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. 2013 Nov 26;6(1):204–218. doi: 10.4161/mabs.27227

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Copyright © 2014 Landes Bioscience

This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.

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graphic file with name mabs-6-204-g4.jpg — Figure 4. (A) SH313-F9 was converted into scFv-Fc, scIgG and IgG, produced in mammalian cells and tested by titration ELISA for binding to CD30. (B) Affinity maturation of SH313-F9 in the scFv format resulted in molecules with enhanced antigen binding compared with the parental scFv SH313-F9. These candidates were tested as scFv, scFv-Fc and IgG by titration ELISA for binding to CD30. (B) Affinity maturation of SH313-F9 in the scFabΔC or FabΔC formats resulted in molecules with enhanced antigen binding compared with the parental antibody. These candidates were tested as scIgG (only scFabΔC) and IgG by titration ELISA for binding to CD30. Background binding to BSA was generally very low (< 0.02) and subtracted from the shown absorption measured for CD30 binding.