Hydrophobic Interaction Chromatography
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Hydrophobic Interaction Chromatography

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Pr-181P PreDictor RoboColumn Capto Butyl Inquiry
Pr-182P PreDictor RoboColumn Capto Phenyl (high sub) Inquiry
Pr-428C Process Characterization Kit Inquiry
Re-186P ReadyToProcess Capto Butyl Inquiry
Re-187P ReadyToProcess Capto Octyl columns Inquiry
Re-188P ReadyToProcess Capto Phenyl (high sub) Inquiry
Re-429C ReadyToProcess Capto Butyl ImpRes columns Inquiry
SDB10001 SDB1-HIC Resin 1ml Inquiry
5ml Inquiry
25ml Inquiry
50ml Inquiry
250ml Inquiry
1L Inquiry
SDBH0001 SDB-HIC Resin 5ml Inquiry
10ml Inquiry
25ml Inquiry
50ml Inquiry
250ml Inquiry
1L Inquiry
SDEH0001 SDE-HIC Resin 25ml Inquiry
50ml Inquiry
250ml Inquiry

Introduction of Hydrophobic Interaction Chromatography

The separation and purification of proteins is the premise of biological research, and hydrophobic interaction chromatography (HIC) can effectively complete this procedure. HIC uses the difference in the hydrophobic force between the sample molecule and the stationary phase. When eluted with the mobile phase, the migration speed of each component is different to achieve the purpose of separation.

Schematic diagram showing hydrophobic interaction between proteins in an aqueous solution (A) and between proteins and a hydrophobic ligand on an HIC adsorbent (B).Figure. 1 Schematic diagram showing hydrophobic interaction between proteins in an aqueous solution (A) and between proteins and a hydrophobic ligand on an HIC adsorbent (B). (Mccue J T, 2009)

Principle of HIC

In biological macromolecules like proteins and polypeptides, hydrophobic groups often appear on their surfaces, and hydrophobic interactions can combine the hydrophobic groups with hydrophobic chromatographic media. Hydrophobic forces between molecules and hydrophobic chromatographic mediums vary due to their hydrophobicity. Biomolecules such as proteins or polypeptides can interact more effectively with hydrophobic chromatographic media when the solution has high ionic strength. By linearly or stepwise decreasing the ionic strength of the chromatographic medium, the sample to be separated can be selectively desorbed from a hydrophobic chromatographic medium. Hydrophobic substances elute at higher ionic strengths, while hydrophobic substances elute at lower ionic strengths.

Outstanding Advantages of Our HIC Products

  • Mild conditions for interaction with protein
  • Strong selectivity
  • Excellent physical and chemical stability
  • No environmental pollution
  • Easy to combine with other chromatography techniques
  • High protein recovery rate, less possibility of denaturation, and no inactivation

Compared with other technologies, Our HIC is not easy to cause structural changes and loss of activity of proteins, so it is widely used in various fields such as food science, pharmaceutical science, analytical chemistry, biotechnology, etc., and can be used to separate multiple proteins in a substance. It can also be used for the separation of multiple substances.

Applications of Our HIC Products

  • In the field of biotechnology, our products can be used for the separation of one or more substances, such as the separation of cells, proteins, cytokines and DNA.
  • In biomedical research, isolation and detection of viruses and living cells.

Creative BioMart provides a series of fast, simple, and high-quality HIC products to meet your scientific research needs. You can quickly find the reagents you need by searching keywords such as CAT number or product name. Please tell us your product needs, we will provide you with a comprehensive consultation. If you have any questions, please feel free to contact us.

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Reference:

  1. Mccue J T. (2009) Theory and use of hydrophobic interaction chromatography in protein purification applications[J]. Elsevier Science & Technology. 463: 405-414.
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