Separation of Proteins Containing Thiol by Covalent Chromatography (CAT#: STEM-ACM-0228-CJ)

Covalent chromatography is a method for separation of molecules, based on formation of reversible covalent bonds between functional groups in molecules and complementary structures on a stationary solid phase. Covalent chromatography thus involves a synthetic step by which a solute is covalently immobilized to a solid support—the chemisorbent— later followed by chemical cleavage and regeneration of the sorbent.

Biochemistry; Biomedical

1. Preparation of Column: The column is loaded with solid support such as sepharose, agarose, cellulose etc.. Ligand is selected according to the desired isolate. Spacer arm is attached between the ligand and solid support.
2. Loading of Sample: Solution containing a mixture of substances is poured into the elution column and allowed to run at a controlled rate.
3. Elution of Ligand-Molecule Complex: Target substance is recovered by changing conditions to favor elution of the bound molecules.

• Sample: Plants; Natural Food; Protein; Drug; Pollutants; Blood; Saliva; Serum; Plasma; Antibodies; Viruses & More
• Equipment: Agarose; Silica gel; Aluminium oxide; Acrylate; Organic polymers; Wash Buffer
• (Optional): Ligand; Spacer arm; Column

1. Specially designed to separate proteins containing thiol
2. The most frequently used ligand an adiquate 2′-pyridyl group
3. It is used to purify many proteins, however its application is restricted due to its price and difficult regeneration.