Protein production in yeast

Complex eukaryotic (e.g. human, mouse, llama, ...) proteins (e.g. membrane proteins, receptors, cytoplasmic proteins, secreted proteins like cytokines, chemokines, e.) can be expressed recombinantly in Pichia pastoris and purified up to in vivo-grade purity (Endotox-free) or for crystallography. From construct to protein in one month under optimal circumstances.

Preferentially, the gene of interest is provided codon optimized for expression in Pichia pastoris (not essential). For production and purification, relevant references to previous work and the conditions required for future work (e.g amount required, purity, endotox-free?, sample buffer requirement can be very helpful). We can offer both tagged and tag-less protein purification. We have a broad range of biophysical characterization methods available for detailed analysis of the produced protein.

Using Pichia pastoris we can rapidly clone, express and purify proteins of interest for use in bio-assays or in vivo vaccination/treatment/antigen-challenge…-experiments. We have developed an OPENPichia strain and compatible modular cloning toolbox enabling license-free strain development and protein production.
 

Center for medical Biotechnology, Lab for Medical Biotechnology, Technologiepark Zwijnaarde75, B-9052 Zwijnaarde
 

Responsible PI and contact: prof. Nico Callewaert (PhD) and dr. Nele Vervaet