Affinity media ligands

Affinity media ligands are molecules that are immobilized onto a solid support for use in affinity chromatography. Affinity chromatography is a separation technique used to purify proteins or other biomolecules based on their specific interactions with ligands immobilized on a chromatography matrix.

These ligands have a high affinity for the target molecule, allowing for selective binding and purification. Affinity media ligands can vary widely depending on the target molecule and the desired purification method. Some common types of affinity media ligands include:

Antibodies:

Antibodies are widely used as affinity ligands for the purification of antigens or proteins that specifically bind to the antibody's epitope.

Enzymes:

Enzymes can be used as affinity ligands for the purification of substrates or other proteins that interact with the enzyme.

Receptors:

Cell surface receptors or soluble receptors can be used as affinity ligands for the purification of ligands or other proteins that bind specifically to the receptor.

Metal ions:

Metal ions such as nickel, cobalt, or zinc can be immobilized on a chromatography matrix and used as affinity ligands for the purification of proteins containing specific metal-binding domains, such as polyhistidine tags.

Lectins:

Lectins are proteins that bind specifically to carbohydrate moieties. They can be immobilized on a chromatography matrix and used as affinity ligands for the purification of glycoproteins or other carbohydrate-containing molecules.

Affinity chromatography using media ligands offers high specificity and purity in protein purification processes.