IAM.PC is for simplified protein isolation and purification, allowing for rapid purification of membrane proteins while maintaining biological activity.
The phase is based on the prevalent membrane lipid, phosphatidylcholine (PC), and consists of monolayers of amphiphilic phospholipids covalently bonded to aminopropyl silica particles through a terminal amide linkage. As a result, the bulky phosphatidylcholine groups shield many of the amine binding sites on the silica surface, preventing amine interaction with protein molecules.
The membrane nature of the IAM phase imparts surface characteristics, which are useful in the chromatography of membrane proteins. These include high protein loading, increased protein recovery, recovery of functional activity, and selectivity for membrane proteins.
Large membrane proteins can interact with any combination of polar head, hydrophobic chain, or inner amine groups. The subsurface has been show to interact with certain solutes and may or may not contribute to the separation of a given molecule.