Bottoms Up: Improving Proteomic Sample Preparation with Recombinant Asp-N and Multi-Enzyme Workflows
Tryptic digestion often leaves gaps in protein sequences. In this webinar Dr. Hosfield describes the advantages of using a new recombinant Asp-N protease to fill in the gaps.
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
We love to talk science.
Sign up to receive monthly invitations to our webinars.