High purity protein is a common requirement for biochemical and structural studies. A common approach is to recombinantly express an affinity-tagged version of the protein of interest. This is, however, not always a viable option. Some proteins are unstable or inactive once tagged or require posttranslational modifications that do not permit recombinant expression. In these cases, researchers often settle for lower purity protein rather than exhaustively explore purification options, since the purification optimization process can be time and labor intensive when no particular column resins or buffer conditions are dictated by an affinity tag.
Bio-Rad Laboratories has recently released a study demonstrating how to purify untagged protein to high homogeneity without undergoing laborious manual troubleshooting steps. Bio-Rad’s ChromLab software can be programmed to execute several runs sequentially thereby automating and accelerating this tedious process.
To learn how to purify untagged protein with ease read Protein Purification Workflow Development Using Bio-Rad’s NGC™ Chromatography System.
