Hydrophobic Interaction Chromatography (HIC) is a powerful method for separating proteins and biomolecules based on their surface hydrophobicity. It is performed under native conditions and is ideally suited for analyzing protein variants and aggregates without compromising biological activity. 

How HIC Works 

• Biomolecules bind to hydrophobic ligands on the stationary phase in the presence of high salt concentrations.

• Elution occurs by gradually reducing the salt concentration. 

• Compatible with HPLC and UHPLC systems for analytical applications. 

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What HIC is used for? 

• Drug-Antibody-Ratio (DAR) analysis of Antibody-Drug-Conjugates (ADCs) 

• Protein modifications analysis in proteins (Deamidations, Oxidations, Reductions, Sialylation…) 

• Protein Aggregate determination 

• Hydrophobicity screening in protein drug candidates 

• All biomolecule separations by hydrophobicity at native conditions 

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What Tosoh offers 

• Wide range of ligand chemistries for different selectivities 

• Columns optimized for HPLC and UHPLC performance

• Proven quality for demanding biopharmaceutical analyses

• Technical support and application expertise