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. 2020 Sep 1;21(17):6354. doi: 10.3390/ijms21176354

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Production and characterization of human anti-hYKL-40 Fabs. (a) SDS-PAGE analysis of two human anti-hYKL-40 Fabs, H1 (Fab) and H2 (Fab), purified from periplasmic extracts of E. coli transformed with the indicated expression vectors. + and − indicate with and without the reducing reagent (β-mercaptoethanol), respectively. (b) Soluble ELISA of serially diluted H1 (Fab) and H2 (Fab) on immobilized hYKL-40 surfaces to measure their apparent affinities (EC₅₀, nM). (c) Size-exclusion chromatography analysis of H1 (Fab) and H2 (Fab). The positions of the molecular mass markers, shown as kDa, on the retention time x-axis are shown above the peaks. (d) Protein thermal shift assay of H1 (Fab) and H2 (Fab) to determine their thermal stability (T_m, °C). Fab: antigen-binding fragment; SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; M: molecular mass marker.