Spike S1 RBD (SARS-CoV-2): ACE2 Inhibitor Screening Assay Kit
The pandemic coronavirus disease 2019 (COVID-19) is caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2). As a first step of the viral replication strategy, the virus attaches to the host cell surface before entering the cell. The Spike protein receptor binding domain (RBD) recognizes and attaches to the Angiotensin-Converting Enzyme 2 (ACE2) receptor found on the surface of type I and II pneumocytes, endothelial cells, and ciliated bronchial epithelial cells. Drugs targeting the interaction between the Spike protein of SARS-CoV-2 and ACE2 may offer some protection against the viral infection.
The Spike S1 RBD (SARS-CoV-2): ACE2 Inhibitor Screening Assay Kit is designed for screening and profiling inhibitors of this interaction. The key to this kit is the high sensitivity of detection of bound His-labeled ACE2 by HRP-labeled Anti-His. Only a few simple steps on a microtiter plate are required for the assay. First, SARS-CoV-2 Spike S1 is coated on a 96-well plate. Next, ACE2-His is incubated with SARS-CoV-2 Spike S1 on the plate. Finally, the plate is treated with Anti-His-HRP followed by addition of an HRP substrate to produce chemiluminescence, which then can be measured using a chemiluminescence reader.
This product has been cited 15 times.
PBS (Phosphate buffered saline)
Luminometer or microplate reader capable of reading chemiluminescence
Adjustable micropipettor and sterile tips
Catalog # | Component | Amount | Storage | |
100684 | SARS-CoV-2 Spike S1 Protein (RBD), mFc Tag | 5 μg | -80°C | Avoid multiple freeze/ thaw cycles! |
11003 | ACE2, His-Tag | 5 μg | -80°C | |
79311 | 3x Immuno Buffer 1 | 50 ml | -20°C | |
79728 | Blocking Buffer 2 | 50 ml | +4°C | |
Anti-His-HRP | 10 μl | -80°C | ||
79670 | ELISA ECL substrate A (transparent bottle) | 6 ml | Room Temp |
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ELISA ECL substrate B (brown bottle) | 6 ml | Room Temp |
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79699 | 96-well white microplate | 1 | +4°C |
Hoffmann, M. et al. 2020. Cell, 181:1-10
Yan, R. et al. Science, In Press 4 March 2020. DOI: 10.1126/science.abb2762