Cayman SARS-CoV/SARS-CoV-2 Spike Glycoprotein RBD Chimeric Monoclonal Antibody (Clone D001)

Severe acute respiratory syndrome coronavirus (SARS-CoV) spike glycoprotein, also known as the surface glycoprotein, is a viral structural protein encoded by the S gene in SARS-CoV RNA that contains the receptor binding domain (RBD).¹ SARS-CoV is a member of the Betacoronavirus genus of viruses and has an approximately 79% sequence identity with SARS-CoV-2, the causative agent of COVID-19.^2,3 SARS-CoV spike glycoprotein is a transmembrane glycoprotein that assembles into homotrimers on the virus surface and is composed of an N-terminal S1 subunit, which contains the receptor binding domain (RBD), and a C-terminal S2 subunit, which facilitates fusion between viral and host cell membranes.^4,5,6 The 193-amino acid RBD of the SARS-CoV spike protein is a target for neutralizing antibodies.^5,7 The SARS-CoV RBD, which spans amino acid residues 318 to 510, is 73% identical to that of SARS-CoV-2 and can bind to human angiotensin-converting enzyme 2 (ACE2), which is the host cell surface receptor for both SARS-CoV and SARS-CoV-2.^5,4,7,6 SARS-CoV is the causative agent of SARS, a primarily respiratory illness characterized by fever, cough, shortness of breath, and an approximately 10% fatality rate.³ Caymans SARS-CoV/SARS-CoV-2 Spike Glycoprotein RBD Chimeric Monoclonal Antibody (Clone D001) is composed of human IgG1κ constant domains and variable regions from a mouse immunized with purified recombinant SARS-CoV spike glycoprotein RBD. It can be used for ELISA, flow cytometry (FC), immunocytochemistry (ICC), and immunofluorescence (IF) applications, as well as microneutralization assays.

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