diPhenyl Magnetic Beads

Hydrophobic interaction chromatography  (HIC) is a technique for separating macromolecules from one another based on a reversible interaction between the external hydrophobic region of a biological macromolecule and the hydrophobic ligand (such as phenyl, octyl, or butyl) of a HIC medium. The interaction is enhanced by a buffer with a high salt concentration and reduced with a low salt concentration. Therefore, based on salt concentration in a buffer, the protein with less hydrophobicity is eluted first, whereas the protein with more hydrophobicity elutes last. Compared with other chromatography methods, HIC is a more popular method for separating and purifying protein and peptides in analytical and preparatory scale applications since it employs a less denaturing environment.