TEV Protease Cleavage of MBP and His Affinity Tags in de novo Fusion Proteins
Loading...
View/Download File
Persistent link to this item
Statistics
View StatisticsJournal Title
Journal ISSN
Volume Title
Title
TEV Protease Cleavage of MBP and His Affinity Tags in de novo Fusion Proteins
Published Date
2023-07
Publisher
Type
Presentation
Abstract
Polyhistidine (His) and Maltose Binding Protein (MBP) tagged proteins were successfully expressed in Escherichia coli. TEV protease cleavage and MBP-free cloning were pursued as strategies for obtaining pure, MBP-free protein variants for further research. A protocol for TEV cleavage was developed, and methods of subsequent purification or alternative cloning were explored.
Description
UROP Project conducted in the Seelig Lab under the direction of Burckhard Seelig.
Polyhistidine (His) and Maltose Binding Protein (MBP) tagged proteins were successfully expressed in Escherichia coli. TEV protease cleavage and MBP-free cloning were pursued as strategies for obtaining pure, MBP-free protein variants for further research. A protocol for TEV cleavage was developed, and methods of subsequent purification or alternative cloning were explored.
Related to
Replaces
License
Series/Report Number
Funding information
This research was supported by the Undergraduate Research Opportunities Program (UROP) and by NASA under award 80NSSC21K0595.
Isbn identifier
Doi identifier
Previously Published Citation
Other identifiers
Suggested citation
Soltau, Alexander D.; Malisetti, Nithya; Winslow, Peter J; Seelig, Burckhard. (2023). TEV Protease Cleavage of MBP and His Affinity Tags in de novo Fusion Proteins. Retrieved from the University Digital Conservancy, https://hdl.handle.net/11299/256042.
Content distributed via the University Digital Conservancy may be subject to additional license and use restrictions applied by the depositor. By using these files, users agree to the Terms of Use. Materials in the UDC may contain content that is disturbing and/or harmful. For more information, please see our statement on harmful content in digital repositories.