Fig. 2.
Fig. 2. Epo-independent HCDP210 cells. / (A) Expression and tyrosine phosphorylation of P210 in Epo-independent HCDP210 cells: Fifty million serum-starved HCD57 and HCDP210 cells were lysed and ABL immunoprecipitates were fractionated on a 6% sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), transferred to nitrocellulose, and probed with antiphosphotyrosine (α P-Tyr) (4G10, left panel) or anti-ABL antibodies (right panel). Arrows show BCR-ABL P210 (top) and the endogenous c-ABL (bottom) proteins. IP indicates immunoprecipitation. (B) Growth curve of HCD57 (diamond) and HCDP210 (square) cells in the presence (solid lines) and the absence (dotted lines) of 2 u/mL Epo. (C) Constitutive JAK2 tyrosine phosphorylation in HCDP210 cells: serum starved cells were stimulated with or without Epo (100 u/mL) for 5 minutes. JAK2 immunocomplexes were fractionated on an 8% SDS-PAGE, transferred to nitrocellulose, and probed with 4G10 (upper panel) or anti-JAK2 antisera (lower panel).

Epo-independent HCDP210 cells.

(A) Expression and tyrosine phosphorylation of P210 in Epo-independent HCDP210 cells: Fifty million serum-starved HCD57 and HCDP210 cells were lysed and ABL immunoprecipitates were fractionated on a 6% sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), transferred to nitrocellulose, and probed with antiphosphotyrosine (α P-Tyr) (4G10, left panel) or anti-ABL antibodies (right panel). Arrows show BCR-ABL P210 (top) and the endogenous c-ABL (bottom) proteins. IP indicates immunoprecipitation. (B) Growth curve of HCD57 (diamond) and HCDP210 (square) cells in the presence (solid lines) and the absence (dotted lines) of 2 u/mL Epo. (C) Constitutive JAK2 tyrosine phosphorylation in HCDP210 cells: serum starved cells were stimulated with or without Epo (100 u/mL) for 5 minutes. JAK2 immunocomplexes were fractionated on an 8% SDS-PAGE, transferred to nitrocellulose, and probed with 4G10 (upper panel) or anti-JAK2 antisera (lower panel).

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