mcherry immunoreactivity Search Results


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  • 99
    Vector Laboratories avidin biotin peroxidase complex abc solution
    Avidin Biotin Peroxidase Complex Abc Solution, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 1705 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Millipore a2a r
    A2a R, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 229 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    MBF Bioscience neurolucida software
    Neurolucida Software, supplied by MBF Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 5830 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Jackson Immuno normal donkey serum v v
    Normal Donkey Serum V V, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 99/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Carl Zeiss axioskop 2 epifluorescent microscope
    Axioskop 2 Epifluorescent Microscope, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 88/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    myh9  (Abcam)
    91
    Abcam myh9
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Myh9, supplied by Abcam, used in various techniques. Bioz Stars score: 91/100, based on 206 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher alexa 488 conjugated anti chicken antibodies
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Alexa 488 Conjugated Anti Chicken Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Carl Zeiss axio imager m2 microscope
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Axio Imager M2 Microscope, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 99/100, based on 3045 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    TaKaRa anti dsred antibody
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Anti Dsred Antibody, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 198 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Carl Zeiss zeiss mrc camera
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Zeiss Mrc Camera, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 90/100, based on 103 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Vector Laboratories goat anti rabbit biotinylated igg
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Goat Anti Rabbit Biotinylated Igg, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 148 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Agilent technologies streptavidin horseradish peroxidase complex
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Streptavidin Horseradish Peroxidase Complex, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 374 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Vector Laboratories biotinylated goat anti rabbit igg antibody
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Biotinylated Goat Anti Rabbit Igg Antibody, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 1489 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Agilent technologies biotinylated swine anti rabbit ig
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Biotinylated Swine Anti Rabbit Ig, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Ted Pella epon 12
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Epon 12, supplied by Ted Pella, used in various techniques. Bioz Stars score: 91/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Cell Signaling Technology Inc neuropeptide y d7y5a xp rabbit mab
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Neuropeptide Y D7y5a Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore rabbit anti th antibody
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Rabbit Anti Th Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 548 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore rabbit polyclonal anti c fos antibody
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Rabbit Polyclonal Anti C Fos Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 168 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tyrosine hydroxylase th
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Tyrosine Hydroxylase Th, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 943 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Abcam proteasome degradation
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Proteasome Degradation, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    W Nuhsbaum leica dmirb microscope
    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse <t>anti-myh9</t> antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)
    Leica Dmirb Microscope, supplied by W Nuhsbaum, used in various techniques. Bioz Stars score: 90/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse anti-myh9 antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)

    Journal: Molecular Brain

    Article Title: Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

    doi: 10.1186/s13041-018-0388-1

    Figure Lengend Snippet: Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse anti-myh9 antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + -ATPase α1 subunits but not from those overexpressing mCherry. Full length images of western blots are presented in Additional file 12 : Figure S11, Additional file 13 : Figure S12, Additional file 14 : Figure S13)

    Article Snippet: Na+ /K+ -ATPase α1 subunits could not co-immunoprecipitate myh9 expressed in HEK293 cells. (A) Immunoprecipitation of Na+ /K+ -ATPase α1 subunits expressed in HEK293 cells.

    Techniques: Recombinant, Transfection, Immunoprecipitation, Western Blot

    Recombinant myh9 co-immunoprecipitate Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with GFP (In, lane 1) or myh9 tagged with GFP in the C-terminus (In, lane 4; myh9-GFP) were precleared (PC) with mouse IgG1 antibodies ( a , lanes 2 and 5) or goat immunoglobulins (gIgG) ( b , lanes 2 and 5) prior to immunoprecipitation (IP) using mouse anti-GFP antibodies of the IgG1 isotypes ( a , lanes 3 and 6) or goat anti-GFP antibodies ( b , lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. Na + /K + -ATPase α1 immunoreactive bands in lanes 1, 4 and 6 but not in any other lanes ((i) and (iii)) indicated co-immunoprecipitation of Na + /K + -ATPase α1 subunits from HEK293 cells transfected with myh9-GFP plasmids but not from those transfected with GFP plasmids. As expected immunoprecipitation using anti-GFP antibodies led to the co-immunoprecipitation of β-actin (lane 6 in (ii) and (iv)) from HEK293 cells transfected with myh9-GFP plasmids but not from those transfected with GFP plasmids. Immunoprecipitation using goat anti-GFP antibodies ( b ) led to a cleaner co-IP of Na + /K + -ATPase α1 subunits from HEK293 cells expressing myh9-GFP. Full length images of western blots are presented in Figure Additional file 4 : Figure S3B (for part a ) and Additional file 5 : Figure S4B (for part b )

    Journal: Molecular Brain

    Article Title: Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

    doi: 10.1186/s13041-018-0388-1

    Figure Lengend Snippet: Recombinant myh9 co-immunoprecipitate Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with GFP (In, lane 1) or myh9 tagged with GFP in the C-terminus (In, lane 4; myh9-GFP) were precleared (PC) with mouse IgG1 antibodies ( a , lanes 2 and 5) or goat immunoglobulins (gIgG) ( b , lanes 2 and 5) prior to immunoprecipitation (IP) using mouse anti-GFP antibodies of the IgG1 isotypes ( a , lanes 3 and 6) or goat anti-GFP antibodies ( b , lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. Na + /K + -ATPase α1 immunoreactive bands in lanes 1, 4 and 6 but not in any other lanes ((i) and (iii)) indicated co-immunoprecipitation of Na + /K + -ATPase α1 subunits from HEK293 cells transfected with myh9-GFP plasmids but not from those transfected with GFP plasmids. As expected immunoprecipitation using anti-GFP antibodies led to the co-immunoprecipitation of β-actin (lane 6 in (ii) and (iv)) from HEK293 cells transfected with myh9-GFP plasmids but not from those transfected with GFP plasmids. Immunoprecipitation using goat anti-GFP antibodies ( b ) led to a cleaner co-IP of Na + /K + -ATPase α1 subunits from HEK293 cells expressing myh9-GFP. Full length images of western blots are presented in Figure Additional file 4 : Figure S3B (for part a ) and Additional file 5 : Figure S4B (for part b )

    Article Snippet: Na+ /K+ -ATPase α1 subunits could not co-immunoprecipitate myh9 expressed in HEK293 cells. (A) Immunoprecipitation of Na+ /K+ -ATPase α1 subunits expressed in HEK293 cells.

    Techniques: Recombinant, Transfection, Immunoprecipitation, Co-Immunoprecipitation Assay, Expressing, Western Blot

    Interaction of actin-binding-site-less (ΔABS) and tail-less (Δtail) NMHC-IIs with Na + /K + -ATPase α1 subunits expressed in HEK293 cells. a Tail-less NMHC-IIs were made by deleting the tail regions, yellow shaded, of human (h) myh9 (i.e., hMyh9 AAs: 1928–1960), human (h) myh10 isoform 2 (i.e., hMyh10.2 AAs: 1934–1976) and mouse (m) myh14 isoform 3 (i.e., mMyh14.3 AAs:1946–1992) following a conserved proline residue (bold and underlined) where the numbers indicate the position of the amino acids in the WT constructs. b Actin-binding-site-less (ΔABS) NMHC-IIs were made by deleting a 23 amino acids (AAs) segment, yellow shaded, of hMyh9 (i.e., AAs: 654–676), hMyh10.2 (i.e., AAs: 661–683) and mMyh14.3 (i.e., AAs: 674–696). For both ( a ) and ( b ) symbols below sequences indicate fully (*), strongly (:) or weakly (.) conserved residues, and the lack of a symbol indicates amino acid divergence. c The actin binding site (ABS) of human myh14. The 3-D coordinates of human myh14 was retrieved from protein data bank (PDB: 5I4E). Structural features of myh14 was visualized and analyzed using UCSF Chimera ( http://www.cgl.ucsf.edu/chimera/ ). Left panel shows the relative position of the ABS (red ribbon), nucleotide analog (adenosine diphosphate vanadate (ADP.VO4): ball and stick model) binding site and N-terminal SH3 domain (deep blue) in the motor domain of human myh14 (5I4E.pdb). The center and right panel show the relative position of the ABS (red ribbon; and ball and stick model) with respect to the position of the adenosine diphosphate vanadate (ADP.VO4) and magnesium co-factor (green ball) in the motor domain of myh14. d Tail-less (Δtail) but not actin-binding-site-less (ΔABS) myh14 co-immunoprecipitate Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of non-transfected HEK293 cells (In; 1) or HEK293 cells transiently transfected with GFP (In; 4), myh14-GFP (In; 7), myh14-ΔABS-GFP (In; 10), or myh14-Δtail-GFP (In; 13) plasmids (where the GFP tag is in their C-terminus) were precleared with rabbit IgG (PC; lanes 2, 5, 8, 11 and 14) prior to immunoprecipitation using rabbit anti-GFP antibodies (IP; lanes 3, 6, 9, 12 and 15). Loading of PC complexes in the gel preceded those of the IP complexes. Presence of Na + /K + -ATPase α1 immunoreactive bands in lanes 1, 4, 7, 9, 10, 13 and 15 and absence of any Na + /K + -ATPase α1 immunoreactive bands in lanes 2, 3, 5, 6, 8, 11, 12 and 14 (in (i)) indicated co-immunoprecipitation of Na + /K + -ATPase α1 subunits from HEK293 cells transfected with myh14-GFP or myh14-Δtail-GFP plasmids but not from non-transfected HEK293 cells or those transfected with GFP or myh14-ΔABS-GFP plasmids. While myh14-ΔABS-GFP showed almost complete loss of actin binding (indicated with double asterisk ‘*’; lane 12, panel (ii)) both myh14-GFP and myh14-Δtail-GFP co-immunoprecipitated β-actin (lane 9 and lane 15 in panel (ii) respectively). Full length images of western blots are presented in Additional file 7 : Figure S6 B

    Journal: Molecular Brain

    Article Title: Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

    doi: 10.1186/s13041-018-0388-1

    Figure Lengend Snippet: Interaction of actin-binding-site-less (ΔABS) and tail-less (Δtail) NMHC-IIs with Na + /K + -ATPase α1 subunits expressed in HEK293 cells. a Tail-less NMHC-IIs were made by deleting the tail regions, yellow shaded, of human (h) myh9 (i.e., hMyh9 AAs: 1928–1960), human (h) myh10 isoform 2 (i.e., hMyh10.2 AAs: 1934–1976) and mouse (m) myh14 isoform 3 (i.e., mMyh14.3 AAs:1946–1992) following a conserved proline residue (bold and underlined) where the numbers indicate the position of the amino acids in the WT constructs. b Actin-binding-site-less (ΔABS) NMHC-IIs were made by deleting a 23 amino acids (AAs) segment, yellow shaded, of hMyh9 (i.e., AAs: 654–676), hMyh10.2 (i.e., AAs: 661–683) and mMyh14.3 (i.e., AAs: 674–696). For both ( a ) and ( b ) symbols below sequences indicate fully (*), strongly (:) or weakly (.) conserved residues, and the lack of a symbol indicates amino acid divergence. c The actin binding site (ABS) of human myh14. The 3-D coordinates of human myh14 was retrieved from protein data bank (PDB: 5I4E). Structural features of myh14 was visualized and analyzed using UCSF Chimera ( http://www.cgl.ucsf.edu/chimera/ ). Left panel shows the relative position of the ABS (red ribbon), nucleotide analog (adenosine diphosphate vanadate (ADP.VO4): ball and stick model) binding site and N-terminal SH3 domain (deep blue) in the motor domain of human myh14 (5I4E.pdb). The center and right panel show the relative position of the ABS (red ribbon; and ball and stick model) with respect to the position of the adenosine diphosphate vanadate (ADP.VO4) and magnesium co-factor (green ball) in the motor domain of myh14. d Tail-less (Δtail) but not actin-binding-site-less (ΔABS) myh14 co-immunoprecipitate Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of non-transfected HEK293 cells (In; 1) or HEK293 cells transiently transfected with GFP (In; 4), myh14-GFP (In; 7), myh14-ΔABS-GFP (In; 10), or myh14-Δtail-GFP (In; 13) plasmids (where the GFP tag is in their C-terminus) were precleared with rabbit IgG (PC; lanes 2, 5, 8, 11 and 14) prior to immunoprecipitation using rabbit anti-GFP antibodies (IP; lanes 3, 6, 9, 12 and 15). Loading of PC complexes in the gel preceded those of the IP complexes. Presence of Na + /K + -ATPase α1 immunoreactive bands in lanes 1, 4, 7, 9, 10, 13 and 15 and absence of any Na + /K + -ATPase α1 immunoreactive bands in lanes 2, 3, 5, 6, 8, 11, 12 and 14 (in (i)) indicated co-immunoprecipitation of Na + /K + -ATPase α1 subunits from HEK293 cells transfected with myh14-GFP or myh14-Δtail-GFP plasmids but not from non-transfected HEK293 cells or those transfected with GFP or myh14-ΔABS-GFP plasmids. While myh14-ΔABS-GFP showed almost complete loss of actin binding (indicated with double asterisk ‘*’; lane 12, panel (ii)) both myh14-GFP and myh14-Δtail-GFP co-immunoprecipitated β-actin (lane 9 and lane 15 in panel (ii) respectively). Full length images of western blots are presented in Additional file 7 : Figure S6 B

    Article Snippet: Na+ /K+ -ATPase α1 subunits could not co-immunoprecipitate myh9 expressed in HEK293 cells. (A) Immunoprecipitation of Na+ /K+ -ATPase α1 subunits expressed in HEK293 cells.

    Techniques: Binding Assay, Atomic Absorption Spectroscopy, Construct, Transfection, Immunoprecipitation, Western Blot

    Interaction of multiple myosins with Na + /K + -ATPase α1 subunits expressed in rat brain. WT adult rat brain lysates (In, lane 1 in a and b ) were precleared (PC) with indicated immunoglobulin isotypes (PC; lane2 = mIgG2b, lane 6 = rIgG and lane 9 = mIgG1) prior to immunoprecipitation (IP) using indicated antibodies (IP; lane 3 = myh9, lane 4 = myh10, lane 5 = KIF5B, lane 7 = Myh14, lane 8 = myoVa and lane 10 = myoVI). Loading of PC complexes in the gel preceded those of the IP complexes. Na + /K + -ATPase α1 subunits (i) were co-immunoprecipitated with myh9, myh10, KIF5B, myh14, myoVa and myoVI expressed in rat brain tissues. Co-immunoprecipitation of Na + /K + -ATPase α1 subunits by KIF5B served as a positive control. All the myosins assayed co-immunoprecipitated β-actin (ii). Denatured mouse IgG-HC (i.e., lanes 2–5, 9 and 10; panel (ii)), but not those of rabbit IgG (i.e., lanes 6–8) separated from their intact immunoglobulins (that is used for PC or IP) could be seen as this section was probed with mouse anti-β-actin antibodies

    Journal: Molecular Brain

    Article Title: Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

    doi: 10.1186/s13041-018-0388-1

    Figure Lengend Snippet: Interaction of multiple myosins with Na + /K + -ATPase α1 subunits expressed in rat brain. WT adult rat brain lysates (In, lane 1 in a and b ) were precleared (PC) with indicated immunoglobulin isotypes (PC; lane2 = mIgG2b, lane 6 = rIgG and lane 9 = mIgG1) prior to immunoprecipitation (IP) using indicated antibodies (IP; lane 3 = myh9, lane 4 = myh10, lane 5 = KIF5B, lane 7 = Myh14, lane 8 = myoVa and lane 10 = myoVI). Loading of PC complexes in the gel preceded those of the IP complexes. Na + /K + -ATPase α1 subunits (i) were co-immunoprecipitated with myh9, myh10, KIF5B, myh14, myoVa and myoVI expressed in rat brain tissues. Co-immunoprecipitation of Na + /K + -ATPase α1 subunits by KIF5B served as a positive control. All the myosins assayed co-immunoprecipitated β-actin (ii). Denatured mouse IgG-HC (i.e., lanes 2–5, 9 and 10; panel (ii)), but not those of rabbit IgG (i.e., lanes 6–8) separated from their intact immunoglobulins (that is used for PC or IP) could be seen as this section was probed with mouse anti-β-actin antibodies

    Article Snippet: Na+ /K+ -ATPase α1 subunits could not co-immunoprecipitate myh9 expressed in HEK293 cells. (A) Immunoprecipitation of Na+ /K+ -ATPase α1 subunits expressed in HEK293 cells.

    Techniques: Immunoprecipitation, Positive Control

    Na + /K + -ATPase α1 subunits co-immunoprecipitate multiple myosins expressed in adult rat brain. WT adult rat brain lysates (In, lane 2 in a , b and c ) were precleared (PC) with mouse IgG1 antibodies (PC, lane 1 in a , b and c ) prior to immunoprecipitation (IP) using mouse anti-Na + /K + -ATPase α1 antibodies of the IgG1 isotypes (IP, lane 3 in a , b and c ). Loading of PC complexes in the gel preceded those of the lysate inputs (In). Na + /K + -ATPase α1 subunits co-immunoprecipitated myh9 ( a (i)), myh10 ( b , (i)), myoVa ( c (i)), β-actin ((iii) in a , b and c ) and myosin regulatory light chain (MRLC) ((iv) in a , b and c ) from rat brain. An asterisk (‘*’; (iv) in a , b and c ) indicates lack of detection of the input signal for the MRLCs. As expected anti-Na + /K + -ATPase α1 antibodies immunoprecipitated Na + /K + -ATPase α1 subunits expressed in brain tissues ((ii) in a , b and c )

    Journal: Molecular Brain

    Article Title: Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

    doi: 10.1186/s13041-018-0388-1

    Figure Lengend Snippet: Na + /K + -ATPase α1 subunits co-immunoprecipitate multiple myosins expressed in adult rat brain. WT adult rat brain lysates (In, lane 2 in a , b and c ) were precleared (PC) with mouse IgG1 antibodies (PC, lane 1 in a , b and c ) prior to immunoprecipitation (IP) using mouse anti-Na + /K + -ATPase α1 antibodies of the IgG1 isotypes (IP, lane 3 in a , b and c ). Loading of PC complexes in the gel preceded those of the lysate inputs (In). Na + /K + -ATPase α1 subunits co-immunoprecipitated myh9 ( a (i)), myh10 ( b , (i)), myoVa ( c (i)), β-actin ((iii) in a , b and c ) and myosin regulatory light chain (MRLC) ((iv) in a , b and c ) from rat brain. An asterisk (‘*’; (iv) in a , b and c ) indicates lack of detection of the input signal for the MRLCs. As expected anti-Na + /K + -ATPase α1 antibodies immunoprecipitated Na + /K + -ATPase α1 subunits expressed in brain tissues ((ii) in a , b and c )

    Article Snippet: Na+ /K+ -ATPase α1 subunits could not co-immunoprecipitate myh9 expressed in HEK293 cells. (A) Immunoprecipitation of Na+ /K+ -ATPase α1 subunits expressed in HEK293 cells.

    Techniques: Immunoprecipitation

    Interaction of non-muscle myosin heavy chains with Na + /K + -ATPase α1 subunits endogenously expressed in HEK293 cells. HEK293 cell lysates (In, lane 1 in a and b ) were precleared (PC) with mouse IgG2b (PC, lane 2 in a and b ) prior to immunoprecipitation (IP, lane 3) using antibodies for myh9 ( a ) and myh10 ( b ). Loading of PC complexes in the gel preceded those of the IP complexes. Immunoprecipitation of myh9 ( a ) and myh10 ( b ) led to the co-immunoprecipitation of Na + /K + ATPase α1 subunits ((i) in a and b ) and β-actin ((ii) in a and b ) expressed in HEK293 cells. Na + /K + -ATPase α1 and β-actin immunoreactive signals in the depleted supernatant lane (DS, lane 4 in a ) indicates that the ATPase survives the IP procedure. Denatured mouse IgG-HC and IgG-LC separated from their intact immunoglobulins (that is used for PC or IP) are seen in ( a and b ) as those blot sections were probed with mouse anti-β-actin antibodies

    Journal: Molecular Brain

    Article Title: Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

    doi: 10.1186/s13041-018-0388-1

    Figure Lengend Snippet: Interaction of non-muscle myosin heavy chains with Na + /K + -ATPase α1 subunits endogenously expressed in HEK293 cells. HEK293 cell lysates (In, lane 1 in a and b ) were precleared (PC) with mouse IgG2b (PC, lane 2 in a and b ) prior to immunoprecipitation (IP, lane 3) using antibodies for myh9 ( a ) and myh10 ( b ). Loading of PC complexes in the gel preceded those of the IP complexes. Immunoprecipitation of myh9 ( a ) and myh10 ( b ) led to the co-immunoprecipitation of Na + /K + ATPase α1 subunits ((i) in a and b ) and β-actin ((ii) in a and b ) expressed in HEK293 cells. Na + /K + -ATPase α1 and β-actin immunoreactive signals in the depleted supernatant lane (DS, lane 4 in a ) indicates that the ATPase survives the IP procedure. Denatured mouse IgG-HC and IgG-LC separated from their intact immunoglobulins (that is used for PC or IP) are seen in ( a and b ) as those blot sections were probed with mouse anti-β-actin antibodies

    Article Snippet: Na+ /K+ -ATPase α1 subunits could not co-immunoprecipitate myh9 expressed in HEK293 cells. (A) Immunoprecipitation of Na+ /K+ -ATPase α1 subunits expressed in HEK293 cells.

    Techniques: Immunoprecipitation