Recombinant Protein Production

Life science research often requires proteins to be expressed in large quantities for functional and structural studies, for use in raising antibodies or for controls during immunoassays. We have access to incubators, equipment and extensive expertise to allow expression of proteins in either eukaryotic or prokaryotic cells. We can perform up-stream molecular biology and down-stream purification of the proteins, using our considerable infrastructure of chromatography systems. If refolds are required, we can investigate optimal conditions to yield well-folded proteins.

Once we have isolated your proteins, we can also perform initial or in depth characterisation, including functional assays and reports on secondary and tertiary structure. For small proteins, we have facilities to solve atomic-level structures by NMR methods. All protein reagents are characterised by polyacrylamide gel analysis and mass spectrometry, where appropriate.

Recombinant proteins can be expressed in mammalian cells, insect cells or bacterials cells and from a variety of vectors. A range of purification tags can be incorporated at N- or C-termini, including cleavable tags. We will work with you to devise and carry out a cloning and expression strategy and follow this through to full purification using FPLC and HPLC. Final products are extensively characterised for identity and purity.

Expression of small proteins in bacteria often works well, particularly if those proteins do not have extensive disulphide cross links. Functional or structural subunits of larger proteins can also be expressed in bacteria.

Larger proteins, or those requiring physiological folding or fidelity of post translational modifications are better expresed in eukaryotic cells.

Not applicable