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. 2006 Aug 14;174(4):569–580. doi: 10.1083/jcb.200602043

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Copyright © 2006, The Rockefeller University Press

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Figure 8. — HB-EGF binds the N-syndecan ectodomain with a similar affinity as HB-GAM. (A and B) In an ELISA assay, different concentrations of the IgG-tagged N-syndecan ectodomain (ENS) were added on HB-EGF– or HB-GAM–precoated 96-well plates, and the amount of the specific binding of N-syndecan ectodomain after incubation was estimated for both proteins. HB-GAM and HB-EGF bind the N-syndecan ectodomain with similar affinity. (C and D) In the competition assay, biotinylated HB-GAM or HB-EGF were bound to the immobilized N-syndecan ectodomain. A gradient of unbiotinylated HB-GAM or HB-EGF was used to compete with biotinylated protein in N-syndecan ectodomain binding. HB-GAM inhibits HB-EGF binding strongly. HB-EGF also competes with HB-GAM binding to the N-syndecan ectodomain, although with somewhat lesser efficacy. Error bars represent the SEM of independent experiments.