Human ACE‑2 APC‑conjugated Antibody

Angiogensin I Converting Enzyme-2 (ACE-2), also called ACEH (ACE homolog), is a type I transmembrane zinc protease that cleaves angiotensins I and II to produce vasodilatory and anti-proliferative peptides. The balance between ACE-1 and ACE-2 activity is critical for maintaining cardiovascular, renal, and pulmonary function (1). ACE-2 also functions as the cellular uptake receptor for the SARS coronoavirus. Within the extracellular domain, human ACE-2 shares 83% aa sequence identity with mouse and rat ACE-2. 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 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 (2). Genetic data from Drosophila, mice and rats show that ACE-2 is an essential regulator of heart function in vivo (3). ACE-2 isoforms of 75 kDa and 120 kDa are differentially expressed between lung and kidney, respectively, and a shed soluble form is generated by TACE/ADAM17 mediated cleavage.