Proteins are complex molecules that can have positively or negatively charged surface areas. The most widely used method to produce a pure protein is ion exchange (IEX) chromatography. It separates molecules based on the charge distribution on their surface with functional groups of the chromatography media carrying the opposite charge. By choosing the right chromatographic conditions (e.g. salt concentration, buffer system and pH), proteins can be separated from impurities. In common practice, bound molecules are selectively eluted by step-wise or continuously increasing concentration of a monovalent salt, or impurities can be bind to the resin or membrane in a flow through mode.
Tentacle Ion Exchange Chromatography Technology: How it Works
MilliporeSigma offers a comprehensive product portfolio of IEX chromatography, to provide you with the solution you need.
A synthetic polymer media, with proprietary tentacle technology, offers a number of advantages over conventional resins. Long linear polymer chains increase the functional groups’ accessibility for biomolecules, ensuring a tighter binding of target substances and sharp elution profiles. The result: high throughput and high selectivity with excellent purity and yield.
A unique family of ion exchangers designed for highly productive downstream purification of biomolecules. Based on the proven tentacle technology, its rigid base beads enable easy packing. With its high binding capacity and excellent pressure-flow behavior, you are able to reduce time and manufacturing costs, resulting in outstanding productivity.