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. 2015 Aug 24;9:309. doi: 10.3389/fncel.2015.00309

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Copyright © 2015 Scharinger, Eckrich, Vandael, Schönig, Koschak, Hecker, Kaur, Lee, Sah, Bartsch, Benedetti, Lieb, Schick, Singewald, Sinnegger-Brauns, Carbone, Engel and Striessnig.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Absence of smaller C-terminally–derived Cav1.3 α1 fragments in WT and Cav1.3DCRD^HA/HA brain preparations. (A) Mouse brain homogenate (100 μg of protein/lane) prepared from WT or Cav1.3DCRD^HA/HA (HA) mice were separated on 4–15% gradient SDS-PAGE and immunostained with anti-HA antibody. The blot was overexposed to also visualize less abundant smaller fragments. in separate experiments α1- associated HA-immunoreactivity could be detected with only 10% (10 μg/lane) of the protein amount used (n = 3) demonstrating the sensitivity of the assay. (B) Mouse brain membranes (100 μg of protein/lane) were analyzed as in (A). (C) Mouse brain membranes (100 μg of protein/lane) from WT or Cav1.3^-/- (KO) mice were blotted as in (B) and stained with anti-Cav1.3α1_CT antibodies. To some WT samples (33 μg/lane) a 45 kDa recombinant C-terminal control peptide was added (arrow, amounts indicated) before separation to demonstrate successful transfer and sensitive detection as a positive control for sensitivity.