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. 2016 Jan 19;6:19661. doi: 10.1038/srep19661

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The main complexes are marked with arrows. (a) Nuclear protein extracts were incubated with free probe containing the E2F1 binding site in the presence of 2.5× unlabelled probe (lane 3), 10× unlabelled probe (lane 4), 2.5× mutation probe (lane 5), 10× mutation probe (lane 6), or in the absence of any competitor (lane 2). The super-shift assay was conducted using 10 ng anti-E2F1 antibodies (lane 7). (b) Nuclear protein extracts were incubated with free probe containing the Sp1 binding site in the presence of 10× unlabelled probe (lane 3), 25× unlabelled probe (lane 4), 10× mutation probe (lane 5), 25× mutation probe (lane 6), or in the absence of any competitor (lane 2). The super-shift assay was conducted using 10 ng anti-Sp1 antibodies (lane 7). (c) Nuclear protein extracts were incubated with free probe containing the KLF15 binding site in the presence of 50× unlabelled probe (lane 3), 125× unlabelled probe (lane 4), 50× mutation probe (lane 5), 125× mutation probe (lane 6), or in the absence of any competitor (lane 2).The super-shift assay was conducted using 10 ng anti-KLF15 antibodies (lane 7). (d) Nuclear protein extracts were incubated with free probe containing the E2F4 binding site in the presence of 20× unlabelled probe (lane 3), 40× unlabelled probe (lane 4), 20× mutation probe (lane 5), 40× mutation probe (lane 6), or in the absence of any competitor (lane 2). The super-shift assay was conducted using 10 ng anti-E2F4 antibodies (lane 7).