Recombinant protein expression in E. coli often results in the formation of insoluble aggregates called inclusion bodies. In vitro refolding techniques can be adopted to recover recombinant protein but the biological activity of the target is often lost during this process. While there are several approaches to bypass inclusion body formation, chaperone co-expression can be a good option. Chaperones assist newly synthesized proteins fold into their native states while shielding exposed hydrophobic patches of non-native proteins to prevent their aggregation. In this webinar we will present some popular chaperone co-expression strategies that could help you achieve higher yields of recombinant soluble protein.
| Chaperone co expression strategies for recombinant soluble protein production in E. Coli | ||
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| BacPower™ Bacterial Expression System | ||
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