Recombinant Protein Expression & Purification

We know that recombinant proteins or peptides are pivotal for your application or research. For that reason, we have established our recombinant protein expression and purification platform, where we combine the most recent knowhow and full transparency from dedicated people.

We can support you with the design of vectors and the choice of expression system.

Our experience tells us, that the best results are obtained when we understand how the protein is implemented in your application. We ensure that the construct is verified by DNA sequencing.

The palette of expression systems in our facilities includes E. Coli such as Rosetta, BL21 (DE3) and SHuffle E, and several mammal cell systems: Expi293f, ExpiCHO. We

Protein purification in Ovodan Biotech facilities is based on our automated chromatographic technology using customized ÄKTA equipment. The purification strategy is carefully implemented in the vector design to ensure as few steps as possible.

As standard our QC includes, SDS page and ELISA if antibodies are available. However, we strongly recommend mass spectrometry to verify aa-sequence and identify glycosylation sites. This expertise we are also able to provide.


As a crucial part of the Ovodan Biotech SARS-CoV-2 antibody discovery project we needed to secure materials for immunizations, screening rounds and affinity purification of antibodies.

The project aimed at antibody discovery of potential neutralizing antibodies, hence the Receptor Binding Domain aa 319-541 was chosen as the relevant sequence.

SARS-CoV-2 activities are primarily relevant for human infections, so we chose to use the Expi293f expression system. The vector was designed to include the Tyr-Pho signal peptide and a N-terminal HIS-tag.

The pilot-scale expression in a 25mL batch resulted in a limited yield. QC by SDS-page unveiled a 37 kDa molecule which indicates that the protein is glycosylated. When verifying the protein by Mass Spectrometry we obtained full coverage of the aa sequence and identified the two glycosylation sites.

Available recombinant proteins