This case study demonstrates an efficient purification workflow for a low-expressing recombinant protein. Multiple chromatography resins were screened for the capture step of this recombinant protein, with goals to minimize fermentation dilution and increase purity and recovery to >75%. Optimal wash and elution conditions were determined using a design of experiments (DOE) approach. An elution buffer containing NaCl and MgCl2 was found to purify the target molecule with high recovery and purity.


  • Importance of screening multiple resins
  • DOE for optimizing purification and elution conditions
  • Evaluation of modifiers for enhancing purity and recovery
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Bioprocessing Recombinant Proteins