Our website does not fully support your browser.

We've detected that you are using an older version of Internet Explorer. Your commerce experience may be limited. Please update your browser to Internet Explorer 11 or above.

We believe this site might serve you best:

United States

United States

Language: English

Promega's Cookie Policy

Our website uses functional cookies that do not collect any personal information or track your browsing activity. When you select your country, you agree that we can place these functional cookies on your device.

A Recombinant Asp-Specific Protease for Bottom-up Mass Spectrometry Workflows

Part # PS303


Chris Hosfield1, Jim Hartnett1, Alba Katiria González Rivera1,2, Ethan Strauss1, Sergei Saveliev1, Michael Rosenblatt1and Marjeta Urh1
1Promega Corporation, 2800 Woods Hollow Rd, Madison, WI 53711; 2University of Wisconsin-Madison, Madison, WI.

Bottom-up mass spectrometry workflows typically utilize 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. LysC, another commonly used protease, is also robust and specific, but has specificity similar to trypsin. Site-specific proteases with orthogonal specificity such as GluC and AspN are useful but can suffer from relatively poor digestion performance. Here we report the expression, purification and characterization of a protease which displays both high cleavage efficiency and a strong preference for cleavage N-terminal to aspartic acid. This new recombinant protease should have broad utility for bottom-up LC-MS/MS workflows.

Printed in USA.