11 - 12 Nov 2020  • 

Optimising Expression Platforms


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11 - 12 Nov 2020


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Optimising Expression Platforms convenes protein expression & production specialists to share their real-world experiences and results. We have .. Read more engineered a large panel of CHO cell lines for the production of therapeutic proteins with tailor-made glycosylation. Recombinant protein production is a widely used technique, yet half of these experiments fail at the expression phase and only a quarter of target proteins are successfully purified. We have discovered that the energetics of RNA structure ensembles, that model the 'accessibility' of translation initiation sites, accurately predicts the expression outcomes of 11,430 recombinant protein production experiments in Escherichia coli. We have further discovered that normalised B-factors, that model the 'flexibility' of amino acid residues, accurately predicts the solubility of 12,158 recombinant proteins expressed in Escherichia coli. We have developed TIsigner (Translation Initiation coding region designer) and SoDoPE (Soluble Domain for Protein Expression) that allows users to choose a protein region of interest for optimising expression and solubility, respectively. Ipsen Bioinnovation produces engineered protein neurotoxins to support the discovery and development of novel pharmaceutical botulinum toxins.

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