Bottom-up mass spectrometry workflows typically use trypsin to digest proteins into peptides suitable for LC-MS/MS analysis. While trypsin is an excellent protease, alternative proteases are useful for numerous applications including increasing protein sequence coverage and identifying post-translational modifications.
In this webinar Dr. Hosfield describes the features of a new recombinant Asp-N protease (rAsp-N). rAsp-N displays both high cleavage efficiency and a strong preference for cleavage N-terminal to aspartic acid. He will explain how this enzyme can be effectively used to digest a variety of sample types, including complex protein mixtures and therapeutic molecules such as monoclonal antibodies.
In addition, he describes how a multi-enzyme approach can be successfully employed to achieve 100% sequence coverage of an IgG from a single injection. Combining peptides derived from digestion with orthogonal proteases prior to LC-MS/MS analysis could be a general strategy to ensure high sequence coverage while simultaneously reducing demand on instrument time.
Chris Hosfield, PhD
Senior Research Scientist
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