Name: Size Exclusion Chromatography Resins
Description:Size exclusion chromatography(SEC), also referred to as gel-filtration chromatography, uses porous particles to separate biological molecules of different sizes. Molecules that are smaller than the pore size can enter the particles and therefore have a longer path length and longer residence time than larger molecules that cannot enter the particles.
Name: Ion Exchange Chromatography Resins
Description:Ion Exchange Chromatography is driven by interactions between the charges in the target molecule and the charges of the immobilized ligand on the chromatography resin. Ion exchange chromatography as a whole can be divided into two different sub types. Cation exchange chromatography, in which positively charged species in the mobile phase bind to a negatively charged ligand on the resin; and anion exchange chromatography, in which the binding species in the mobile phase are negatively charged, and the immobilized ligand is positively charged.
Name: Hydrophobic interaction chromatography Resins
Description:Hydrophobic interaction chromatography(HIC) is a powerful tool for the process purification of biomolecules. The technique utilizes the accessible hydrophobic regions located on protein surfaces and their interactions with a weakly hydrophobic stationary phase. HIC is an excellent complement to ion exchange and size exclusion chromatography particularly when protein isoforms exist or when feedstock impurities are of similar isoelectric point or molecular weight. The selectivity differences exploited by HIC can also be used after affinity separations in which closely related proteins with similar recognition sites are not distinguishable by the affinity ligand.
Name: Affinity chromatography Resins
Description:Affinity chromatography makes use of specific binding interactions between molecules. It is this specificity that makes this mode of chromatography especially attractive as a capture step to isolate the target molecule from crude extracts. A particular ligand is chemically immobilized or "coupled" to a solid support so that when the crude extract is passed over the column, those molecules having a specific binding affinity to the ligand become adsorbed. After the non-specifically binding components are washed away, the target molecule is desorbed from the support, resulting in its purification from the original sample.