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 p...

TAP (tandem affinity purification) allows rapid and clean isolation of a tagged protein along with its interacting partners from cell lysates. Initially developed in yeast, the TAP method has subsequently been adapted to other cells and organisms. In combination with MS analysis, this method has become an indispensable tool for systematic identification of target-associated protein complexes. T...

We report our experimental results supporting the hypothesis that a specific metal-chelating peptide (CP) on the NH2 terminus of a protein can be used to purify that protein using immobilized metal ion affinity chromatography (IMAC). The potential utility of this approach resides with recombinant proteins since the nucleotide sequence that codes for the protein can be extended to include codons...