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Chromatographic Media


Chromatography is a most frequently used laboratory technique for separation and purification of biomolecules mixture. The mixture is dissolved in the mobile phase (a kind of fluid), which carries it through the stationary phase (a structure holding another material). The separation is based on differential partitioning between the mobile and stationary phases.


According to the different separation mechanism and principle, chromatography techniques are classified into different types for separation and purification process of the various target biomolecules. There are 4 types of commonly used chromatography techniques: Affinity chromatography, Ion exchange chromatography (IEC), Gel filtration (also known as Size-exclusion chromatography (SEC) and molecular sieve chromatography), and Hydrophobic interaction chromatography (HIC). 


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Affinity chromatography

Affinity chromatography is a powerful chromatography technique of separating and purifying proteins based on the highly specific interaction between antigen and antibody, enzyme and substrate, or receptor and ligand. Such interactions including hydrogen bonding, ionic interaction, disulfide bridges, hydrophobic interaction, etc. Affinity chromatography are widely recognized for their high selectivity, high resolution and high capacity.


Ion exchange chromatography

Ion exchange chromatography (IEX) is a practical chromatography process that separates ions and polar molecules based on their respective charged groups. It works on almost any kind of charged molecule—including large proteins, small nucleotides, and amino acids.
 


Gel filtration chromatography

Gel filtration chromatography, also known as size exclusion chromatography (SEC), is a chromatographic method that separates molecules by their size or molecular weight. SEC can be used for wide ranges of separation and purification of components with large molecular weight differences and low resolution requirement, such as proteins, polysaccharides and other macromolecules.


Hydrophobic interaction chromatography

HIC is a useful method for purification and separation of biomolecules based on their surface hydrophobicity. HIC can be applied in the separation and purification of hydrophobic proteins such as aromatic and aliphatic compounds. In HIC, the matrix material is lightly substituted with hydrophobic groups, such as methyl, ethyl, propyl, octyl, or phenyl groups.