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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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Western blot analysis of α1-subunits in WT and mutant mouse brain homogenates. (A) Proteins (100 μg/lane) were separated on 5% SDS page and immunostained with polyclonal antibody Cav1.3 α1_CT. The Cav1.3 α1 subunit was specifically detected as a 231 kDa protein at expression levels indistinguishable between WT and homozygous mutants (HA) (see Results). KO, Cav1.3^-/- negative control. (B) Same separation as in A (100 μg/lane) but detection with anti-Cav1.3α1_NT. The migration of recombinant mCav1.3_L (L) and mCav1.343_S (43S) on the same gel (not shown) and their calculated molecular mass are indicated by arrows (left). Migration of molecular mass standards as well as the brain long and short α1-subunit species are also indicated (right). An unspecific ∼120 kDa band served as loading control. One representative experiment of at least three independent experiments is shown for all panels. KO, Cav1.3^-/-; HA, Cav1.3DCRD^HA/HA, WT, wild-type littermate.