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. Author manuscript; available in PMC: 2010 Jul 1.
Published in final edited form as: Nat Chem Biol. 2009 Nov 29;6(1):22–24. doi: 10.1038/nchembio.277

Figure 2.

Figure 2

(a) RNAs binding as analyzed by gel-shift assay. Proteins were extracted from tumor, normal liver, normal colon, and colon carcinoma CT26 cells, respectively, and incubated with (γ-32P) ATP end-labeled 14-16 (left pane) or 14-8 RNA (right panel). The final products were resolved on 6% poly-acrylamide gel and visualized by autoradiography. In competitive and non-competitive binding assays, unlabeled RNAs were added at a 25-fold molar excess, respectively. The gel is representative of three experiments. (b) Coomassie blue-stained SDS-PAGE gel analyzing the aptamer 14-16-mediated target purification. Lane 1, molecular marker; lane 2, purification with control aptamer library as a control; and lane 3, purification with aptamer 14-16. (c) In vitro binding assays confirming that in vivo selected RNA 14-16 is an aptamer that binds specifically to recombinant protein p68. (d) Aptamer 14-16-mediated inhibition of p68 ATPase activity. ATP hydrolysis was measured in the absence or presence of 20 ng/μl (0.6 μM) RNA 14-16. *p < 0.05 versus library group without stimulation; #p < 0.05 versus library group with stimulation. The assay is representative of three experiments.