In addition, we show that the expressed Sp圜-antigen format is highly compatible with downstream antibody phage display selection and screening procedures, requiring minimal post-expression handling with no sample modifications. We demonstrate that Sp圜 has broad utility as a protein-fusion tag partner in a eukaryotic expression/secretion context, retaining its functionality and permitting the direct, selective capture and immobilization of soluble antigen fusions using solid phase media coated with a synthetic modified SpyT peptide reagent. In this report, we describe a simple, yet powerful strategy that exploits the properties of the Sp圜atcher/SpyTag (Sp圜/SpyT) covalent interaction to improve substantially the speed and efficiency in obtaining functional antibody clones of interest. An early bottleneck in the rapid isolation of new antibody fragment binders using in vitro library approaches is the inertia encountered in acquiring and preparing soluble antigen fragments.
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