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Fig. 1 | Journal of Experimental & Clinical Cancer Research

Fig. 1

From: DTL promotes cancer progression by PDCD4 ubiquitin-dependent degradation

Fig. 1

DTL bound with PDCD4. a 293 T cells were transfected with Flag-DTL plasmid and the cell lysates were co-immunoprecipitated by Flag magnetic affinity resin. Several differential bands were shown in Coomassie staining SDS-PAGE gels. The band indicated by array showed protein at the position about 55KDa, which was proved to be PDCD4 in the mass spectrometry experiment. b 293 T cell lysates were prepared by weak RIPA lysis and co-immunoprecipitated by DTL antibody with IgG as negative control. The result showed that PDCD4 interacts with DTL. c Co-immunoprecipitation assay using PDCD4 as bait protein demonstrated the interaction between PDCD4 and DTL. d Sub-localizations of DTL and PDCD4 were analyzed using immunofluorescence. Laser Confocal Microscopy photos showed that DTL and PDCD4 were co-localization both in the nuclei and cellular matrix. The scale bars represent 5 μm. e CUL4A constructed in PLVX-AcGFP-N1 vector was transient transfected into 293 T cells and immunoprecipitated by PDCD4 antibody. f shDTL constructed in PLKO.1-puro was transient transfected into 293 T cells. Interaction between PDCD4 and CUL4A was detected

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