HIC Chromatography Media Nano Butyl-15L

   HIC is used to separate proteins on the basis of relative hydrophobicity. The unique feature of HIC is that proteins bind at high salt concentration and elute at low salt concentration.By combining HIC with ion exchange or affinity chromatography, the purification of biomolecules can be completed efficiently. While in reversed phase column chromatography (RPC), desorption is often promoted by the addition of an increasing amount of organic solvent. Therefore gentle binding and elution condition of HIC allows a better retaining of the biologic activity of the target protein than RPC in which organic solvents are applied.  The strength of the hydrophobic interaction is influenced strongly by the nature of the salt components in the mobile phase. The salt concentration needed depends on the protein hydrophobicity and solubility. HIC is particularly attractive for protein purification after ion exchange and affinity chromatography, where the sample with high…

Boronic Acid Affinity Chromatography Resin Immobilized Metal Ion Affinity Chromatography Resins Protein A Affinity Resin Hydrophobic Interaction Chromatography Resins Ion Exchange Chromatography Resins