Related Experiment Video
Updated: Sep 26, 2026
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Large scale protein production of the extracellular domain of the transforming growth factor-beta type II receptor
Alwin Scharstuhl1, Harrie Glansbeek, Elly L Vitters
1Rheumatology Research Laboratory, Department of Rheumatology, University Medical Center Nijmegen, Geert Grooteplein zuid 26-28, 6525 GA, Nijmegen, The Netherlands. a.scharstuhl@ncmls.kun.nl
Abstract:
To study the (patho)physiological role of transforming growth factor-beta (TGF-beta), potent and selective inhibitors are necessary. Since TGF-beta signaling is initiated by the high affinity binding to the type II receptor (RII), the extracellular part of RII (solRII) can function as a TGF-beta antagonist. SolRII was cloned and large-scale protein synthesis was performed in the yeast Pichia pastoris expression system. Our results indicate that via this system, high levels of pure concentrated solRII can be obtained. Moreover, purified solRII is an active protein as shown by ELISA and bioassay. In conclusion, our large-scale protein expression procedure results in high quantities of purified solRII, which is a powerful tool to study the natural role of TGF-beta.
