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. 2015 Mar 26;8:12. doi: 10.1186/s13048-015-0148-0

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© Ndiaye 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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Overexpression analysis of LAPTM4B in HEK cells. LAPTM4B was cloned into the his-tag pQE2 vector and used to transfect HEK cells. Proteins were extracted and subjected to immunoblotting using the anti-bovine (LA)₂-LAPTM4B polyclonal antibody (panel A) or a commercially available anti-LAPTM4B antibody (panel B). Two proteins of 26.3 and 31.5 kDa were observed with both antibodies. His-tag LAPTM4B proteins produced by HEK cells were purified by affinity chromatography and subjected to immunoblotting using a bovine ubiquitin antibody that only recognized the 31.5 kDa LAPTM4B form (panel C).