Cleavage sites are used to remove tags from recombinant proteins after purification to obtain the native protein. Here are some commonly used cleavage sites: 

1.   TEV Protease (Tobacco Etch Virus Protease) Site: 

     ●      Sequence: ENLYFQ↓G 

     ●      Description: TEV protease specifically recognizes and cleaves this sequence, enabling precise removal of tags. 

2.   Thrombin Cleavage Site: 

     ●      Sequence: LVPR↓GS 

     ●      Description: Thrombin cleaves between arginine and glycine residues, leaving a minimal scar on the protein. 

3.   Factor Xa Cleavage Site: 

     ●      Sequence: IEGR↓ 

     ●      Description: Factor Xa cleaves after the arginine residue, providing an alternative to thrombin or TEV protease. 

4.   Enterokinase Cleavage Site: 

     ●      Sequence: DDDDK↓ 

     ●      Description: Enterokinase cleaves this sequence, offering a precise method for tag removal while leaving the target protein intact. 

Cleavage sites like TEV, thrombin, Factor Xa, and enterokinase are used to remove tags post-purification, ensuring that the native form of the protein is maintained. 

GenCefe provide one-stop solutions from codon optimization, gene synthesis, to protein expression and purification. In addition to four conventional expression systems of bacterial, yeast, insect cell, and mammalian cell, we have also developed a patented cell free expression technology, which is suitable for the production of difficult proteins such as toxic proteins and membrane proteins.