Inexpensive synthetic-based matrix for both conventional and rapid purification of protein A- and tandem affinity purification-tagged proteins.
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.
Sawin
Kenneth E
KE
Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, UK. ken.sawin@ed.ac.uk
Bicho
Claudia C
CC
Snaith
Hilary A
HA
D002846:Chromatography, Affinity / Q000191:economics / Q000379:methods*; D007074:Immunoglobulin G / Q000737:chemistry; D008689:Methacrylates / Q000737:chemistry; D011506:Proteins / Q000302:isolation & purification; D012685:Sepharose / Q000031:analogs & derivatives; D013205:Staphylococcal Protein A / Q000302:isolation & purification*
D007074:Immunoglobulin G; D008689:Methacrylates; D011506:Proteins; D013205:Staphylococcal Protein A; C036210:immunoglobulin G-sepharose; D012685:Sepharose