDS-PAGE
Purity > 98 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mouse Car4 (NP_031633.1) without the C-terminal propeptide (Met 1-Ser 277) was expressed,with a C-terminal polyhistidine tag.
Bio-activity Measured by its esterase activity . The specific activity is >10 pmoles/min/μg .
Research Area Cancer |Signal transduction |Metabolism |Mitochondrial
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 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.