Call Now

Mouse Carbonic Anhydrase XII / Car12 Protein (His Tag)

2310047E01Rik,AI314958,Car12

Catalog Number P50014-M08H
Organism Species Mouse
Host Human Cells
Synonyms 2310047E01Rik,AI314958,Car12
Molecular Weight The secreted recombinant mouse CA12 consists of 288 amino acids and has a calculated molecular mass of 32.8 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 40-45 kDa protein in SDS-PAGE under reducing conditions.
predicted N Ala 25
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the extracellular domain (Met 1-Ser 301) of mouse CA12 (NP_848483.2) precursor was expressed with a C-terminal polyhistidine tag.
Bio-activity Measured by its esterase activity. The specific activity is >50 pmoles/min/μg, as measured with 1 mM 4-Nitrophenyl acetate and 0.4 μg enzyme at 400 nm in 100 μL of 12.5 mM Tris, 75 mM NaCl, pH 7.5.
Research Area Cardiovascular |Cardiovascular disease Therapeutic Targets |Hypertension Therapeutic Targets
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 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. CA12, also known as Car12 and carbonic anhydrase XII, is a type I  membrane enzyme of an N-terminal extracellular catalytic domain, a membrane-spanning α-helix, and a small intracellular C-terminal domain. It is highly expressed in colon, kidney, prostate, intestine and activated lymphocytes and moderately expressed in pancreas, ovary, and testis. Overexpression of the CA12 is observed in certain human cancers and is used as a tumor marker. rmCA12 corresponds to the extracellular domain and has both carbonic anhydrase activity and esterase activity.
Reference
  • Sahin, U. et al., 1996, Proc. Natl. Acad. Sci. U.S.A. 92 (25): 11810–11813.
  • Ivanov, S.V. et al., 1998, Proc. Natl. Acad. Sci. USA 95:12596 - 12601.
  • Strausberg, R.L. et al., 2002, Proc. Natl. Acad. Sci. USA 99:16899 - 16903.
  • Liao, S.Y. et al., 2003, J. Med. Genet. 40:257 - 262.
  • Supuran, C. T. et al., 2008, Curr Pharm Des. 14 (7): 601-602.
  • Elleuche, S. et al., 2009, Curr Genet. 55 (2): 211-222.