Fig. 1: In vitro properties of the anti-latent TGF-β1 antibody SOF10.
From: Selective blockade of latent TGF-β1 activation suppresses tissue fibrosis with good safety
a Lead identification flow. b The affinities of SOF10 for latent TGF-β1 from different species were determined by surface plasmon resonance. KD=equilibrium dissociation constant. The data in the table are presented as the mean ± standard deviation (N = 3). c The binding selectivity of SOF10 for different isoforms was determined by surface plasmon resonance. Biacore sensorgrams showing the binding of 0, 25, and 100 nM SOF10 (red, green, and blue, respectively) to human latent TGF-β1, latent TGF-β2, latent TGF-β3, mature TGF-β1, mature TGF-β2, and mature TGF-β3 are shown. d The inhibitory effect of SOF10 on protease-mediated latent TGF-β1 activation was evaluated via quantification of mature TGF-β1 release by ELISA. The data are reported as the means ± SDs. ***P < 0.001 vs. treatment with control IgG (N = 3). e Integrin αvβ6-mediated latent TGF-β1 activation was evaluated by coculturing HEK-BlueTM TGF-β reporter cells and Detroit562 cells, which endogenously express integrin αvβ6 and latent TGF-β1. TGF-β activity was measured with the SEAP reporter gene system and normalized to that observed in the absence of antibodies (considered 100%). The data are presented as the means ± SDs (N = 3). f Integrin αvβ8-mediated latent TGF-β1 activation was evaluated by coculturing HEK-BlueTM TGF-β reporter cells and LC-1 sq cells, which endogenously express integrin αvβ8 and latent TGF-β1. TGF-β activity was measured with the SEAP reporter gene system and normalized to that observed in the absence of antibodies (considered 100%). The data are presented as the means ± SDs (N = 3).
