Dundee: High-throughput screening of conditions for protein solubilisation

03 Jun 2008 | News

Licensing opportunity

Researchers at Dundee University, Scotland, are looking for companies to license a high-throughput screening system that identifies buffer conditions required for maintaining proteins in solution. The technique tests up to 96 buffer conditions simultaneously. This is achieved by mixing test-solubilising solutions with the samples, followed by protein quantification using a conventional protein assay kit.

Maintaining proteins in soluble form is key to creating large numbers of protein constructs and expression systems. Many proteins are prone to aggregate in conventional buffers containing high salt and reducing agents such as DTT.

Effective protein isolation using ion-exchange or affinity chromatography requires the removal of buffer components such as high-salt or imidazole, which often causes proteins to fall out of solution. Additives that maintain proteins in solution exist; however, testing them against an array of factors such as pH is time-consuming and requires large amounts of sample.

The screening technique developed at Dundee allows a range of solubilising solutions to be tested with their adequate controls. This method tests of a variety of pHs, buffers and additives, and, say the researchers, identifies conditions for optimal maintenance of proteins in solution, in a time-efficient manner.


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