Human ACE‑2 Antibody

Angiotensin I Converting Enzyme (ACE-2), also called ACEH (ACE homologue), is a dimeric, zinc-dependent metalloprotease of the ACE family that also includes somatic and germinal ACE (1, 2). ACE-2 mRNA is found at high levels in heart, testis, and kidney and at lower levels in a wide variety of tissues (1, 3). ACE-2 is the SARS-CoV and SARS-CoV2 Spike protein receptor in vivo (4-6), functions catalytically as a carboxypeptidase to cleave several substrates including angiotensins I and II, and acts as a partner for B0AT1-family amino acid transporters (1, 2). Through these functions, ACE-2 has been shown to be involved in several diseases including SARS, COVID19, acute lung injury (4, 7), heart disease (8), liver and lung fibrosis (9), inflammatory lung disease (10), and cardiopulmonary disease (11). Full length ACE-2 protein includes an extracellular region composed of a single N-terminal peptidase domain and C-terminal collectrin-like domain (CLD), a transmembrane domain, and a short cytoplasmic tail (12). The N-terminal peptidase region is required for binding to SARS-CoV and SARSCoV2 spike proteins, while the CLD contains a region that promotes dimerization and association with amino acid transporters (2). The peptidase domain contains a long deep cleft that undergoes a large hinge-bending movement at substrate and inhibitor binding (12).  Classical ACE inhibitors such as captopril and lisinopril do not inhibit ACE-2 activity and inhibitors of ACE-2 do not inhibit ACE activity (13).