HIGHLIGHTS
SUMMARY
Recombinant peptide production can be achieved by construction of a fusion_protein that contains an affinity tag to aid in isolation, as well as a protease cleavage site to allow for separation of the peptide from the fusion_protein during isolation and purification. Common fusion_proteins used in heterologous expression include glutathione S-transferase, small ubiquitinlike modifier (SUMO), intein proteins, thioredoxin, and maltose binding protein. Possible proteases and associated recognition sequences that can be used in fusion_proteins include tobacco etch virus protease, factor Xa protease, enterokinase, and thrombin. Use of a C-terminal intein fusion_protein will also . . .
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