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.
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U2 - 10.1007/s10529-009-0160-9
DO - 10.1007/s10529-009-0160-9
M3 - Article
C2 - 19898750
AN - SCOPUS:77649338416
VL - 32
SP - 361
EP - 366
JO - Biotechnology Letters
JF - Biotechnology Letters
SN - 0141-5492
IS - 3
ER -