Abstract
The extracellular domains (ECD) of epidermal growth factor receptors, ErbB1, 2, 3 and 4, were designed as soluble dimeric forms. Each ECD was fused to a short hinge region derived from IgG, such that the stable dimer could be formed with disulfide bridges. This hinge-tagged design minimized the molecular weight to approximately 50% of the conventional Fc-fusion design without an Fc domain of IgG. The refolded dimers could be easily analyzed and characterized by SDS-PAGE. Hinge-tagged soluble ErbBs demonstrated significant affinity for betacellulin and heregulin. The IgG hinge-tag should be a simple method to design soluble dimers that would be useful for high throughput screening of ligands, antagonists or derivatives.
| Original language | English |
|---|---|
| Pages (from-to) | 361-366 |
| Number of pages | 6 |
| Journal | Biotechnology Letters |
| Volume | 32 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 01-02-2010 |
| Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
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Otani, T., Hashizume, T., Nagaoka, T., Fukuda, T., Tang, C. K., Salomon, D. S., & Seno, M. (2010). Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB). Biotechnology Letters, 32(3), 361-366. https://doi.org/10.1007/s10529-009-0160-9