Hydrophobic interaction chromatography (HIC) is a powerful tool for the process purification of biomolecules. Five HIC ligands featuring different degrees of hydrophobicity and selectivity. The hydrophobicity of HIC resins increases through the ligand series.

• Typically used in intermediate purification and polishing steps

Ether HIC resins: Ether hydrophobic interaction chromatography (HIC) resins have the highest hydrophilicity (lowest hydrophobicity) of the HIC ligands. The ether ligand is useful for very hydrophobic molecules such as membrane proteins. It is typically used in intermediate purification and polishing steps.

Phenyl HIC resins: Phenyl hydrophobic interaction chromatography resins are in the middle of the hydrophobicity range. Primary applications are for the separation of proteins, their isoforms, and aggregate removal.

Butyl HIC resins: Butyl hydrophobic interaction chromatography (HIC) resins have the second highest hydrophobicity of the HIC ligands. There are three pore sizes available for this ligand and each has been optimised for a specific molecular size profile. The primary applications are the separation of proteins, their isoforms, and aggregate removal.

Hexyl HIC resins: Hexyl hydrophobic interaction chromatography (HIC) resin has the highest hydrophobicity of the HIC ligands. It is used for very hydrophilic proteins or where a low salt elution environment is required.