Recombinant Mouse Antibody (Fab408) is capable of binding to AChE.
Figure 1 SDS-PAGE analysis of AChE antibody Fab408.
Electrophoresis patterns obtained by SDS-PAGE in non-reducing conditions (12.5% PhastGel, left) and native-PAGE (7.5% PhastGel, center) with migration from the cathode (top) toward the anode (bottom), and by isoelectric focusing (pI 3-9 PhastGel, right). The three Fabs are more homogenous in mass than in charge, a feature that likely result from variations in the C-terminus generated by papaine cleavage of the CH chain; yet, all isoforms bind EeAChE equally, as verified by a native-PAGE mobility shift assay (not shown). The neutral average pI of Fab408 and cationic average pIs of Fab403 and Fab410 are evident.
Bourne, Y., Renault, L., Essono, S., Mondielli, G., Lamourette, P., Boquet, D., ... & Marchot, P. (2013). Molecular characterization of monoclonal antibodies that inhibit acetylcholinesterase by targeting the peripheral site and backdoor region. PLoS One, 8(10), e77226.
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• Confirmed specificity
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