Human ACE-2 Antibody Summary
Gln18-Ser740
Accession # Q9BYF1
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Human ACE‑2 by Western Blot. Western blot shows lysates of human kidney. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human ACE‑2 Monoclonal Antibody (Catalog # MAB10821) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (HAF018). A specific band was detected for ACE‑2 at approximately 120 kDa (as indicated). This experiment was conducted under reducing conditions and using Western Blot Buffer Group 1.
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Detection of Human ACE‑2 by Simple WesternTM. Simple Western lane view shows lysates of human kidney, loaded at 0.2 mg/mL. A specific band was detected for ACE‑2 at approximately 153 kDa (as indicated) using 20 µg/mL of Mouse Anti-Human ACE‑2 Monoclonal Antibody (Catalog # MAB10821). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: ACE-2
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).
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- Yan, et al. (2020) Science 367:1444.
- Tipnis, S.R. et al. (2000) J. Biol. Chem. 275:33238.
- Kuba, K. et al. (2005) Nature Med. 11:875.
- Hoffmann, M. et al. (2020) Cell.181:1.
- Wrapp, et al. (2020) Science 367:1260.
- Imai, Y. et al. (2005) Nature 436:112.
- Huang, L. et al. (2003) J. Biol. Chem. 278:15532.
- Schrom, E. et al. (2017) Mol. Therapy Nuc. Acid 7:350.
- Jia, H. et al. (2016) Shock. 46:239.
- Cole-Jeffrey, C.T. et al. (2015) J. Cadiovasc. Pharmacol. 66:540.
- Towler, P. et al. (2004) J. Biol. Chem. 279:17996.
- Crackower, M.A. et al. (2002) Nature 417:822.
Product Datasheets
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