Abstract

Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis can be employed to efficiently separate multiple antigenic peptides (MAPs). Moreover, the electrophoresed MAPs are amenable for transfer to nitrocellulose membrane for immunoblotting. MAPs involve a hepta lysine core with end groups for anchoring multiple copies of the same synthetic peptide. MAPs are amenable to staining with Coomassie and silver on SDS polyacrylamide gels as well as by Fast Green on a blotted nitrocellulose membrane. They lend themselves to analysis on an immunoblot as they behave like low molecular weight proteins. Affinity immunoblotting for analysis of antibody clonotype distribution has also been carried out using these peptides.

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