Fig. 1 | Nature Communications
Laminin binds promiscuously to GFs and chemokines. a Binding of multiple isoforms of full-length laminin (–111, –211, –332, –411, –421, –511, and –521) to GFs and CXCL chemokines were measured by ELISA. A450 nm represents absorbance at 450 nm. BSA-coated wells served as negative controls (n = 4, mean ± SEM). Signals greater than 0.1 (gray box) are considered to be significant. b Affinities (KD values are shown) of full-length laminin against VEGF-A165, PlGF-2, and PDGF-BB were measured by SPR. A SPR chip was functionalized with laminin-521 (~2000 resonance units (RU)), and each GF was flown over the chip at indicated concentrations. Curves represent the specific responses (in RU) to laminin obtained. Experimental curves were fitted with Langmuir binding kinetics. Binding kinetics values [dissociation constants (KD) and rate constants (Kon and Koff)] determined from the fitted curves are shown. Two experimental replicates