Autophosphorylation of the Insulin-like Growth Factor I Receptor Cytoplasmic Domain

The cytoplasmic domain of the β subunit of the insulin-like growth factor I receptor (amino acids 936–1337) was overexpressed in Sf9 insect cells using a baculovirus expression system, and the 6-His tagged receptor was purified by metal-affinity chromatography. Autophosphorylation of the receptor wa...

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Veröffentlicht in:	Biochemical and biophysical research communications 2000-12, Vol.279 (3), p.955-960
Hauptverfasser:	Lopaczynski, Wlodzimierz, Terry, Cheryl, Nissley, Peter
Format:	Artikel
Sprache:	eng
Schlagworte:	6-His tag Animals Cells, Cultured Chromatography, Gel Cytoplasm - metabolism Dimerization Disulfides - metabolism Humans IGF-I receptor dimer Insecta insulin receptor Phosphorylation Plasma - metabolism Protein Structure, Tertiary Protein-Serine-Threonine Kinases - metabolism Rabbits Receptor, IGF Type 1 - chemistry Receptor, IGF Type 1 - metabolism Serine - metabolism Threonine - metabolism
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