Abstract
Immunoglobulin G (IgG)-Sepharose is often used for purification of protein A- and tandem affinity purification (TAP)-tagged proteins from eukaryotic cells, but because it is based on an agarose matrix, it is not always optimal for all proteins. Synthetic matrices such as IgG-Dynabeads have improved properties over IgG-Sepharose but are generally expensive. Here we describe the preparation and properties of an IgG matrix based on Fractogel EMD beads. As a synthetic-based matrix, IgG-Fractogel has clear advantages over IgG-Sepharose. IgG-Fractogel can also be used in applications that usually use IgG-Dynabeads but at a significantly reduced cost.