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. 2015 Oct 20;6(41):43743–43758. doi: 10.18632/oncotarget.6193

Figure 3. Surface expression of CDCP1 requires N-glycosylation.

Figure 3

(A) PC3-N2 and PC3-ML2 cells were either treated with 1 μg/ml tunicamycin for 24 h (+TM) or untreated (−TM). The cells were then fixed and subjected to immunofluorescence confocal microscopy using anti-CDCP1 antibody (CS4115, green). The nucleus was counterstained with TO-PRO3 (blue) and the images merged. (B) Protein extracts were prepared from PC3-N2 and ML2 cells that had been surface biotinylated (+) or untreated (−) and additionally grown in the presence (+) or absence (−) of tunicamycin. Biotinylated and nonbiotinylated protein fractions were separated by streptavidin affinity. The biotinylated bound (E) and unbound (FT) fractions, non-biotinylated bound (Ec) and unbound (FTc) fractions were separated by SDS-PAGE and immunoblotted with ant-CDCP1 (CS4115).