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. 2017 Jul 24;7:6312. doi: 10.1038/s41598-017-06395-6

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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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Minispryn transcript and protein. (a) Northern blot showing the size and tissue distribution of the murine minispryn transcript. A single band of approximately 7 kb is only detected in heart and skeletal muscle. The blot was stripped and re-hybridized with a GAPDH probe to demonstrate the presence of mRNA in each lane. Key: B, brain; H, heart; Lu, lung; Li, liver; Ki, kidney; St, stomach; SI, small intestine; M, muscle; O, ovary; Th, thymus; Te, testes; U, uterus; PU, pregnant uterus; Pl, placenta; Sp, spleen. (b) Western blot of several mouse tissues showing that minispryn is a protein of approximately 90 kDa that is found predominantly in heart and skeletal muscle. (c) Antibody specificities were determined in heterologous cells. Lysates prepared from HEK-293T cells expressing full-length myospryn (clone 21B) and minispryn (clone 7E) were processed for immunoblotting with antibodies detecting their cognate antigen. The 819 antibody only detects minispryn in transfected cells whereas des122 only detects myospryn under the same conditions. The lysates were also immunoblotted with anti-tubulin antibodies to demonstrate similar levels of protein in each transfection. Lysates prepared from untransfected HEK-293T cells are also shown. (d) In tissue, minispryn and myospryn were immunoprecipitated from RIPA extracts of cardiac muscle using specific antibodies. Minispryn and myospryn are robustly immunoprecipitated with their cognate antisera but also co-IP with the antisera raised against the paralogous protein. Neither myospryn nor minispryn are immunoprecipitated with unrelated IgG. (e) Minispryn and myospryn similarly co-immunoprecipitate from RIPA extracts of skeletal muscle. X denotes an empty lane.