Extended Data Fig. 2: HMB-001 has the highest affinity for both FVIIa and sTLT-1.
BiAbs (0.5–4 nM and as indicated on individual sensorgrams) were captured on immobilized anti-human IgG antibodies and binding of FVIIa (0–4 nM) (a) and sTLT-1 (0–60 mM) (b) was assessed with SPR at 25 °C and pH 7.4 (n = 2). Binding data were fitted to a Langmuir 1:1 binding model to determine association and dissociation rates as well as equilibrium dissociation constants (KD). Coloured lines represent binding data and solid black lines represent the fit of the data. Representative sensorgrams from one run are shown below. BiAbs, bispecific antibodies; IgG, immunoglobulin G, FVIIa, recombinant factor VIIa; SPR, surface plasmon resonance; sTLT-1, soluble extracellular fragment of TREM-like transcript 1.