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. 2014 Jul 30;15(1):638. doi: 10.1186/1471-2164-15-638

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© Sharma et al.; licensee BioMed Central Ltd. 2014

This article is published under license to BioMed Central Ltd. 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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SDS-PAGE profile of buffalo HOXC11 protein. A) SDS-PAGE (15%) for HOXC11 protein showing its resolved chromatographic fractions. M denotes marker, L: load, FT: flow through, W: wash, Gr: gradient, Ni: Ni-NTA fraction and Di: dialyzed protein. B) SDS-PAGE of HOXC11 protein; lane 1 represents uninduced; lane 2, induced and lane 3, marker. C) Validation of purified buffalo HOXC11 protein by Western blot with anti-His and HRP conjugated anti-rabbit IgGs used as primary and secondary antibodies, respectively. Lane 1, represents uninduced; lane 2, induced and lane 3, marker. D) Tryptophan emission spectra. Fluorescence of refolded protein was scanned at 280 nm excitation wavelength and 300–400 nm emission wavelength.