ResourceSeparations

Hydrophobic interaction and reversed phase chromatography

25 Jul 2025

Hydrophobic interaction chromatography (HIC) separates biomolecules in relatively mild conditions according to differences in their hydrophobicity. Many scientists use HIC in protein purification as a complement to other techniques that separate according to charge, size, or biospecific recognition.

Explore both theoretical and practical aspects of the technique, the resins available, and how to select them, together with application examples, and detailed instructions for the most common procedures.

Links

Tags

Protein PurificationProtein purification is a vital step in drug discovery, therapeutics, biotech and life science research. The purification process typically involves subcellular or membrane protein extraction with cell lysis kits, separation of proteins from cell debris by filtration or spin columns, and the isolation of proteins of interest from other proteins and impurities with affinity purification (including fusion protein tags and antibody binding proteins A, G and L), immunoprecipitation or chromatographic methods, such as ion exchange, size exclusion and immobilized metal affinity chromatography. All purification methods come in multiple formats for your laboratory needs, including agarose or magnetic beads, resins, columns and filter plates. Find the best protein purification equipment in our peer-reviewed product directory: compare products, check customer reviews and receive pricing direct from manufacturers.Biomolecules
Hydrophobic interaction and reversed phase chromatography