Data from: Liquid chromatography-mass spectrometry (LC-MS) data of a multi-epitope peptibody with bFGF/VEGFA

<p><span><span><span><span><span><span><span><span><span><span><span>The <span><span><span>protein </span></span></span><span><span><span>primary </span></span></span><span><span><span>structure of the recombinant </span></span></span>Peptibody were investigated systematically by Liquid Chromatography-Mass Spectrometry (LC-MS)<span><span><span>. T</span></span></span><span><span>he 15 amino acids of N-terminal were </span></span>Met-Gln-Lys-Arg-Lys-Arg-Lys-Lys-Ser-Arg-Tyr-Lys-Ser-Gly-Gly and <span><span>the C-terminal was Lys (K</span></span><span><span>), the same as</span></span> the theoretical sequence. <span><span>With more </span></span><a><span class="15"><span>protease</span></span></a><span><span>s, the whole sequence was detected at the coverage of </span></span>trypsin 87.5%, <span><span>c</span></span><span><span>hymotrypsin</span></span> 75.3% and <span><span>Glu-C</span></span> 76.7%<span><span>. The </span></span>peptide-mapping could be used as an valuable standard to certify the complete expression and primary structure of Peptibody. The pI and MW were 8.93 and 37.415 kDa, within the errors allowed . The binding specificity after production were analyzed using anti-VEGFA and anti-His antibodies.</span></span></span></span></span></span></span></span></span></span></span></p>