EXPERTS IN INSECT, MAMMALIAN AND BACTERIAL EXPRESSION

Protein production and purification from OET
Oxford Expression Technologies Ltd (OET) is a name that you can trust within the field of pharmaceuticals and biotechnology. We offer a range of services including optimisation of expression and amplification of a virus, and once those process have taken place, we can then produce rout protein within insect or mammalian cells. We also offer protein purification services too. Find out more by getting in touch with our trusted team.

Protein purification and production within insect or mammalian cells
We provide tailored protein purification services combining technical expertise with flexible, scalable processes. Supporting early-stage vaccine R&D and broader protein development. We deliver consistent, reliable, high-quality results from research through to large-scale engineering runs. Full documentation can be provided in the form of Batch Records and CoAs.
Protein Production
We can easily scale insect, mammalian and bacterial cells for biomass production up to 40 L or more in shake flasks. Alternatively, we can use our Wave bioreactor system with capacity to 25 L per run, enabling efficient and controlled production at scale. During cell harvest, we utilise high-capacity centrifugation systems or advanced hollow fibre membrane technologies to efficiently recover material from infected cultures prior to purification.
Protein Purification
We work closely with you to design the most effective purification strategy, tailored to the target protein sequence, expression system, cell line and key properties such as size, charge, and solubility. Our team uses a broad range of techniques including; affinity chromatography, ion exchange, hydrophobic interaction and size exclusion chromatography, often in combination to maximise purity and yield. We also optimise buffer conditions (pH, salts, and additives such as reducing agents, protease inhibitors and detergents) to maintain protein integrity. Engineering runs can be produced to ‘endotoxin-free’ standards for preclinical applications.
To view an step by step example of protein purification of eGFP using our pOETeGFP Sf9 reporter plasmid then click here

Expression in Mammalian Cells
Mammalian expression projects are performed using plasmid constructs for either transient or stable expression in several different mammalian cell lines. We have access to a wide range of mammalian promoters to customise gene expression including our own BacMam vectors.
Stable Cell Line
Stable cell lines are produced following transfection of mammalian cells with the plasmid containing the target gene and a selectable antibiotic marker. The cell line is either banked or screened to produce a clonal cell line.
Transient Expression
The plasmid containing the gene of interest is transfected into the target mammalian cell line and expression levels are determined by SDS-PAGE/Western blot.
The plasmid containing the gene of interest is transfected into the target mammalian cell line and expression levels are determined by SDS-PAGE/Western blot.
Scale up and Purification
To find out more about protein production and purification services, contact Oxford Expression Technologies Ltd.
Expression in Bacterial Cells
We offer recombinant protein expression services in bacterial cells, including gene synthesis and cloning, transformation into E. coli, expression optimisation, scale-up, and protein purification to deliver high-quality recombinant protein for research and commercial applications.
Gene Synthesis and Cloning
We can arrange the synthesis of any gene or we can work with any plasmid you supply as a starting material.
Recombinant Bacteria
We offer a wide range of bacterial host cells, tailored to the project requirements
Once optimal expression conditions are confirmed at small scale, produciton can be scaled ufor purification of the target protein
Scale up and Purification


CONTACT US
Oxford Expression Technologies Ltd
Unit 9 Innovation Quarter
Oxford Technology Park
Kidlington
OX5 1GN
+44 (0) 1865 536808


