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. 2011 Oct 21;286(51):43717–43725. doi: 10.1074/jbc.M111.292755

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 1. — Immunoprecipitation of DHPR, JP1, and JP2 from solubilized rabbit skeletal muscle and HEK293-T microsomes. A, 100 μg of proteins solubilized from rabbit skeletal muscle microsomes (M) were immunoprecipitated (ip) with antibodies against JP1, RyR (34C), caveolin-3 (Cav3), α1s-DHPR (DHPR), and a non-correlated control antibody (CT). After gel electrophoresis, proteins were transferred to a nylon membrane and incubated with anti-JP1 antibody. B, 100 μg of proteins solubilized from skeletal muscle microsomes were immunoprecipitated with antibodies against JP1, RyR, caveolin-3, and α1s-DHPR and a non-correlated control antibody. After gel electrophoresis, proteins were transferred to a nylon membrane and incubated with an antibody against α1s-DHPR. C, 100 μg of proteins solubilized from rabbit skeletal muscle microsomes were immunoprecipitated with antibodies against JP2, α1s-DHPR, and a non-correlated control antibody. After gel electrophoresis, proteins were transferred to a nylon membrane and incubated with anti-JP2 antibody. D, solubilized proteins from HEK293-T cells transfected with pEGFP-α1s-DHPR, pEGFP-β1a-DHPR, and pCDNA-JP1 were immunoprecipitated with antibodies against α1s-DHPR, JP1, and a non-correlated control antibody. Proteins were separated by gel electrophoresis, transferred to a nylon membrane, and incubated with an antibody against DHPR. E, solubilized proteins from HEK293-T cells transfected with pEGFP-α1s-DHPR, pEGFP-β1a-DHPR, and pCDNA-JP1 were immunoprecipitated with antibodies against α1s-DHPR, JP1, and a non-correlated control antibody. Proteins were separated by gel electrophoresis, transferred to a nylon membrane, and incubated with an anti-JP1 antibody.