Mouse Carbonic Anhydrase XII (His Tag) recombinant protein

Mouse Carbonic Anhydrase XII (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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 ?-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.

CARBONIC ANHYDRASE XII; CA12; CAR12; HST18816; 2310047E01RIK; CAXII; CARBONIC ANHYDRASE 12; AI314958; FLJ20151

Q8CI85

Human Cells

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.

Mouse

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.

> 95 % as determined by SDS-PAGE

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.