Cayman SARS-CoV-2 Spike Glycoprotein S2 Subunit Extracellular Domain Chimeric Monoclonal Antibody (Clone D001)

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped positive-stranded RNA virus, a member of the Betacoronavirus genus, and the causative agent of COVID-19.^1,2,3,4,5 The SARS-CoV-2 spike glycoprotein, also known as the surface glycoprotein, is a viral structural protein encoded by the S gene in SARS-CoV-2 RNA.¹ It is composed of an S1 and S2 subunit divided by a furin S-cleavage site not found in other SARS-CoVs.^6,7 The C-terminal S2 subunit, which facilitates fusion between viral and host cell membranes, contains a fusion peptide (FP) and two heptad repeats (HRs), as well as transmembrane and cytoplasmic domains.^7,8 Upon insertion of the FP in the target cell membrane, the HRs form a six-helical bundle (6-HB) that enables SARS-CoV-2 to fuse with the target cell. The SARS-CoV-2 spike glycoprotein S2 subunit increases amyloid-β (1-40) (Aβ40) and Aβ42 levels in primary mouse neuron culture supernatants and the number of hippocampal and cortical Aβ plaques in APPswe/PSEN1dE9 transgenic mice.⁹ Caymans SARS-CoV-2 Spike Glycoprotein S2 Subunit Extracellular Domain Chimeric Monoclonal Antibody (Clone D001) is composed of human IgG1κ constant domains and variable regions from a mouse immunized with purified recombinant SARS-CoV-2 spike glycoprotein S2 subunit extracellular domain (ECD). It can be used for ELISA, flow cytometry (FC), immunocytochemistry (ICC), and immunofluorescence (IF) applications.

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