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. 2015 May 12;16:28. doi: 10.1186/s12865-015-0091-2

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© Rao et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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EI-03 binds directly to E-FABP. (A) A coomasie-stained gel depicting the purity of E-recombinant FABP protein (15.3 kDa) used in thermal shift assays. (B) Normalized melting curves depicting enhanced thermal stability of E-FABP in the presence of EI-03, as is evident by a Tm shift of 1.0-2.1°C when compared to EI-06 or DMSO control. The data shown are representative of three independent experiments.