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prepcission protease

Prescission protease, also known as PreScission protease, is a recombinant enzyme widely used in molecular biology and protein research for cleaving fusion proteins from their affinity tags or purification tags. This protease is derived from a gene fusion of the N-terminal region of the Escherichia coli SUMO (Small Ubiquitin-like Modifier) protein and the C-terminal region of a viral protease called NS3 from a strain of Hepatitis C virus.

The primary function of prescission protease is to selectively cleave peptide bonds between itself and a specific recognition sequence (usually a short peptide) in the fusion protein. This recognition sequence is typically introduced during the genetic engineering of a fusion protein construct.

Here's how prescission protease works:

  1. Fusion Protein: A fusion protein is created by combining a protein of interest with an affinity tag or purification tag for easier detection or purification.

  2. Recognition Sequence: A specific recognition sequence recognized by prescission protease is engineered between the protein of interest and the tag.

  3. Cleavage: When prescission protease is added to the fusion protein, it specifically recognizes and cleaves the peptide bond at the recognition sequence, separating the protein of interest from the tag.

  4. Tag Removal: After cleavage, the tag can be separated from the protein of interest, leaving the pure protein ready for downstream applications or analysis.

Prescission protease is particularly valuable in the field of recombinant protein expression and purification, as it allows for the removal of purification tags without leaving extra residues or artifacts on the target protein. This protease is often used in affinity chromatography and other protein purification techniques, enabling the isolation of highly pure and biologically active proteins for various research and biotechnological applications.

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