High-efficiency Columns for the Separation of Large Biomolecules
- High protein loading capacity for protein purification applications
- Wide range of analytical and preparative applications, including the separation of bovine serum proteins, snake venom proteins, and monoclonal antibodies (Mabs)
- Based on 5μm ultra-high purity spherical silica gel particles with 300Å pores
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.
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