TEV Protease Cleavage of MBP and His Affinity Tags in de novo Fusion Proteins

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TEV Protease Cleavage of MBP and His Affinity Tags in de novo Fusion Proteins

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2023-07

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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.

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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.

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This research was supported by the Undergraduate Research Opportunities Program (UROP) and by NASA under award 80NSSC21K0595.

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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.

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