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. 2017 Aug 15;7:8164. doi: 10.1038/s41598-017-08212-6

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Small protein contaminants in the Sigma mSPE-7 IgE preparation are not responsible for its cytokinergic activity. (A) Analysis of the unpurified Sigma mSPE-7 IgE preparation by size-exclusion chromatography using the Superdex S200 HPLC column revealed the presence of small protein contaminants. Fractions smaller than monomeric IgE (fractions 1) were collected and pooled as small contaminants (fractions 2, also magnified in inset). (B) Although unpurified Sigma mSPE-7 IgE, in the absence of antigen, resulted in significant RBL-SX38 degranulation compared to buffer background control (black lower bar; ****P < 0.0001), the contaminants alone or in combination with 5 μg/ml recombinant SPE-7 IgE monomer, did not exhibit any cytokinergic activity (black lower bars; ns P > 0.05). Means of 3 independent experiments ± SEM are shown. Statistically significant difference to background control was determined by one-way ANOVA with Dunnett’s post-test.