Chitin-Binding Domain With Self-Splicing Inteins Tag Protein Purification by Affinity Chromatography (CAT#: STEM-MB-1283-LGZ)

Introduction

Typically, a combination of chromatographic techniques are used during protein purification. In many cases, the first step will be an affinity chromatography step, depending on the affinity tag you choose during structure design. If a protease cleavage site is included between the affinity tag and the protein of interest, this specific protease can be used to remove the affinity tag immediately after the affinity chromatography step or later in the purification process. To increase the purity, a second chromatographic step, such as ion exchange chromatography or hydrophobic interaction chromatography, can be used. As a final polishing step, size exclusion chromatography is usually performed, as this also immediately serves as a quality control step to assess the oligomeric state of the protein of interest.