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.{53462,53459,53461,55257,55258} The SARS-CoV-2 spike glycoprotein, also known as the surface glycoprotein, is located on the outer envelope of the virion.{53462} It is composed of an S1 and S2 subunit divided by a furin S-cleavage site not found in other SARS-CoVs.{46767,49561} The S1 subunit contains the receptor-binding domain (RBD), which binds to the carboxypeptidase angiotensin-converting enzyme 2 (ACE2), and the S1 and S2 subunits are cleaved by the protease TMPRSS2 to facilitate viral fusion with the host cell membrane.{49542,49536,49558} In this way, ACE2 acts as the functional receptor for SARS-CoV-2. SARS-CoV-2 infection can result in the production of neutralizing antibodies, which bind to the SARS-CoV-2 spike RBD preventing further viral entry and infection, starting approximately 4-10 days after symptom onset.{55337,55338} Cayman’s SARS-CoV-2 Spike Glycoprotein Neutralizing Monoclonal Antibody (Clone 57) disrupts the spike glycoprotein RBD-ACE2 interaction and can be used for ELISA, flow cytometry (FC), immunocytochemistry (ICC), and immunofluorescence (IF) applications.