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. Author manuscript; available in PMC: 2012 Feb 9.
Published in final edited form as: J Cell Physiol. 2008 Jun;215(3):803–817. doi: 10.1002/jcp.21365

Fig. 7.

Fig. 7

Tyrosine phosphorylation analysis of different FGFR constructs overexpressed in 293T cells. Western blotting with PY20 antibody was used for detecting phosphorylation in immunoprecipitated FGFR proteins. (A) Schematics of constructs used in the studies summarized in Figs. 7 and 8; epitop tags at the c-terminus of each construct (myc or HA) were utilized for immunoprecipitation and Western blot analysis with corresponding anti-myc and anti-HA antibodies. (B, C) Western blot detections of immunoprecipitated FGFR4 proteins; overeexpressed FGFR4(−16) and FGFR3-4(−16), analyzed in parallel, also yielded no phosphorylation (data not shown). (D) Assessment of SU5402 (40 nM) effect on tyrosine phosphorylation of overexpressed FGFR3-1; drug added for 30 minutes prior to lysate harvesting impaired phosphorylation of the chimeric receptor. Plain control (untreated cells) and inhibitor vehicle control (DMSO) were analyzed in parallel. Also shown in the panel, only the non-phosphorylated FGFR3-1 form (i.e., SU5402-treated) reacted with the anti-FGFR1 antibody in Western blot analysis.