Affinity chromatography is a method for separating biomolecules from a mixture based on highly specific macromolecular binding interactions between a biomolecule and another substance. The specific type of binding interaction depends on the biomolecule of interest; antigen and antibody, enzyme and substrate, receptor and ligand, or protein and nucleic acid binding interactions are frequently exploited for isolation of various biomolecules.
In a typical affinity chromatography experiment, ligands are attached to a solid, insoluble matrix to form stable covalent bonds. First load the stationary phase into the column that introduces the mobile phase. Molecules bound to the ligand will remain bound to the immobilized phase. A wash buffer is then used to remove non-target biomolecules by disrupting their weaker interactions with the stationary phase, while biomolecules of interest will remain bound. The target biomolecule can then be removed by using a so-called elution buffer, which disrupts the interaction between the bound target biomolecule and the ligand. The target molecule is thus recovered in the eluting solution. Compared with other chromatographic methods, affinity chromatography has higher separation selectivity and separation resolution.
Fig.1 Schematic diagram of affinity chromatography principle.
STEMart provides you with a variety of affinity chromatography technology equipment to help you quickly and efficiently separate and analyze to meet your various R&D and application needs. If you have any questions or requirements for chromatography equipment, please feel free to contact us.
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