Methods to monitor the functional subproteomes of SERPIN protease inhibitors

Abstract

Conformational variants of the unique family of protease inhibitors annotated as SERPINs are most often underrepresented in proteomic analyses. This limits understanding the complex regulation that this family of proteins presents to the networks within the protease web of interactions. Using bead-based separation provided by a family of proteomic enrichment products—notably AlbuVoid™ and AlbuSorb™, we demonstrate their utility to satisfy investigations of serum SERPINs. We also suggest their use to develop functional profiles of the SERPIN proteoforms, and how those can establish relationships to disease phenotypes, gene mutations, and dysregulated mechanisms.