Affinity purification of protein is a common technique in most protein labs which is often the bottle neck in achieving faster experimental results. The technique usually involves the use of HIS or GST tags which need to be enzymatically cleaved from of the recombinant protein in a laborious and time-consuming process so as not to interfere with the protein’s functional activity or crystallization process. Furthermore, many functional assays and crystallography experiments require large amounts of protein which can be frustrated by the drawn-out purification/tag cleavage process.
In this technical note, Justin L. Burns et. al. from the Georga Insitute of Technology report how the combination of the Profinity eXact fusion-tag and Profinia automated purification system allowed them to recover milligram quantities of protein from a gram-negative bacteria in under 2 hours.