Volker Nölle

Solubilization and renaturation of biologically active human bone morphogenetic protein-4 from inclusion bodies

Highlights • Biologically active rhBMP-4 was produced in a prokaryotic host as inclusion bodies.• Different refolding recipes were tested for optimal dimerization yield.• One-step purification of dimer with cation-exchange membrane chromatography.• The product induces trophoblast differentiation in induced pluripotent stem cells.• Comparison between commercial rhBMP-4 from cell culture and product from E. coli.

Sicherung der Produktqualität rekombinanter Wachstumsfaktoren

The demand for high grade recombinant proteins is growing. Especially in the field of cell-based therapies, all materials used, including cytokines and growth factors must comply to the highly demanding GMP specifications. We show how essential protein parameters are monitored to ensure consistent high product quality using the cytokine interleukin-4 as an example.