Carbonic Anhydrase II / CA2 Antikörper (Antigen Affinität reinigt)

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Carbonic anhydrases (Cas) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. Carbonic anhydrases (CAs) form a family of enzymes that catalyze the rapid conversion of carbon dioxide and water to bicarbonate and protons, a reaction that occurs rather slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion, they are therefore classified as metalloenzymes. Several forms of carbonic anhydrase occur in nature. The primary function of the enzyme in animals is to interconvert carbon dioxide and bicarbonate to maintain acid-base balance in blood and other tissues, and to help transport carbon dioxide out of tissues. Plants contain a different form called β-carbonic anhydrase, which, from an evolutionary standpoint, is a distinct enzyme, but participates in the same reaction and also uses a zinc ion in its active site. Mouse carbonic anhydrase 2, also known as Carbonic anhydrase II, Carbonate dehydratase II, Carbonic anhydrase C and CA2, is cytoplasm protein which belongs to thealpha-carbonic anhydrase family. CA2 is essential for bone resorption and osteoclast differentiation. CA2 can hydrates cyanamide to urea. It is involved in the regulation of fluid secretion into the anterior chamber of the eye. Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone.

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