Protein Purification

The use of small peptide ‘tags’ in recombinant proteins greatly simplifies their detection and purification. These short sequences may be placed at either the amino-terminus or carboxyl-terminus of fusion proteins. For many purposes the tags need not be cleaved away, because the expressed proteins usually fold correctly and are biologically active. The presence of the tag, however, allows recognition of the fusion protein by an antibody or specific ligand to the tag itself rather than to the protein of interest. Producing an antibody to an individual protein is expensive and time-consuming.

Our antibodies to peptide tags are quite specific. Immuno-precipitation, immuno-blotting and immuno-affinity purification of tagged recombinant fusion proteins allow researchers to monitor their production and purify them with a minimum of steps. The HIS-select nickel affinity ligand similarly captures fusion proteins with a poly-histidine tag. We offer a wide variety of peptide tools to allow the plant proteomics investigator to choose the tag best suited for the target protein.