Lesson Code: BPU-1110 (PREMIUM LESSON) Describes the use of various chromatographic methods in downstream protein purification including size exclusion, ion exchange, hydrophobic interaction and affinity chromatographies. The basics of a chromatography set-up are covered along with critical factors affecting protein separation such as column packing, resolution, column capacity, pressure and the gel matrix.

  • Category: Biopharma Processes and Equipment


After taking this e-Lesson you will be able to:

- Explain the role of different chromatographic methods in protein purification.

- Describe where chromatography fits into downstream processing.

- Construct a general outline of a protein purification process for both intracellular and extracellular proteins.

- Explain what is meant by preparative chromatography.

- Describe the difference between "Size Exclusion", "Ion-Exchange", "Hydrophobic Interaction" and "Affinity" chromatography.

- Explain terms such as solubility, charge, molecular size, adsorption properties and binding specificity.

You can download a PDF product brochure here:


EU_Bioprocessing Product Sheet.pdf


US_Bioprocessing Product Sheet.pdf