Hydrophobic Interaction Chromatography (HIC)
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Hydrophobic Interaction Chromatography (HIC)
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Separation using HIC is based on the reversible interaction between a protein and the hydrophobic ligand bound to the chromatography matrix.
The interaction is enhanced by buffers with high ionic strength, which makes HIC an excellent purification step after ammonium sulfate precipitation or after elution in high salt during ion exchange chromatography (IEX). HIC is well-suited for the capture or intermediate steps in a purification scheme.
During HIC, sample components bind to the column in high ionic strength buffer, typically 1 to 2 M ammonium sulfate or 3 M NaCl. High concentrations of salt, especially ammonium sulfate, may precipitate proteins. Therefore, check the solubility of the target protein under the binding conditions to be used. Elution is usually performed by decreasing the salt concentration, stepwise or using a gradient.
We offer a wide range of HIC Media in lab packs and prepacked column formats.
