Anti-ACE2 (Capture/Detector)

ACE-2, also called ACEH (ACE homolog), is an integral membrane protein and a zinc metalloprotease of the ACE family that also includes somatic and germinal ACE . Human ACE-2 has about 40% amino acid identity to the N- and C-terminal domains of human somatic ACE. The predicted human ACE-2 protein sequence consists of 805 amino acids, including a N-terminal signal peptide, a single catalytic domain, a C-terminal membrane anchor, and a short cytoplasmic tail. ACE-2 cleaves angiotensins I and II as a carboxypeptidase. ACE-2 Mrna is found at high levels in testis, kidney, and heart and at moderate levels in colon, small intestine, and ovary. 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 data from Drosophila, mice and rats show that ACE-2 is an essential regulator of heart function in vivo. Protein function: Essential counter-regulatory carboxypeptidase of the renin- angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity. [The UniProt Consortium]