Mouse Angiotensin I Converting Enzyme 2 ACE2 ELISA Kit

Kit Components

 1. Recombinant Mouse ACE2 standard: 2 vials

 2. One 96-well plate precoated with anti- Mouse ACE2  Ab

 3. Sample diluent buffer: 12 mL - 1

 4. Detection antibody: 130 µL, dilution 1:100

 5. Streptavidin-HRP: 130 µL, dilution 1:100

 6. Antibody diluent buffer: 12 mL x1   

 7. Streptavidin-HRP diluent buffer: 12 mL x1

 8. TMB developing agent: 10 mL x1

9. Stop solution: 10 mL x1.

10. Washing solution (20x): 25 mL x1.

Background

Angiotensin I Converting Enzyme (ACE), also known as peptidyl-dipeptidase A or CD143, is a zinc metallopeptidase which is capable of releasing a C-terminal dipeptide featured with oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Therefore, it can cleave the C-terminal dipeptide from angiotensin I to produce the octapeptide angiotensin II, a potent vasopressor. It also inactivates the potent vasodilator, bradykinin, by the sequential removal of two C-terminal dipeptides. Two alternatively spliced ACE isoforms have been identified. The somatic ACE (sACE), found in endothelial, epithelial and neuronal cells, is made up of two highly similar active domains termed N- and C-domains containing the HExxH consensus sequence for zinc binding. The germinal ACE (gACE), found exclusively in the testes, is composed of a gACE-specific 67 amino acid sequence at N-terminus and a single catalytically active domain identical to the C-domain of sACE. Physiological functions of the two tissue-specific isozymes are not interchangeable. ACE plays an important role in blood pressure control and water and salt metabolism. In addition, it has showed diverse functions in immunity, reproduction and neuropeptide regulation. For example, ACE degrades Alzheimer amyloid β peptide (Aβ), retards Aβ aggregation, deposition, fibril formation, and inhibits cytotoxicity.

ACE2, also termed ACE-related carboxypeptidase, Metalloprotease MPROT15 or ACEH (ACE homolog), is a member of the ACE family. The mouse ACE 2 is a predicted 798 amino acid protein consisting of an N-terminal signal peptide, a single catalytic domain, a C- terminal membrane anchor, and a short cytoplasmic tail.  ACE-2 is expressed primarily in testis, kidney and heart and at moderate levels in colon, small intestine and ovary. As a carboxypeptidase, ACE-2 cleaves angiotensins I and II. Notably, classical ACE inhibitors such as captopril and lisinopril do not inhibit ACE-2 activity. Novel peptide inhibitors of ACE-2 do not inhibit ACE activity. Genetic analysis shows that ACE-2 is an essential regulator of heart function in vivo.