Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile <i>Alvinella pompejana</i>

<table>Purification of the recombinant ApPol<svg height="9.875" id="M112" style="vertical-align:-2.29482pt" version="1.1" viewbox="0 0 7.9375 9.875" width="7.9375" xmlns="http://www.w3.org/2000/svg">
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</svg> protein. Aliquots from various steps of the purification were subjected to 10% SDS-PAGE analysis, and the proteins were visualized by staining with Coomassie Brilliant Blue. ApPol<svg height="9.875" id="M113" style="vertical-align:-2.29482pt" version="1.1" viewbox="0 0 7.9375 9.875" width="7.9375" xmlns="http://www.w3.org/2000/svg">
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<g transform="translate(72,-64.1)">
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<tspan style="font-size: 12.50px; " x="0" y="0">𝜂</tspan>
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</svg> has a molecular mass of 85 kDa. Lane 1, markers; lane 2, cell extract; lane 3, Talon eluate; lane 4, HiTrap Heparin HP eluate.</table>

Journal of Nucleic Acids

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Figure 2

Figure 2: Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile <i>Alvinella pompejana</i> 

Journal of Nucleic Acids

Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana

Figure 2