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Hydrophobic Interaction
Hydrophobic interaction chromatography (HIC) is a powerful tool for the purification of biomolecules. The technique USES the interaction between the hydrophobic region on the protein surface and the weakly hydrophobic groups in the stationary phase for chromatography separation. HIC is a good complement to ion exchange and dimensional exclusion chromatography, especially when protein isomers are present in the sample, or when the target sample is similar to the isoelectric point or molecular weight of the impurity and is difficult to separate. HIC can be used after affinity chromatography by selectivity difference when affinity filler is difficult to distinguish proteins with similar recognition sites.
Hydrophobic Interaction
QuikSep Glycosyl Hydrophobic Chromatography Resins
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QuikSep Hydrophobic Interaction Resin
Hydrophobic chromatography separates proteins based on their differences in hydrophobicity, namely, through the reversible interaction between the hydrophobic groups on the surfaces of proteins and hydrophobic media.
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