Hydrophobicity Chromatography-based Lectin Purification Service

Hydrophobicity Chromatography-based Lectin Purification Service

Hydrophobicity Chromatography-based Lectin Purification Service at CD BioGlyco

CD BioGlyco now provides hydrophobicity chromatography-based Lectin Purification Service with the most advanced hydrophobicity chromatography (HIC) technique and years of experience in the field of purification.

  • How does HIC work?

HIC acts as a separator based on the surface hydrophobicity of the molecule. HIC is an effective separation technique that maintains the biological activity of proteins after purification due to matrices and the use of conditions that operate under less denaturing conditions. Hydrophobic ligands on the HIC resin bind to proteins in binding buffers with high salt concentrations. When the ionic strength of the buffer is reduced, the interaction of the protein with the hydrophobic ligand is reversed. As a result, the least hydrophobic proteins are eluted first. The most hydrophobic protein requires a more drastic reduction in salt concentration to reverse the interaction, so it is the last to elute.

Fig.1 Schematic illustration of HIC. (Chen, et al., 2015)Fig.1 Schematic illustration of HIC. (Chen, et al., 2015)

  • Suitable for Purification of a Large Range of Molecules
    • Recombinant proteins and peptides
    • mRNA
    • Plasmids
  • Suitable Protocol to Meet Different Experimental Requirements
    • HIC is used as a complementary technology in combination with other technologies to improve separation efficiency.
  • Suitable for Purification of Other Steps
    • HIC is used after purification of the sample by ammonium sulfate precipitation.
    • HIC is used as an intermediate step after ion exchange separation.
  • Other Purification Methods

Fig.2 Flow chart of our purification. (CD BioGlyco)Fig.2 Flow chart of our purification. (CD BioGlyco)


  • Multifunctional Technology
    • HIC is used for polishing steps, capture, or intermediate purification.
  • Biochemistry
    • HIC is used to isolate polar peptides after the digestion of proteins to determine protein function and stability.
  • Pharmacology
    • HIC is applied to analyze polar drugs and metabolites, including peptides, proteins, and antibodies.
  • Agricultural
    • HIC is applied to analyze plant extract polar components, such as those in peptides, carbohydrates, phenolic acids, and flavonoids.
  • Food Industry
    • HIC is applied to detect marine biotoxins, small polar compounds, food contaminants, and biogenic amines (produced by organisms).


  • HICs are used when there is a need to isolate polymerized proteins from more desirable monomeric forms.
  • HIC is more selective and effective in removing polymer species than other chromatographic methods such as affinity and ion exchange.
  • HIC removes undesired variant forms or misfolds from proteins.

CD BioGlyco supports our clients' purification of lectin with our purification technologies, which we have accumulated over many years. We depend on the objective and required purity to optimize methods. Please feel free to contact us if hydrophobic chromatographic purification is required in the production of lectins.


  1. Chen, T.; et al. Hydrophobic interaction chromatography for antibody drug conjugate drug distribution analysis. Am. Pharm. Rev. 2015, 18: 16-20.
This service is for Research Use Only, not intended for any clinical use.

About Us

CD BioGlyco is a world-class biotechnology company with offices in many countries. Our products and services provide a viable option to what is otherwise available.

Contact Us

Copyright © CD BioGlyco. All rights reserved.