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. 1999 Dec 27;147(7):1391–1398. doi: 10.1083/jcb.147.7.1391

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© 1999 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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MIBP is predominantly expressed in skeletal muscle. (A) Immunoblot with mAb 5B4.7. Each lane was loaded 10 ng of recombinant proteins. Lane 1, MBP; lane 2, MBP–MIBP; lane 3, His–MIBP; lanes 4–7, His fusion proteins containing partial MIBP sequences as indicated in the figure; and lane 8, His fusion protein containing an irrelevant protein Nck2. (B) Immunoblot showing mAb 5B4.7 specifically recognizes mammalian MIBP. Equal amounts of C2C12 cell extracts (5 μg/lane) were probed with 3.3 nM irrelevant control mouse IgG (lane 1), 3.3 nM mAb 5B4.7 (lane 2), 3.3 nM mAb 5B4.7 preincubated with 1.65 nM (lane 3), 3.3 nM (lane 4), 16.5 nM (lane 5), or 33 nM (lane 6) MBP–MIBP, or 3.3 nM mAb 5B4.7 preincubated 33 nM MBP (lane 7). Note that binding of mAb 5B4.7 to mammalian MIBP was blocked by an excess amount of MBP–MIBP (lanes 5 and 6) but not of MBP (lane 7). (C) MIBP is predominantly expressed in skeletal muscle. Equal amounts (15 μg/lane) of human fetal tissues were analyzed by immunoblotting with mAb 5B4.7.