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. 2014 Mar;95(100):96–103. doi: 10.1016/j.pep.2013.11.015

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© 2013 The Authors

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig. 5 — Soluble partially purified KMO-FLAG. (A) Western blot using chemiluminescence detection, anti-FLAG M2 antibody and goat anti-mouse HRP secondary antibody, (a) soluble fraction from over-expressed KMO-12His-FLAG (57 kDa) in bacterial cells. (B) SDS-PAGE gel stained with simplyblue showing anti-FLAG conjugated protein A magnetic bead purification of KMO-12His-FLAG, (a) Cell-free extract prior to purification, (b) flowthrough proteins which did not bind to the beads, (c) first magnetic bead wash, (d) second bead wash, (e) purified KMO-12His (57 kDa) (bold arrow) eluted from the beads by TEV protease has precipitated with two contaminant E. coli proteins (indicated using arrows). (C) Cartoon illustrating the flKMO-12His-FLAG construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)