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. 2011 Sep 8;286(44):38264–38274. doi: 10.1074/jbc.M111.277012

FIGURE 1.

FIGURE 1.

Recombinant RPL11 protein forms a stable complex with MDM2 (residues 210–437) through co-expression and co-purification from E. coli. A, scheme to purify and identify MDM2-RPL11 complexes. B–D, co-purification of the MDM2-RPL11 complexes was carried out through nickel affinity column followed by anion exchange and size exclusion chromatography. Fractions were visualized on SDS-PAGE (B and D). B, FT indicates flow-through; W indicates washout, and E indicates elution. C and D, size exclusive chromatography of RPL11 alone and MDM2-RPL11 complex. The elution profile was monitored by Coomassie staining or immunoblotting (IB) using anti-L11 antibodies. Panels a and b indicate that these two panels were obtained from two independent experiments for the MDM2-RPL11 complexes (panel a) and RPL11 alone (panel b), respectively.