2019-05-02T10:36:48+00:00

Time critical purification of multiple Fab constructs for assay

Time critical purification of multiple Fab constructs for assay 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 us to generate 100 mgs for use in their conjugation experiments. [...]

2019-05-02T10:37:45+00:00

Adapting use of size exclusion chromatography to improve yields of an unstable, purified protein

Adapting use of size exclusion chromatography to improve yields of an unstable, purified protein 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 chromatography. However the literature referred to [...]

2019-05-02T10:37:51+00:00

Generation of a Nuclear Receptor Protein with known stability issues for SPR studies

Generation of a Nuclear Receptor with known stability issues for SPR studies 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, characterised protein. The protein needed a His tag [...]

2019-05-02T10:37:58+00:00

Production and analysis of an extensively post-translationally modified secreted protein

Production and analysis of an extensively post-translationally modified secreted protein 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 Solutions An HEK293 system was chosen because, as a mammalian cell line, [...]

2019-05-02T10:38:04+00:00

Production of a post-translationally modified protein

Production of a post-translationally modified protein 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 challenge was to obtain this amount of protein after expression in E. coli and demonstrate palmitoylation using mass spectrometry analysis. The protein was well expressed but very insoluble in initial experiments. [...]

2019-05-02T10:38:09+00:00

Generation of a novel, secreted protein for structure determination

Generation of a novel, secreted protein for structure determination 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 challenge was to obtain sufficient >95% pure protein for crystallisation experiments, as measured by SDS-PAGE, size exclusion and mass spectrometry analysis.  In addition, we were also aiming to take forward the shortest, [...]