The recombinant SARS COV2 S Trimer is an active engineered protein designed to mimick the native coronavirus S protein trimer conformation which consists of three S proteins . The furin cleavage site has been mutated at position 683 and 685 so that the protein is not cleaved into the S1 and S2 primary domains by cellular proteases. S protein trimerization is achieved utilizing a T4 Folsom trimerzation domain that is inserted into the sequence to be expressed by the cell line. Post expression, the S monomers spontaneously form the Trimer conformation. The Trimerization conformation has been by verified both by HPLC chromatography and by SEC-MALS.
Fig.1:a) ELISA Binding of S trimer (cat#RKNCOVST) product to the human ACE (cat#RKQ9BYF1F)