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. 2016 Oct 27;9(1):68–84. doi: 10.1080/19420862.2016.1248012

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© 2017 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 5. — Improved thermal- and storage-stability of rabbit antibodies humanized with a λcapped V_κ1-V_H3-consensus scFv framework. (A) Thermal unfolding curves of each scFv variant fitted with the Boltzmann equation to data points (n=3 ; mean ± SD) generated in a DSF assay. (B) Maintenance of scFv monomer content (% of total protein content) during 2-week storage at 37°C; data points (n=3 ) reflect mean ± SD. (C) SE-HPLC chromatograms of exemplary protein samples at the indicated concentrations and after storage at the indicated durations/temperatures; scFv monomer (*), scFv dimer (†) and buffer matrix (‡) peaks are indicated.