Protein Science

A client was looking to solve the crystal structure of a secreted protein which contained a number of disulphide bonds and potential N-linked glycosylation sites, which leads to the attachment of complex sugar molecules. There was already literature available describing the expression of [...]

As a leading protein purification company, BiVictriX required us to develop a method to purify 10mg each of 24 different antibody-binding fragments (Fabs) to be tested in assays. Once analysed by BiVictriX, a smaller number of chosen constructs were to be scaled up by [...]

A client asked us to express and purify at least 2 mg each of two similar enzymes for selectivity assays. There was literature precedent for both proteins, and a similar approach would be taken with each, purifying via affinity chromatography followed by size exclusion [...]

Our client needed a nuclear receptor protein for Biacore Surface plasmon resonance (SPR) studies. There was precedent for the production of the protein and was available commercially, but it was well known to have stability issues.  Our challenge was to supply high quality, pure, [...]

We were asked to generate a secreted protein that is known to undergo significant post-translational modification. The challenge was to not only make it but to clearly demonstrate that all the required post-translational modifications had occurred. Our Solution An HEK293 system [...]

Our client required 20mg of protein for NMR structural studies. The protein was known to be post-translationally modified with palmitic acid on a cysteine residue. Our Solution Our solutions to this challenge were to reduce the temperature during expression far below [...]

Our client required >2 mg of a novel, secreted protein for X-ray structure determination studies. The protein was thought to be N-glycosylated. Our Solution Our solution was to evaluate three C-terminally deleted constructs for secreted expression in HEK cells, based on structural alignments [...]