Scouting and Preparative Purification of His-Tagged Proteins Application Note
Authors: Dr. Mark McAlister, John Phelan and Dr. Roberto Sarra | Last updated: June 2021
Overview
The structure of a protein influences its function and how it interacts with other molecules. Therefore, structural biology plays a crucial role in the design of novel drugs.
Common structure determination methods, such as x-ray crystallography, require the preparation of proteins to high purity and at relatively large quantities. Ion exchange chromatography is a ubiquitous, cost-effective, and easy method for protein purification.
In this application note, we introduce Vivapure® and Sartobind® solutions to demonstrate the simplicity, efficiency and relevance of Sartobind® membrane adsorbers from scouting to preparative purification.
- Document type: Application Note
- Page count: 6
- Read time: 8 minutes
Key Takeaways
- The significance of protein purification in structural biology laboratories
- Ion exchange chromatography as an alternative to metal affinity purification
- Methods and buffers used for a scouting purification process with Vivapure® IEX
- Scale up to preparative purification using the same Sartobind membrane adsorber technology
This Resource is Designed for:
- Researchers in laboratories using protein expression and purification for structural and functional analyses
Applications Supported:
- Scouting purification
- Preparative purification
- His-tagged protein purification
- Ion exchange chromatography
