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. 2011 Jan 27;300(4):G627–G636. doi: 10.1152/ajpgi.00563.2010

Fig. 7.

Fig. 7.

c-jun binds to potential AP-1 cis-elements of hSERTp2. Nuclear extracts from control (untreated) or EGF-treated (10 ng/ml, 24 h) Caco-2 cells were incubated with DIG-labeled distal AP-1 cis-element of the hSERTp2. DNA-protein complexes in response to EGF treatment were competed by excess of unlabeled probe (lane 4). Excess of cold oligonucleotides representing the AP-1 consensus sequence (125-fold excess, lane 5; 150-fold excess, lane 6) competed out the increase in binding observed in EGF-treated nuclear extracts (lane 3). Addition of c-jun antibody abolished the increase in binding in response to EGF treatment (lane 7). These data indicate that c-jun binds to the potential AP-1 cis-elements of hSERTp2. A representative blot is shown.