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 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
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Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB). / Otani, Takayuki; Hashizume, Toshihiro; Nagaoka, Tadahiro; Fukuda, Tomoko; Tang, Careen K.; Salomon, David S.; Seno, Masaharu.
In: Biotechnology Letters, Vol. 32, No. 3, 01.02.2010, p. 361-366.Research output: Contribution to journal › Article
TY - JOUR
T1 - Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB)
AU - Otani, Takayuki
AU - Hashizume, Toshihiro
AU - Nagaoka, Tadahiro
AU - Fukuda, Tomoko
AU - Tang, Careen K.
AU - Salomon, David S.
AU - Seno, Masaharu
PY - 2010/2/1
Y1 - 2010/2/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77649338416&partnerID=8YFLogxK
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U2 - 10.1007/s10529-009-0160-9
DO - 10.1007/s10529-009-0160-9
M3 - Article
VL - 32
SP - 361
EP - 366
JO - Biotechnology Letters
JF - Biotechnology Letters
SN - 0141-5492
IS - 3
ER -