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. 2017 Aug 22;4:61. doi: 10.3389/fmolb.2017.00061

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Copyright © 2017 Weizman, Levin, Zaretsky, Sagi and Aharoni.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The A2 bi-specific inhibitor exhibits similar biochemical activity as the two mono-specific H3 (DR3) and pTACE inhibitors. (A) Binding of A2 to TL1A in comparison to the mono-specific H3 protein. Binding analysis was performed by ELISA using plates that were pre-coated with TL1A (see Section Materials and Methods for detailed description). (B) Inhibition of TACE by A2 in comparison to the mono-specific pTACE inhibitor. Inhibition of TACE activity was assessed using a fluorogenic peptide substrate DEVD-AMC.