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. 2000 Mar 6;148(5):1047–1062. doi: 10.1083/jcb.148.5.1047

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© 2000 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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SdpII-specific antibodies identify different splice variants of the protein in a number of different cell lines and tissues. a, Lysates from HeLa cells transfected with the full-length proteins SdpI, SdpII-s, SdpII-l, or vector alone were separated on SDS-PAGE, transferred to nitrocellulose, and probed with either tag-specific antibodies (anti-Xpress) or affinity-purified antibodies raised against SdpI (antiserum 2703) and SdpII (antisera P339 and 3685). b, Postnuclear supernatants from various rat tissues and cellular extracts were resolved by SDS-PAGE, transferred to nitrocellulose, and subjected to Western blot analysis. SdpII-specific antibodies recognized a 65-kD band predominantly in the PC12 cell line and heart, and, less prominent, in testis and additional cellular extracts. In addition, a protein of an electrophoretic mobility of 52 kD was detected in all tissues analyzed, which appears to be enriched in brain, kidney, testis, and skeletal muscle.