Fig. 8.
Fig. 8. βc phosphorylated in response to GM-CSF, IL-3, or IL-5 is immunoprecipitable by anti-GMRα antibody. (A) Mo7e cells were starved overnight and then treated with either 6 nmol/L GM-CSF, IL-3, or medium for 5 minutes at 4°C and then immunoprecipitated with either anti–IL-3Rα (9F5), anti-GMRα (8G6), or anti-βc (8E4) antibody. (B) TF-1.8 cells were starved overnight and then treated with either 6 nmol/L GM-CSF, IL-3, or IL-5 or medium for 5 minutes at 4°C and then immunoprecipitated with either anti-GMRα (8G6) or anti-βc (8E4) antibody. Immunoprecipitated proteins were separated on 7.5% SDS-PAGE, Western transferred, and then immunoblotted with antiphosphotyrosine antibody (PY20).

βc phosphorylated in response to GM-CSF, IL-3, or IL-5 is immunoprecipitable by anti-GMRα antibody. (A) Mo7e cells were starved overnight and then treated with either 6 nmol/L GM-CSF, IL-3, or medium for 5 minutes at 4°C and then immunoprecipitated with either anti–IL-3Rα (9F5), anti-GMRα (8G6), or anti-βc (8E4) antibody. (B) TF-1.8 cells were starved overnight and then treated with either 6 nmol/L GM-CSF, IL-3, or IL-5 or medium for 5 minutes at 4°C and then immunoprecipitated with either anti-GMRα (8G6) or anti-βc (8E4) antibody. Immunoprecipitated proteins were separated on 7.5% SDS-PAGE, Western transferred, and then immunoblotted with antiphosphotyrosine antibody (PY20).

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