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Tools for improving yields and purity from recombinant bacterial proteins



Various methods for the extraction and purification of recombinant proteins from bacteria are in use and have been well described. Common methods for cell lysis involve mechanical disaggregation of cells, such as sonication, but this can be time-consuming when working with multiple samples and more importantly can result in localized heating leading to loss of protein activity. In this webinar, we provide data showing that gentle detergent based lysis leads to greater protein activity and higher yields when compared to mechanical methods such as sonication. We also investigate the use of dual purification strategies and explore optimizing conditions to improve the purity of protein purification techniques.


  • Optimal detergent selection to maximize yield of target protein of interest
  • Detergent choice and how it impacts detergent removal for downstream applications
  • Simple protein purification strategies to improve yield & quality
  • Choosing between dialysis and diafiltration for sample clean-up and buffer exchange


Life science researchers who need to extract, isolate and purify recombinantly expressed proteins and preserve proteins while performing buffer exchange


Garry Seward

Garry Seward


Product Manager - Molecular Workflow Tools

Garry K. Seward, Ph.D. is a Product Manager for Molecular Workflow Tools at MilliporeSigma where he is responsible for introducing new protein and nucleic acid sample preparation products to the market. Before transitioning into marketing, Dr. Seward gained experience in biochemistry and cell biology developing biosensors to target integrin receptor biomarkers.

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