E. coli is the most widely used recombinant expression system to overexpress protein given that it is inexpensive, easy to scale up, and relatively fast. Due to its wide-spread use, there are numerous molecular tools, products, and expression/purification protocols available. Determining which tools and products to use, such as plasmid, strain-type, affinity tag and resin system, or buffer exchange device can be daunting. Here, we present a workflow overview of the recombinant protein expression from E. coli and provide insight and various tips and tricks about how to optimize and improve protein yield and purity enabling you to make the best decisions for your protein of interest.
What Will You Learn?
Determining best conditions for:
- Protein overexpression in E. coli
- Affinity protein purification
- Protein concentration and buffer exchange
- Additional tips about membrane ultrafiltration fractionation, and detergent removal
Who Should Watch?
Scientists, lab technicians, researchers who work with protein
Speakers
Natasha L. Pirman, Ph.D
Molecular Workflow Tools
Lead Application Scientist
Dr. Natasha L. Pirman is an Application Scientist for Molecular Workflow Tools where she is involved in developing new sample preparation products and applications for both protein and nucleic acid applications. Prior to joining us, Dr. Pirman utilized her expertise in protein biochemistry to explore structural protein changes to Intrinsically Disordered Proteins and human kinase disease models for drug target investigations.
Protein biology
- Protein expression
Duration:35min
Language:English
Session 1:presented May 31, 2021
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