Anti-CA2 Antibody Picoband® (monoclonal, 10E11) Fluoro488 Conjugated

CA2 is a cytosolic enzyme with the highest activity among all known CAs. The carbonic anhydrases (ACs) 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 relatively slowly in the absence of a catalyst. Mutations in the CA2 gene result in the CA II deficiency syndrome, an autosomal recessive disorder that produces osteopetrosis, renal tubular acidosis and cerebral calcification. This gene is mapped to 8q22.

E.coli-derived human CA2 recombinant protein (Position: S2-K260) . Human CA2 shares 81.1% and 80.7% amino acid (aa) sequence identity with mouse and rat CA2, respectively.

Essential for bone resorption and osteoclast differentiation. Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.

1.Aramaki, S., Yoshida, I., Yoshino, M., Kondo, M., Sato, Y., Noda, K., Jo, R., Okue, A., Sai, N., Yamashita, F. Carbonic anhydrase II deficiency in three unrelated Japanese patients. J. Inherit. Metab. Dis. 16: 982-990, 1993. 2.Laitala, T., Vaananen, H. K. Inhibition of bone resorption in vitro by antisense RNA and DNA molecules targeted against carbonic anhydrase II or two subunits of vacuolar H (+) -ATPase. J. Clin. Invest. 93: 2311-2318, 1994. 3.Venta, P. J., Welty, R. J., Johnson, T. M., Sly, W. S., Tashian, R. E. Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107his-to-tyr) : complete structure of the normal human CA II gene. Am. J. Hum. Genet. 49: 1082-1090, 1991.