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. 2023 Aug 14;13(9):302. doi: 10.1007/s13205-023-03724-7

Fig. 4.

Fig. 4

Binding affinity of rcIL-31 to soluble rcOSMRβ and a caninized mAb, 34D03. The binding affinities of rcIL-31 to rcOSMRβ and its specific mAb, 34D03 (a, c) were measured using a surface plasmon resonance (SPR) assay. Bovine serum albumin (BSA) and an mAb that does not bind to rcIL-31 were used as negative controls (b, d). All of these binding curves were built using GraphPad Prism software, and the dissociation constant KD values were determined using Biacore T200 evaluation software. Representative data are shown from three independent experiments with similar results. The values were normalized to the cell samples which were not treated with rcIL-31