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. 2009 Mar 12;37(9):2854–2866. doi: 10.1093/nar/gkp155

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© 2009 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Expression and purification of recombinant human Pol δ. (A) Schematic structures of expression plasmids for Pol δ. (B) Purification profile of Pol δ. Each fraction was electrophoresed in an SDS 4–12% polyacrylamide gel and stained with Coomassie Brilliant Blue. Lane 1, load to a Ni²⁺-Sepharose column; lane 2, flow-through of the Ni²⁺-Sepharose column; lane 3, a wash fraction with 1 M NaCl-containing buffer; lane 4, a wash fraction with 100 mM imidazole-containing buffer; lane 5, eluate from the Ni²⁺-Sepharose column with 300 mM imidazole-containing buffer; lane 6, flow-through of an SP-Sepharose column, lane 7, a wash fraction with 200 mM NaCl-containing buffer; lane 8, a wash fraction with 500 mM NaCl-containing buffer; lane 9, eluate from the SP column with 1 M NaCl-containing buffer. (C) Purified Pol δ wild-type (wt) and exonuclease mutant enzymes. (D) Purified recombinant human RFC visualized with Coomassie staining.