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Expression of Recombinant Extracellular Domain of the Type II Transforming Growth Factor-β Receptor: Utilization in a Modified Enzyme-Linked Immunoabsorbent Assay to Screen TGF-β Agonists and Antagonists

✍ Scribed by Mark S. Fahey; David Dawbarn; Shelley J. Allen; Ian C. Paterson; Stephen S. Prime

Publisher: Elsevier Science
Year: 2001
Tongue: English
Weight: 87 KB
Volume: 290
Category: Article
ISSN: 0003-2697
DOI: 10.1006/abio.2000.4948

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✦ Synopsis

TGF-␤ is a ubiquitous protein that exhibits a broad spectrum of biological activity. The prokaryotic expression and purification of the extracellular domain of the type II TGF-␤ receptor (T␤R-II-ED), without the need for fusion protein cleavage and refolding, is described. The recombinant T␤R-II-ED fusion protein bound commercially available TGF-␤1 and displayed an affinity of 11.1 nM. In a modified ELISA, receptor binding to TGF-␤1 was inhibited by TGF-␤3. The technique lends itself to high-throughput screening of combinatorial libraries for the identification of TGF-␤ agonists and antagonists and this, in turn, may have important therapeutic implications.