Fig. 1.
Fig. 1. Coimmunoprecipitation of GMRα and βc from primary CML cells. (A and B) CML cells were 125I–surface-labeled, treated with (+) or without (−) GM-CSF or IL-3 (6 nmol/L) for 5 minutes at 4°C and immunoprecipitation was performed either with anti-GMRα (8G6), anti–IL-3Rα (9F5), or anti-βc (4F3) MoAb. Immunoprecipitated proteins were separated on 7.5% SDS-PAGE and visualized by phosphorimager and are presented at exposure levels appropriate for the specific signal obtained. (C) Proteins immunoprecipitated from CML cells with different antireceptor antibodies either in the presence (+) or absence (−) of GM-CSF were subjected to Western transfer and immunoblotted using a polyclonal anti-βc antibody.

Coimmunoprecipitation of GMRα and βc from primary CML cells. (A and B) CML cells were 125I–surface-labeled, treated with (+) or without (−) GM-CSF or IL-3 (6 nmol/L) for 5 minutes at 4°C and immunoprecipitation was performed either with anti-GMRα (8G6), anti–IL-3Rα (9F5), or anti-βc (4F3) MoAb. Immunoprecipitated proteins were separated on 7.5% SDS-PAGE and visualized by phosphorimager and are presented at exposure levels appropriate for the specific signal obtained. (C) Proteins immunoprecipitated from CML cells with different antireceptor antibodies either in the presence (+) or absence (−) of GM-CSF were subjected to Western transfer and immunoblotted using a polyclonal anti-βc antibody.

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