C4 A (low ligand - butyl) is a hydrophobic ligand, used in hydrophobic interaction chromatography (HIC). Due to low ligand density of butyl groups on the monolithic surface it is particularly suitable for protein separation.
C4 A (low ligand - butyl) is a hydrophobic ligand, used in hydrophobic interaction chromatography (HIC). Due to low ligand density of butyl groups on the monolithic surface it is particularly suitable for protein separation.
Affinity chromatography is based on the biospecific interaction between a biomolecule (commonly antibody) and its native or synthetic ligand. The effective ligands are immobilized on CIM® monoliths and associate with your antibodies in a highly specific and reversible manner. Association takes place at physiologic pH, while dissociation is most commonly effected by a pH shift. The strength of interaction strongly depends on the type of ligand and antibody. Affinity chromatography has become state of the art in antibody purification. We provide a selection of affinity monolithic columns for efficient purification of IgG and IgM.
Ion exchange chromatography (IEC) is based on electrostatic interaction between a charged molecule and an oppositely charged stationary phase. Depending on the type of charge, one discriminates between anion (AEC) and cation exchange chromatography (CEC). Your molecule binds at low salt concentration, while desorption is effected by increasing salt concentration. Ion exchange ligands are classified as either strong or weak, depending on their charge as a function of pH. IEC is a versatile and extensively used tool in downstream processing, and we contribute with a variety of weak and strong AEC and CEC monolithic columns.
Hydrophobic interaction chromatography (HIC) capitalizes the interaction between non-polar molecules and a hydrophobic stationary phase. Hydrophobic patches of your molecule interact with mildly hydrophobic ligands. The retention of biomolecules is promoted by salt; therefore, the mobile phase contains high salt concentration. Desorption in return is effected by decreasing salt concentration. Due to its exceptional separation power and the maintenance of biologic activity despite hydrophobic conditions, HIC became an integrated part of chromatographic solutions. We offer a selection of three different HIC monolithic columns.
Any individual application employing a biospecific, non-commercial ligand-protein or ligand-peptide interaction requests a tailor-made solution. By coupling your specific ligand to an activated CIM® monolithic surface via a hydrolytically stable covalent linkage, you will obtain your custom made affinity column. The choice of coupling method depends on the ligand to be immobilized; i.e., the chemistry of its active groups, its pH and temperature stability, reactivity, etc. We support your individual needs by providing different activated CIM® monolithic columns.