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Simultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay
JCI Insight.2021-08;
Ester Lopez, Ebene R Haycroft, Amy Adair, Francesca L Mordant, Matthew T O'Neill, Phillip Pymm, Samuel J Redmond, Wen Shi Lee, Nicholas A Gherardin, Adam K Wheatley, Jennifer A Juno, Kevin J Selva, Samantha K Davis, Samantha L Grimley, Leigh Harty, Damian Fj Purcell, Kanta Subbarao, Dale I Godfrey, Stephen J Kent, Wai-Hong Tham, Amy W Chung
… using identical protocols as control proteins. Coupling efficiency of the recombinant RBD
was assessed using an anti-His Tag antibody (A00174, GenScript Corporation). A complete
list of the magnetic bead regions and respective RBD variants is in Supplemental Table 3. …
The SARS-CoV-2 receptor binding domain (RBD) is both the principal target of neutralizing antibodies and one of the most rapidly evolving domains, which can result in the emergence of immune escape mutations, limiting the effectiveness of vaccines and antibody therapeutics. To facilitate surveillance, we developed a rapid, high-throughput, multiplex assay able to assess the inhibitory response of antibodies to 24 RBD natural variants simultaneously. We demonstrate how this assay can be implemented as a rapid surrogate assay for functional cell-based serological methods to measure the SARS-CoV-2 neutralizing capacity of antibodies at the angiotensin-converting enzyme 2-RBD (ACE2-RBD) interface. We describe the e... More
The SARS-CoV-2 receptor binding domain (RBD) is both the principal target of neutralizing antibodies and one of the most rapidly evolving domains, which can result in the emergence of immune escape mutations, limiting the effectiveness of vaccines and antibody therapeutics. To facilitate surveillance, we developed a rapid, high-throughput, multiplex assay able to assess the inhibitory response of antibodies to 24 RBD natural variants simultaneously. We demonstrate how this assay can be implemented as a rapid surrogate assay for functional cell-based serological methods to measure the SARS-CoV-2 neutralizing capacity of antibodies at the angiotensin-converting enzyme 2-RBD (ACE2-RBD) interface. We describe the enhanced affinity of RBD variants N439K, S477N, Q493L, S494P, and N501Y to the ACE2 receptor and demonstrate the ability of this assay to bridge a major gap for SARS-CoV-2 research, informing selection of complementary monoclonal antibody candidates and the rapid identification of immune escape to emerging RBD variants following vaccination or natural infection.