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. Author manuscript; available in PMC: 2009 Dec 16.
Published in final edited form as: Steroids. 2006 Dec 13;72(2):171–179. doi: 10.1016/j.steroids.2006.11.005

Fig. 3.

Fig. 3

p85α interacts more avidly with PV than with TRβ1 in the cytosolic and nuclear compartments. The thyroid extracts of 12 wild-type mice or three TRβPV/PV mice were pooled and separated into nuclear or cytosolic fractions. The purity of each fraction was monitored by the respective markers, poly ADP-ribose polymerase for the nuclear fraction and α-tubulin for the cytosolic fraction. An equal amount of the nuclear or cytosolic fraction (100 μg proteins) were each immunoprecipitated with 5 μg of monoclonal anti-TR/PV antibody J52 followed by Western blot analysis using anti-p85α antibody. Lanes are as marked. Lanes 5 – 8 show the corresponding input of the p85α protein.