LAUSR

Escherichia coli is the most widely used heterologous protein expression system. However, this system remains a challenge due to the low solubility of proteins, insufficient yield, and inclusion body formation. Numerous approaches have sought to address these issues. The use of a fusion tag is one of the most powerful strategies for obtaining large amounts of heterologous protein in E. coli expression system . Here, recent advances in fusion tags that increase the expression of proteins are reviewed. In addition, proposed concepts for designing peptide tags to increase protein expression are discussed.