Hydrophobic Interaction Chromatography
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Hydrophobic Interaction Chromatography

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Cat# Product Name Size Price Qty Inquiry
ISO-183P RESOURCE ISO Inquiry
MAB10001 MAB1-HIC Resin 100ml Inquiry
1L Inquiry
5L Inquiry
20L Inquiry
MABH0001 MAB-HIC Resin 100ml Inquiry
1L Inquiry
5L Inquiry
20L Inquiry
MAEH0001 MAE-HIC Resin 100ml Inquiry
1L Inquiry
5L Inquiry
20L Inquiry
Oc-421C Octyl Sepharose 4 Fast Flow Inquiry
Oc-422C Octyl Sepharose CL-4B Inquiry
Ph-161P Phenyl Sepharose 6 Fast Flow (high sub) in ReadyToProcess Inquiry
Ph-162P Phenyl Sepharose 6 Fast Flow (low sub) in ReadyToProcess Inquiry
Ph-423C Phenyl Sepharose 6 Fast Flow (High Sub) Inquiry
Ph-424C Phenyl Sepharose 6 Fast Flow (Low Sub) 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.

*If your organization requires the signing of a confidentiality agreement, please contact us by email.

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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