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Carbonic Anhydrase III / CA3 항체, 토끼 단클론항체

데이터시트리뷰프로토콜
제품 설명: Active  
발현 숙주: E. coli  
  • Slide 1
10503-H08E-50
10503-H08E-100
50 µg 
100 µg 
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Carbonic Anhydrase III antibody 연구배경

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.

Carbonic anhydrase 3, also known as Carbonate dehydratase III, CA-III and CA3, is a cytoplasm protein which belongs to the alpha-carbonic anhydrase family. CA3 is activated by proton donors such as imidazole and the dipeptide histidylhistidine. It is inhibited by coumarins and sulfonamide derivatives such as acetazolamide. At 6 weeks gestation, transcripts accumulate at low levels in the somites and at high levels throughout the notochord. As gestation continues, CA3 becomes abundant in all developing muscle masses and continues at high to moderate levels in the notochord.

휴먼 Carbonic Anhydrase III antibody 참고자료
  • Ivanov, S.V. et al., 1998, Proc. Natl. Acad. Sci. USA 95:12596-601.
  • Sowden J. et al., 1998, Gene 214:157- 65.
  • Strausberg, R.L. et al., 2002, Proc. Natl. Acad. Sci. USA 99:16899-903.
  • Liao, S.Y. et al., 2003, J. Med. Genet. 40: 257-62.
  • Bataller,L. et al., 2004, Ann Neurol  56 (4): 575-9.
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