Self-removing tags can be used for simple and effective purification of recombinant proteins and peptides. The key component of these tags is an intein, which is a protein element with the ability to excise itself out of a host protein. Engineered inteins have many applications, including the ability to detach themselves (self-cleave) from a fused target proteins in response to a small buffer pH change. This capability has significant applications in the field of protein purification, where one segment of a split intein can serve as a self-removing affinity tag. In this presentation, a novel self-removing tag will be discussed and compared to alternate methods. Case studies will also be presented, along with a deep dive into optimizing this type of protein purification process.

Learning Objectives:

1. Define what how self-removing tags are used during protein purification processes.

2. Describe protein purification steps.

3. Outline examples of proteins which were studied and their expression hosts.