Affinity chromatography is a versatile separation protocol that uses the biological interactions for characterization and detailed analysis of sample components. It is based on highly specific interactions between two molecules, such as the interactions between enzyme and its substrate, receptor, and ligand, or antibody and antigen. These reversible interactions are…

Developed by Marion M. Bradford in 1976, the Bradford assay is quick protocol, and the same amount of proteins are used as the Lowry assay. This assay is somewhat accurate, and out of range samples can be retested within minutes. This assay is recommended for general use, especially for assessing…

Fast protein liquid chromatography (FPLC) is a type of liquid chromatography that provides high resolution by small-diameter stationary phases for protein characterization and separation. The technique features high loading capacity, biocompatible buffer systems, fast flow rates, and stationary phases for common chromatography modes (e.g., gel filtration, ion exchange, reversed phase,…

Gel-filtration chromatography, also known as the size exclusion chromatography, is a versatile technique that permits the separation of proteins and other biological molecules. The gel filtration chromatography separates the proteins solely based on molecular size differences. For this, a porous matrix is used to which the molecules, for steric reasons,…

Ion Exchange Chromatography (IEC) is a powerful liquid chromatographic technique used for bioseparation. The separation is done by a reversible interaction between charged molecules of the sample with charged ligands attached to a column. The method offers a sizeable sample-handling capacity, powerful resolving ability, broad applicability, moderate cost, and the…