Carbonic Anhydrase III, Recombinant, Human (CAIII, CA3, EC 4.2.1.1, Carbonatedehydratase III)

Carbonic anhydrase is widespread in nature, being found in animals, plants, and certain bacteria. In animals it plays an important role in respiration by facilitating transport of CO2 and is involved in the transfer and accumulation of H+ and HCO3-. In chloroplasts of plant cells the role of carbonic anhydrase may be related to photosynthetic fixation of CO2.\n\nMammalian carbonic anhydrases are of several forms differing in enzymatic properties, amino acid sequences and inhibitor binding. In erythrocytes there is usually present both a high activity and a low activity form. The pH-rate profiles and pH-binding curves indicate that the same group with pKa of approximately seven is involved in both forms. All the isoenzymes have a molecular weight of approximately 30,000 and contain one zinc atom per molecule. Although Deutsch et al. (1972) report six carbonic anhydrases in horse red blood cells, most interest has been focused on high and low activity types. Bovine erythrocytes contain two electrophoretically separable forms designated A and B in order of mobility. Both have a high order of activity similar to the human variant

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SPECIFICATIONS

Catalog Number

C1105-42

Size

5ug

Form

Supplied as a sterile-filtered, blue solution in 1x Laemmli Buffer (25mM Tris-HCl pH6.8, 50mM DTT, 1% SDS, 0.1% Bromophenol Blue) and 2.5% glycerol.

Purity

(same/more than) 95.0% as determined by RP-HPLC, Anion-exchange FPLC, Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. A quantitative study of bioenergetics in skeletal muscle lacking carbonic anhydrase III using 31P magnetic resonance spectroscopy. Proc Natl Acad Sci U S A 2007 Jan 2;104(1):371-6\n2. Direct chemiluminescent imaging detection of Cu/Zn-superoxidase dismutase, glutathione peroxidase, carbonic anhydrase-III, and catalase in rat liver cytosol separated by native porous gradient polyacrylamide gel electrophoresis. Electrophoresis 2005 Nov;26(22):4260-9\n3. Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer. Biochemistry 2005 Aug 2;44(30):10046-53\n4. Suppression of carbonic anhydrase III mRNA level by an aryl hydrocarbon receptor ligand in primary cultured hepatocytes of rat. Biol Pharm Bull 2005 Jun;28(6):1087-90\n5. Carbonic anhydrase III is not required in the mouse for normal growth, development, and life span. Mol Cell Biol 2004 Nov;24(22):9942-7\n6. Anti-oxidative response of carbonic anhydrase III in skeletal muscle. IUBMB Life 2004 Jun;56(6):343-7