Hydrophobic Interaction Chromatography Columns for the Separation of Large Biomolecules

Hydrophobic Interaction Chromatography separates biomolecules in a decreasing salt gradient, based on differences in surface hydrophobicity. This method preserves the biological activity of proteins. The HIC separation mechanism is complementary to those of ion-exchange and gel filtration chromatography.

• Based on 5 µm ultrahigh purity spherical silica gel particles, with 300 Å pores

• Proteins separated under non-denaturing conditions

• High protein loading capacity for protein purification applications

• Proprietary multidentate silica bonding for enhanced hydrolytic stability

• High-resolution HPLC separation of proteins and peptides

• Wide range of applications

The ProPac^®HIC-10 column is a high-resolution, high-capacity, silica-based HIC column that provides greater hydrolytic stability under the highly aqueous conditions used in HIC. Examples include the separation of bovine serum proteins, snake venom proteins, enzymes, human skeletal muscle protein (HSMP), monoclonal antibodies, pancreatin, and thrombin and peptide applications including tryptic digests of proteins.

Separation of a mixture of proteins using the ProPac HIC-10, compared to the same separation on two competitors’ columns.

Comparison of the separation of snake venom proteins/peptides using the ProPac HIC-10 and two competitors’ columns.

Gradient separation of a monoclonal antibody using the ProPac HIC-10.