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. Author manuscript; available in PMC: 2009 Feb 1.
Published in final edited form as: J Mol Cell Cardiol. 2007 Nov 12;44(2):352–360. doi: 10.1016/j.yjmcc.2007.10.023

Figure 1. Affinity Purification of FOG-2 Interacting Proteins.

Figure 1

Affinity purified glutathione-S-transferase (GST) or GST fused to the first 12 amino acids of FOG-2 (GST-FOG-2(1–12)) and was incubated with 3.6 milligrams of rat cardiocyte nuclear extract overnight at 4°C. Complexes were purified using glutathione sepharose beads, resolved by SDS-PAGE, and visualized by staining with GelCode reagent. Protein identification was performed by MALDI-TOF mass spectrometry on each visualized subunit. The * indicates a polypeptide isolated using both GST and GST-FOG-2(1–12).