We utilize protein splicing in protein engineering purposes, but also study the purpose and origin of inteins. 

Our research topics include cis-splicing, trans-splicing and creating natural-like split inteins from cis-splicing inteins. 

Trans-splicing is a powerful tool in ligation and protein engineering, and we use natural split Inteins from organisms such as Nostoc Punctiforme and its DnaE intein, and extermophile Halorhabdus utahensis and its salt inducible split inteins. In addition, we also research new organisms and their inteins to be possibly applied in protein engineering. 

In addition to cis- and trans-splicing, a bimolecular splicing reaction can also take place between two precursor proteins, completely without any split intein fragments. The phenomenon is termed iPAS, or intein-mediated Protein Alternative Splicing. Alternative splicing supports the theory that the original purpose of inteins is to create posttranslational variability in protein, with no genetic modifications required. Since iPAS sensitive to the precursor expression order, it could have biotehcnological applications regarding sequence studying of events in living cells. However, this process also presents challenges when studying the original genes and functions of proteins, as the origin becomes harder to trace due to iPAS.