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Protein Affinity Purification
Yeda R&D Co. Ltd Israel flag Israel
Abstract ID:
An efficient protein purification system.Affinity chromatography using affinity tags can be used as a rapid, facile purification separation technique for isolating biologically active compounds, depending upon the affinity properties of the tag rather......
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An efficient protein purification system.


Affinity chromatography using affinity tags can be used as a rapid, facile purification separation technique for isolating biologically active compounds, depending upon the affinity properties of the tag rather than those of the target protein. Some tags are relatively small in size (e.g. His-tag), which allows for minimal interaction with the target protein. Nevertheless, these tags fail to provide a highly specific interaction, which leads to low column capacity and sample impurities. Other affinity tags (e.g. maltose binding protein, glutathione-S-transferase) are in some cases relatively large, sometimes even larger than the protein of interest, and thereby might impair protein activity. The cellulosomal dockerin-cohesin interaction may serve as an efficient affinity purification method, however the binding to the immobilized cohesion is only partially reversible upon treatment with EDTA, and only negligible amounts of the target protein are eluted from the affinity column. The present invention allows for an efficient protein purification using a truncated dockerin affinity tag.


Applications


Affinity-based protein purification system


Advantages








    • Excellent protein recovery from the column, with high levels of purity, in a single step directly from crude cell extracts






    • Truncated dockerin tag provides an improved affinity tag compared to the full-length wild-type module, since higher yields of target protein are achieved under milder and more effective elution conditions





    • Truncated dockerin tag has no significant effect on the activity of the purified protein





    • The system affords facile, cost-effective and efficient regeneration of the column for repeated use, with very high levels of capacity upon repeated rounds of loading and elution





Technology's Essence


Efficient degradation of cellulose by the anaerobic thermophilic bacterium Clostridium thermocellum is carried out by the multi-enzyme cellulosome complex. The enzymes on the complex are attached in a calcium-dependent manner via their dockerin (Doc) module to a cohesin (Coh) module of the cellulosomal scaffoldin subunit. In the present technology, the Coh–Doc interaction was optimized for the purpose of protein affinity purification, by using a shortened Doc of only 48 residues, which is sufficient to function as an effective affinity tag. Thus, Coh–Doc affinity columns provide an efficient and attractive approach for purifying proteins.


Licensing Status

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FEATURED
Last Updated May 2016
Technology Type MECHANISM
Phase of Development EARLY STAGE
CORPORATION