Angiotensin Converting Enzyme, ACE, human

Angiotensin I converting enzyme (ACE) catalyzes the formation of angiotensin II from angiotensin I. It is a membrane-bound enzyme, which is expressed in atherosclerotic lesions. It plays an important role in the development of various diseases like systemic lupus erythematosus, hypertension, chronic kidney disease and diabetic nephropathy.

The specific activity of recombinant human ACE is measured by its ability to cleave hippuryl-HIS-LEU

Recombinant human Angiotensin Converting Enzyme (ACE) is expressed in human HEK 293 cells as a glycoprotein with a calculated molecular mass of 138 kDa (amino acids 30-1232). The DTT-reduced protein migrates as a 180 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher specific activity of the protein. The protein is produced with no artificial tags.

The ACE gene codes for angiotensin-converting enzyme, which is one of the major enzymes in the RAS (renin angiotensin system). The ACE gene is localized on human chromosome 17q23.

One unit is defined as the amount of enzyme required to produce 1.0 micromole of hippuric acid from hippuryl-HIS-LEU per minute in 50 mM HEPES and 300 mM NaCl at pH 8.3 at 37 ^oC.

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4.