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. Author manuscript; available in PMC: 2010 May 1.
Published in final edited form as: Arch Biochem Biophys. 2009 May 1;485(1):16–23. doi: 10.1016/j.abb.2009.01.014

Figure 3.

Figure 3

The CPAF mutants used in this study. A) The various CPAF mutants were generated as GST fusion proteins. Cleavage of full-length CPAF into CPAFn and CPAFc occurs at residue 283. B) The GST-CPAF fusion proteins were purified on beads and were loaded into a SDS PAGE gel in varying amounts as indicated by the bead volume at the top of the figure. After the proteins are separated via electrophoresis, the gels were stained with the Coommassie blue dye. After destaining, the quality and quantity of the fusion proteins were inspected and compared between different samples. The protein band image was acquired using a dried gel.