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Large scale protein production of the extracellular domain of the transforming growth factor- type II receptor using the Pichia pastoris expression system

Posted by on in 2003
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  Alwin Scharstuhl, Harrie Glansbeek, Elly L. Vitters, Peter M. van der Kraan and Wim B. van den Berg
Journal of Chromatography B, Volume 786, Issues 1-2, 25 March 2003, Pages 271-277
Rheumatology Research Laboratory, Department of Rheumatology, University Medical Center Nijmegen, Geert Grooteplein zuid 26-28, Nijmegen, 6525 GA, The Netherlands
Available online 15 October 2002.


To study the (patho)physiological role of transforming growth factor- (TGF-), potent and selective inhibitors are necessary. Since TGF- 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- 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-.

Author Keywords: Transforming growth factor

Subject-index terms: Pichia pastoris; Expression system; Protein production

Corresponding author. Tel.: +31-24-361-8870; fax: +31-24-354-0403
European Contest for Young Scientists on Protein Purification: From Gene to Functional Protein .

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