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Hydrophobic interaction chromatography (HIC) separates biomolecules by the strength of their interaction with hydrophobic ligands attached to an uncharged base matrix.
Proteins and peptides differ from one another in their hydrophobic properties and this difference forms the basis of a hydrophobic interaction chromatography (HIC) separation. Salt solutions are often used to mediate the binding of sample molecules to a hydrophilic matrix substituted with a hydrophobic ligand.
Hydrophobic interaction chromatography has evolved into one of the most powerful methods in preparative biochemistry. Its speed, resolution, and capacity rival ion exchange chromatography; its selectivity is complementary to ion exchange chromatography and size exclusion chromatography; and its ability to clear nucleic acids makes it an indispensable tool for the purification of therapeutic proteins.
GE Healthcare media for hydrophobic interaction chromatography are well established in industry. A wide range of base matrices and ligands has been developed to address the different aspects of downstream purification. These media are designed for robust, high capacity high resolution, hydrophobic interaction chromatography at various stages of process scale purification. Proteins and peptides differ from one another in their hydrophobic properties and this difference forms the basis of a hydrophobic interaction chromatography (HIC) separation. Salt solutions are often used to mediate the binding of sample molecules to a hydrophilic matrix substituted with a hydrophobic ligand.
Read more about the basic principles behind hydrophobic interaction chromatography.
Read about our hydrophobic interaction chromatography products.
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