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  • 90
    Thermo Fisher nupage mops sds buffer kit
    Western blots of purified proteins. (A) Various ST6Gal I and ST3Gal IV purified proteins on Western blots detected by mouse anti-His, HRP-goat anti-mouse IgG with DAB staining. (B) PNGase F digested ST6Gal I (+) and undigested (−) control. Loading was ∼2 μg purified from ProCHO-AT media separated on 12% <t>NuPAGE</t> Novex Bis-Tris gels in <t>MOPS</t> buffer under reducing conditions. Marker: BenchMark His-tagged protein standard. See Table 1 for explanation of all clone names.
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    88
    Thermo Fisher 2 bis 2 hydroxyethyl amino 2 hydroxymethyl 1 3 propanediol
    Western blots of purified proteins. (A) Various ST6Gal I and ST3Gal IV purified proteins on Western blots detected by mouse anti-His, HRP-goat anti-mouse IgG with DAB staining. (B) PNGase F digested ST6Gal I (+) and undigested (−) control. Loading was ∼2 μg purified from ProCHO-AT media separated on 12% <t>NuPAGE</t> Novex Bis-Tris gels in <t>MOPS</t> buffer under reducing conditions. Marker: BenchMark His-tagged protein standard. See Table 1 for explanation of all clone names.
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    99
    Thermo Fisher bis tris gels
    Western blots of purified proteins. (A) Various ST6Gal I and ST3Gal IV purified proteins on Western blots detected by mouse anti-His, HRP-goat anti-mouse IgG with DAB staining. (B) PNGase F digested ST6Gal I (+) and undigested (−) control. Loading was ∼2 μg purified from ProCHO-AT media separated on 12% <t>NuPAGE</t> Novex Bis-Tris gels in <t>MOPS</t> buffer under reducing conditions. Marker: BenchMark His-tagged protein standard. See Table 1 for explanation of all clone names.
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    99
    Thermo Fisher bis tris gel
    SDS-PAGE analysis of viral antigen composition of <t>CVA16</t> and EV71 viral particles. CVA16 P-particles (lane 1), CVA16 R-particles (lane 2), EV71 P-particles (lane 3), and EV71 R-particles (lane 4) were analyzed on a NuPAGE 4–12% <t>Birs-Tris</t> Gel.
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    Thermo Fisher nupage bis tris gel
    Western blot analysis of recombinant C2 phage expressing the fragment of CcOX1. 10 11 phage particles diluted in loading buffer were resolved on 4–12% <t>NuPAGE</t> <t>Bis-Tris</t> gel (Invitrogen) at 200 V for 45 min at room temperature and immunoblotted for detection with anti-pIII antibody. Wild-type M13 phage was used as a control. Migration of the molecular mass standards as well as pIII and pIII–CcOX1 fusion protein are indicated by arrowheads.
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    Thermo Fisher bis tris nupage gels
    Western blot analysis of recombinant C2 phage expressing the fragment of CcOX1. 10 11 phage particles diluted in loading buffer were resolved on 4–12% <t>NuPAGE</t> <t>Bis-Tris</t> gel (Invitrogen) at 200 V for 45 min at room temperature and immunoblotted for detection with anti-pIII antibody. Wild-type M13 phage was used as a control. Migration of the molecular mass standards as well as pIII and pIII–CcOX1 fusion protein are indicated by arrowheads.
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    Thermo Fisher novex bis tris gels
    Western blot analysis of recombinant C2 phage expressing the fragment of CcOX1. 10 11 phage particles diluted in loading buffer were resolved on 4–12% <t>NuPAGE</t> <t>Bis-Tris</t> gel (Invitrogen) at 200 V for 45 min at room temperature and immunoblotted for detection with anti-pIII antibody. Wild-type M13 phage was used as a control. Migration of the molecular mass standards as well as pIII and pIII–CcOX1 fusion protein are indicated by arrowheads.
    Novex Bis Tris Gels, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 356 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Thermo Fisher bis tris z00m gel
    Western blot analysis of recombinant C2 phage expressing the fragment of CcOX1. 10 11 phage particles diluted in loading buffer were resolved on 4–12% <t>NuPAGE</t> <t>Bis-Tris</t> gel (Invitrogen) at 200 V for 45 min at room temperature and immunoblotted for detection with anti-pIII antibody. Wild-type M13 phage was used as a control. Migration of the molecular mass standards as well as pIII and pIII–CcOX1 fusion protein are indicated by arrowheads.
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    99
    Thermo Fisher bis tris precast gels
    PER, TIM, and CLK are found in protein complexes containing CK2. <t>Anti-FLAG</t> immunoprecipitation (IP) from nonsonicated head extracts of flies collected at DD1. FLAG-CK2α or FLAG-CK2β was immunoprecipitated from 1 mg of total protein extracts from heads and 50% of the precipitate was subjected to Western blot analysis. We loaded 50 µg of head extracts as input controls. IgG LC indicates the immunoglobulin G light chain used for the precipitation that is well detected by the anti-mouse secondary antibody. Gray and black bars represent subjective day and subjective night, respectively. Experiments were performed at least twice. (A, Left) FLAG-CK2α was immunoprecipitated from tim > FLAG-CkIIα flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2α (FLAG) and co-IP of CK2β, TIM, PER, and CLK were visualized by immunoblotting. «*» shows an aspecific band recognized by the anti-PER antibody. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs on per + background. The time “CT10” indicates a mixed population of flies harvested at CT8 and CT12. A CB stained band in the size range of CLK is used as a loading control. TIM was run on a 3–8% <t>Tris-Acetate</t> gel. (B, Left) FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIß flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2ß (with anti-CK2ß) and co-IP of CK2α, TIM, PER, and CLK were visualized by immunoblotting. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs. A CB stained band in the size range of CLK is used as a loading control. (C) FLAG-CK2α or FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIα ( α ) flies and tim-gal4 /+ negative controls (C) in a per 0 background. co-IP of CLK was visualized by immunoblotting. Input samples and immunoprecipitates were run on the same gel for C and α. (D) Image showing PDF (green), CK2α (magenta), and CLK (blue) fluorescent immunolabeling in small PDF + LNv-s of an adult fly at ZT3. The fourth square is a composite picture of the three stainings. Single optical planes are shown taken by confocal microscopy.
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    86
    Thermo Fisher gradient bis tris gel
    PER, TIM, and CLK are found in protein complexes containing CK2. <t>Anti-FLAG</t> immunoprecipitation (IP) from nonsonicated head extracts of flies collected at DD1. FLAG-CK2α or FLAG-CK2β was immunoprecipitated from 1 mg of total protein extracts from heads and 50% of the precipitate was subjected to Western blot analysis. We loaded 50 µg of head extracts as input controls. IgG LC indicates the immunoglobulin G light chain used for the precipitation that is well detected by the anti-mouse secondary antibody. Gray and black bars represent subjective day and subjective night, respectively. Experiments were performed at least twice. (A, Left) FLAG-CK2α was immunoprecipitated from tim > FLAG-CkIIα flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2α (FLAG) and co-IP of CK2β, TIM, PER, and CLK were visualized by immunoblotting. «*» shows an aspecific band recognized by the anti-PER antibody. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs on per + background. The time “CT10” indicates a mixed population of flies harvested at CT8 and CT12. A CB stained band in the size range of CLK is used as a loading control. TIM was run on a 3–8% <t>Tris-Acetate</t> gel. (B, Left) FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIß flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2ß (with anti-CK2ß) and co-IP of CK2α, TIM, PER, and CLK were visualized by immunoblotting. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs. A CB stained band in the size range of CLK is used as a loading control. (C) FLAG-CK2α or FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIα ( α ) flies and tim-gal4 /+ negative controls (C) in a per 0 background. co-IP of CLK was visualized by immunoblotting. Input samples and immunoprecipitates were run on the same gel for C and α. (D) Image showing PDF (green), CK2α (magenta), and CLK (blue) fluorescent immunolabeling in small PDF + LNv-s of an adult fly at ZT3. The fourth square is a composite picture of the three stainings. Single optical planes are shown taken by confocal microscopy.
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    99
    Thermo Fisher bis tris mini gels
    PER, TIM, and CLK are found in protein complexes containing CK2. <t>Anti-FLAG</t> immunoprecipitation (IP) from nonsonicated head extracts of flies collected at DD1. FLAG-CK2α or FLAG-CK2β was immunoprecipitated from 1 mg of total protein extracts from heads and 50% of the precipitate was subjected to Western blot analysis. We loaded 50 µg of head extracts as input controls. IgG LC indicates the immunoglobulin G light chain used for the precipitation that is well detected by the anti-mouse secondary antibody. Gray and black bars represent subjective day and subjective night, respectively. Experiments were performed at least twice. (A, Left) FLAG-CK2α was immunoprecipitated from tim > FLAG-CkIIα flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2α (FLAG) and co-IP of CK2β, TIM, PER, and CLK were visualized by immunoblotting. «*» shows an aspecific band recognized by the anti-PER antibody. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs on per + background. The time “CT10” indicates a mixed population of flies harvested at CT8 and CT12. A CB stained band in the size range of CLK is used as a loading control. TIM was run on a 3–8% <t>Tris-Acetate</t> gel. (B, Left) FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIß flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2ß (with anti-CK2ß) and co-IP of CK2α, TIM, PER, and CLK were visualized by immunoblotting. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs. A CB stained band in the size range of CLK is used as a loading control. (C) FLAG-CK2α or FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIα ( α ) flies and tim-gal4 /+ negative controls (C) in a per 0 background. co-IP of CLK was visualized by immunoblotting. Input samples and immunoprecipitates were run on the same gel for C and α. (D) Image showing PDF (green), CK2α (magenta), and CLK (blue) fluorescent immunolabeling in small PDF + LNv-s of an adult fly at ZT3. The fourth square is a composite picture of the three stainings. Single optical planes are shown taken by confocal microscopy.
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    99
    Thermo Fisher bis tris acrylamide gels
    PER, TIM, and CLK are found in protein complexes containing CK2. <t>Anti-FLAG</t> immunoprecipitation (IP) from nonsonicated head extracts of flies collected at DD1. FLAG-CK2α or FLAG-CK2β was immunoprecipitated from 1 mg of total protein extracts from heads and 50% of the precipitate was subjected to Western blot analysis. We loaded 50 µg of head extracts as input controls. IgG LC indicates the immunoglobulin G light chain used for the precipitation that is well detected by the anti-mouse secondary antibody. Gray and black bars represent subjective day and subjective night, respectively. Experiments were performed at least twice. (A, Left) FLAG-CK2α was immunoprecipitated from tim > FLAG-CkIIα flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2α (FLAG) and co-IP of CK2β, TIM, PER, and CLK were visualized by immunoblotting. «*» shows an aspecific band recognized by the anti-PER antibody. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs on per + background. The time “CT10” indicates a mixed population of flies harvested at CT8 and CT12. A CB stained band in the size range of CLK is used as a loading control. TIM was run on a 3–8% <t>Tris-Acetate</t> gel. (B, Left) FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIß flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2ß (with anti-CK2ß) and co-IP of CK2α, TIM, PER, and CLK were visualized by immunoblotting. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs. A CB stained band in the size range of CLK is used as a loading control. (C) FLAG-CK2α or FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIα ( α ) flies and tim-gal4 /+ negative controls (C) in a per 0 background. co-IP of CLK was visualized by immunoblotting. Input samples and immunoprecipitates were run on the same gel for C and α. (D) Image showing PDF (green), CK2α (magenta), and CLK (blue) fluorescent immunolabeling in small PDF + LNv-s of an adult fly at ZT3. The fourth square is a composite picture of the three stainings. Single optical planes are shown taken by confocal microscopy.
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    82
    Thermo Fisher bis tris precasted gels
    PER, TIM, and CLK are found in protein complexes containing CK2. <t>Anti-FLAG</t> immunoprecipitation (IP) from nonsonicated head extracts of flies collected at DD1. FLAG-CK2α or FLAG-CK2β was immunoprecipitated from 1 mg of total protein extracts from heads and 50% of the precipitate was subjected to Western blot analysis. We loaded 50 µg of head extracts as input controls. IgG LC indicates the immunoglobulin G light chain used for the precipitation that is well detected by the anti-mouse secondary antibody. Gray and black bars represent subjective day and subjective night, respectively. Experiments were performed at least twice. (A, Left) FLAG-CK2α was immunoprecipitated from tim > FLAG-CkIIα flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2α (FLAG) and co-IP of CK2β, TIM, PER, and CLK were visualized by immunoblotting. «*» shows an aspecific band recognized by the anti-PER antibody. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs on per + background. The time “CT10” indicates a mixed population of flies harvested at CT8 and CT12. A CB stained band in the size range of CLK is used as a loading control. TIM was run on a 3–8% <t>Tris-Acetate</t> gel. (B, Left) FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIß flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2ß (with anti-CK2ß) and co-IP of CK2α, TIM, PER, and CLK were visualized by immunoblotting. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs. A CB stained band in the size range of CLK is used as a loading control. (C) FLAG-CK2α or FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIα ( α ) flies and tim-gal4 /+ negative controls (C) in a per 0 background. co-IP of CLK was visualized by immunoblotting. Input samples and immunoprecipitates were run on the same gel for C and α. (D) Image showing PDF (green), CK2α (magenta), and CLK (blue) fluorescent immunolabeling in small PDF + LNv-s of an adult fly at ZT3. The fourth square is a composite picture of the three stainings. Single optical planes are shown taken by confocal microscopy.
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    99
    Thermo Fisher bis tris gradient gels
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    Thermo Fisher bis tris protein gels
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    Thermo Fisher bis tris zoom gels
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    Thermo Fisher bis tris gel system
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    Thermo Fisher bis tris protein gel
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    Thermo Fisher bis tris midi gel
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    Thermo Fisher bis tris mini gel
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    Thermo Fisher bis tris novex nupage gels
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    Thermo Fisher gradient nupage bis tris gels
    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The <t>NuPAGE</t> 4–12% <t>Bis-Tris</t> gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.
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    The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% <t>Bis-Tris</t> <t>NuPage®</t> gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p
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    The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% <t>Bis-Tris</t> <t>NuPage®</t> gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p
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    The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% <t>Bis-Tris</t> <t>NuPage®</t> gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p
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    The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% <t>Bis-Tris</t> <t>NuPage®</t> gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p
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    The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% <t>Bis-Tris</t> <t>NuPage®</t> gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p
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    The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% <t>Bis-Tris</t> <t>NuPage®</t> gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p
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    The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% <t>Bis-Tris</t> <t>NuPage®</t> gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p
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    Image Search Results


    Western blots of purified proteins. (A) Various ST6Gal I and ST3Gal IV purified proteins on Western blots detected by mouse anti-His, HRP-goat anti-mouse IgG with DAB staining. (B) PNGase F digested ST6Gal I (+) and undigested (−) control. Loading was ∼2 μg purified from ProCHO-AT media separated on 12% NuPAGE Novex Bis-Tris gels in MOPS buffer under reducing conditions. Marker: BenchMark His-tagged protein standard. See Table 1 for explanation of all clone names.

    Journal: PeerJ

    Article Title: Engineering of CHO cells for the production of vertebrate recombinant sialyltransferases

    doi: 10.7717/peerj.5788

    Figure Lengend Snippet: Western blots of purified proteins. (A) Various ST6Gal I and ST3Gal IV purified proteins on Western blots detected by mouse anti-His, HRP-goat anti-mouse IgG with DAB staining. (B) PNGase F digested ST6Gal I (+) and undigested (−) control. Loading was ∼2 μg purified from ProCHO-AT media separated on 12% NuPAGE Novex Bis-Tris gels in MOPS buffer under reducing conditions. Marker: BenchMark His-tagged protein standard. See Table 1 for explanation of all clone names.

    Article Snippet: Proteins were analyzed in reducing conditions on 12% NuPAGE Novex Bis–Tris gels using the NuPAGE MOPS SDS Buffer Kit (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Western Blot, Purification, Staining, Marker

    SDS-PAGE analysis of viral antigen composition of CVA16 and EV71 viral particles. CVA16 P-particles (lane 1), CVA16 R-particles (lane 2), EV71 P-particles (lane 3), and EV71 R-particles (lane 4) were analyzed on a NuPAGE 4–12% Birs-Tris Gel.

    Journal: PLoS ONE

    Article Title: Immunological and Biochemical Characterization of Coxsackie Virus A16 Viral Particles

    doi: 10.1371/journal.pone.0049973

    Figure Lengend Snippet: SDS-PAGE analysis of viral antigen composition of CVA16 and EV71 viral particles. CVA16 P-particles (lane 1), CVA16 R-particles (lane 2), EV71 P-particles (lane 3), and EV71 R-particles (lane 4) were analyzed on a NuPAGE 4–12% Birs-Tris Gel.

    Article Snippet: SDS-PAGE analysis and Western blotting SDS-PAGE analysis of purified CVA16 virus fractions was performed in a NuPAGE 4–12% Bis-Tris Gel (Invitrogen, CA USA) according to the protocol suggested by the manufacturer.

    Techniques: SDS Page

    Western blot analysis of reactivity of enterovirus antigens with mouse anti-sera raised against formalin-inactivated CVA16 particles. R-particles derived from CVA16 and EV71 were separated on a NuPAGE 4–12% Bis-Tris Gel and analyzed using different antibodies: ( A ) anti-sera generated from formalin-inactivated CVA16 P-particles; ( B ) anti-sera generated from formalin-inactivated CVA16 R-particles; and ( C ) EV71-specific monoclonal antibody MAb N1.

    Journal: PLoS ONE

    Article Title: Immunological and Biochemical Characterization of Coxsackie Virus A16 Viral Particles

    doi: 10.1371/journal.pone.0049973

    Figure Lengend Snippet: Western blot analysis of reactivity of enterovirus antigens with mouse anti-sera raised against formalin-inactivated CVA16 particles. R-particles derived from CVA16 and EV71 were separated on a NuPAGE 4–12% Bis-Tris Gel and analyzed using different antibodies: ( A ) anti-sera generated from formalin-inactivated CVA16 P-particles; ( B ) anti-sera generated from formalin-inactivated CVA16 R-particles; and ( C ) EV71-specific monoclonal antibody MAb N1.

    Article Snippet: SDS-PAGE analysis and Western blotting SDS-PAGE analysis of purified CVA16 virus fractions was performed in a NuPAGE 4–12% Bis-Tris Gel (Invitrogen, CA USA) according to the protocol suggested by the manufacturer.

    Techniques: Western Blot, Derivative Assay, Generated

    Western blot analysis of recombinant C2 phage expressing the fragment of CcOX1. 10 11 phage particles diluted in loading buffer were resolved on 4–12% NuPAGE Bis-Tris gel (Invitrogen) at 200 V for 45 min at room temperature and immunoblotted for detection with anti-pIII antibody. Wild-type M13 phage was used as a control. Migration of the molecular mass standards as well as pIII and pIII–CcOX1 fusion protein are indicated by arrowheads.

    Journal: PLoS ONE

    Article Title: Amyloid-? Peptide Binds to Cytochrome C Oxidase Subunit 1

    doi: 10.1371/journal.pone.0042344

    Figure Lengend Snippet: Western blot analysis of recombinant C2 phage expressing the fragment of CcOX1. 10 11 phage particles diluted in loading buffer were resolved on 4–12% NuPAGE Bis-Tris gel (Invitrogen) at 200 V for 45 min at room temperature and immunoblotted for detection with anti-pIII antibody. Wild-type M13 phage was used as a control. Migration of the molecular mass standards as well as pIII and pIII–CcOX1 fusion protein are indicated by arrowheads.

    Article Snippet: 1011 phage particles diluted in 16 µl of loading buffer were boiled 5 minutes and separated on 4–12% NuPAGE Bis-Tris gel (Invitrogen) at 200 V for 45 min at room temperature as recommended by manufacturer.

    Techniques: Western Blot, Recombinant, Expressing, Migration

    PER, TIM, and CLK are found in protein complexes containing CK2. Anti-FLAG immunoprecipitation (IP) from nonsonicated head extracts of flies collected at DD1. FLAG-CK2α or FLAG-CK2β was immunoprecipitated from 1 mg of total protein extracts from heads and 50% of the precipitate was subjected to Western blot analysis. We loaded 50 µg of head extracts as input controls. IgG LC indicates the immunoglobulin G light chain used for the precipitation that is well detected by the anti-mouse secondary antibody. Gray and black bars represent subjective day and subjective night, respectively. Experiments were performed at least twice. (A, Left) FLAG-CK2α was immunoprecipitated from tim > FLAG-CkIIα flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2α (FLAG) and co-IP of CK2β, TIM, PER, and CLK were visualized by immunoblotting. «*» shows an aspecific band recognized by the anti-PER antibody. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs on per + background. The time “CT10” indicates a mixed population of flies harvested at CT8 and CT12. A CB stained band in the size range of CLK is used as a loading control. TIM was run on a 3–8% Tris-Acetate gel. (B, Left) FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIß flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2ß (with anti-CK2ß) and co-IP of CK2α, TIM, PER, and CLK were visualized by immunoblotting. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs. A CB stained band in the size range of CLK is used as a loading control. (C) FLAG-CK2α or FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIα ( α ) flies and tim-gal4 /+ negative controls (C) in a per 0 background. co-IP of CLK was visualized by immunoblotting. Input samples and immunoprecipitates were run on the same gel for C and α. (D) Image showing PDF (green), CK2α (magenta), and CLK (blue) fluorescent immunolabeling in small PDF + LNv-s of an adult fly at ZT3. The fourth square is a composite picture of the three stainings. Single optical planes are shown taken by confocal microscopy.

    Journal: PLoS Biology

    Article Title: The CK2 Kinase Stabilizes CLOCK and Represses Its Activity in the Drosophila Circadian Oscillator

    doi: 10.1371/journal.pbio.1001645

    Figure Lengend Snippet: PER, TIM, and CLK are found in protein complexes containing CK2. Anti-FLAG immunoprecipitation (IP) from nonsonicated head extracts of flies collected at DD1. FLAG-CK2α or FLAG-CK2β was immunoprecipitated from 1 mg of total protein extracts from heads and 50% of the precipitate was subjected to Western blot analysis. We loaded 50 µg of head extracts as input controls. IgG LC indicates the immunoglobulin G light chain used for the precipitation that is well detected by the anti-mouse secondary antibody. Gray and black bars represent subjective day and subjective night, respectively. Experiments were performed at least twice. (A, Left) FLAG-CK2α was immunoprecipitated from tim > FLAG-CkIIα flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2α (FLAG) and co-IP of CK2β, TIM, PER, and CLK were visualized by immunoblotting. «*» shows an aspecific band recognized by the anti-PER antibody. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs on per + background. The time “CT10” indicates a mixed population of flies harvested at CT8 and CT12. A CB stained band in the size range of CLK is used as a loading control. TIM was run on a 3–8% Tris-Acetate gel. (B, Left) FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIß flies and tim-gal4 /+ negative controls (control) in a per + background. IP of CK2ß (with anti-CK2ß) and co-IP of CK2α, TIM, PER, and CLK were visualized by immunoblotting. (Right) TIM, PER, and CLK immunoblots of the corresponding inputs. A CB stained band in the size range of CLK is used as a loading control. (C) FLAG-CK2α or FLAG-CK2β was immunoprecipitated from tim > FLAG-CkIIα ( α ) flies and tim-gal4 /+ negative controls (C) in a per 0 background. co-IP of CLK was visualized by immunoblotting. Input samples and immunoprecipitates were run on the same gel for C and α. (D) Image showing PDF (green), CK2α (magenta), and CLK (blue) fluorescent immunolabeling in small PDF + LNv-s of an adult fly at ZT3. The fourth square is a composite picture of the three stainings. Single optical planes are shown taken by confocal microscopy.

    Article Snippet: Samples (50 µg) for FLAG, CK2α, and CK2β immunoblots were run on NuPAGE Novex 4–12% Bis-Tris precast gels (Life Technologies).

    Techniques: Immunoprecipitation, Western Blot, Co-Immunoprecipitation Assay, Staining, Immunolabeling, Confocal Microscopy

    CK2α overexpression induces CLK hyperphosphorylation in the presence of PER. (A, B) Western blot of nonsonicated head extracts from flies collected at DD1. Samples were run on 3–8% Tris-Acetate gels in order to better resolve hyperphosphorylated CLK and TIM forms. Gray and black bars represent subjective day and subjective night, respectively. At least two independent experiments were performed for each blot. (A, Top) Comparison between tim > CkIIα and tim-gal4/+ controls in a per + background, for TIM, PER, and CLK proteins. (Bottom) Two independent experiments as above were quantified for CLK abundance, and the mean values are plotted. Error bars stand for the difference of the respective values from each experiment and their mean. The value of w; tim-gal4/+ at CT0 was normalized to 100. (B) Comparison between per 0 ; tim > CkIIα and per 0 ; tim-gal4/+ controls for CLK. (C) CK2α phosphorylates CLK in vitro . (Top) Wild-type CLK was translated with a N-terminal 6-histidine fusion tag in vitro , affinity purified either in the absence or presence of PER or TIM, and subjected to phosphorylation assays by incubation with γ– 32 P-ATP either in the absence (−) or presence (+) of CK2α. Intensity of incorporated 32 P-phosphate into CLK ( 32 P) was analyzed by autoradiography and total CLK protein levels (CLK) were determined by Western blot analysis. The arrow indicates the position of phosphorylated CLK. (Bottom) Quantification of CLK-incorporated 32 P-phosphate after normalization towards total CLK protein levels. Average CLK phosphorylation from at least three experiments ± s.e.m. are shown in the figure with wild-type CLK set to 100.

    Journal: PLoS Biology

    Article Title: The CK2 Kinase Stabilizes CLOCK and Represses Its Activity in the Drosophila Circadian Oscillator

    doi: 10.1371/journal.pbio.1001645

    Figure Lengend Snippet: CK2α overexpression induces CLK hyperphosphorylation in the presence of PER. (A, B) Western blot of nonsonicated head extracts from flies collected at DD1. Samples were run on 3–8% Tris-Acetate gels in order to better resolve hyperphosphorylated CLK and TIM forms. Gray and black bars represent subjective day and subjective night, respectively. At least two independent experiments were performed for each blot. (A, Top) Comparison between tim > CkIIα and tim-gal4/+ controls in a per + background, for TIM, PER, and CLK proteins. (Bottom) Two independent experiments as above were quantified for CLK abundance, and the mean values are plotted. Error bars stand for the difference of the respective values from each experiment and their mean. The value of w; tim-gal4/+ at CT0 was normalized to 100. (B) Comparison between per 0 ; tim > CkIIα and per 0 ; tim-gal4/+ controls for CLK. (C) CK2α phosphorylates CLK in vitro . (Top) Wild-type CLK was translated with a N-terminal 6-histidine fusion tag in vitro , affinity purified either in the absence or presence of PER or TIM, and subjected to phosphorylation assays by incubation with γ– 32 P-ATP either in the absence (−) or presence (+) of CK2α. Intensity of incorporated 32 P-phosphate into CLK ( 32 P) was analyzed by autoradiography and total CLK protein levels (CLK) were determined by Western blot analysis. The arrow indicates the position of phosphorylated CLK. (Bottom) Quantification of CLK-incorporated 32 P-phosphate after normalization towards total CLK protein levels. Average CLK phosphorylation from at least three experiments ± s.e.m. are shown in the figure with wild-type CLK set to 100.

    Article Snippet: Samples (50 µg) for FLAG, CK2α, and CK2β immunoblots were run on NuPAGE Novex 4–12% Bis-Tris precast gels (Life Technologies).

    Techniques: Over Expression, Western Blot, In Vitro, Affinity Purification, Incubation, Autoradiography

    MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The NuPAGE 4–12% Bis-Tris gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.

    Journal: Molecular Biology of the Cell

    Article Title: The Mammalian Septin MSF Localizes with Microtubules and Is Required for Completion of Cytokinesis

    doi: 10.1091/mbc.E02-01-0042

    Figure Lengend Snippet: MSF and Nedd5 coimmunoprecipitate in a septin complex in interphase HeLa cells. Immunoprecipitations were performed as described in MATERIALS AND METHODS using anti-MSF (A and C) or anti-Nedd5 (B and C) antibodies and analyzed by Western blotting with the indicated antibodies (A and B) or by Coomassie blue staining (C). Samples of the starting material were also analyzed (Ly), and immunoprecipitations with nonimmune IgG provided a control. Western blots shown are representative of three independent experiments. Relative molecular weights and the position of the IgG heavy chain are indicated. In C, the identities of the protein bands were determined by Western blotting (A, B, and our unpublished results). hCDC10 was also identified by MALDI-TOF analysis of an in-gel trypsin digest of the protein band (see text). The NuPAGE 4–12% Bis-Tris gradient gels shown in C are representative of at least five independent experiments. Asterisks (*) denote the upper two MSF immunoreactive species.

    Article Snippet: Supernatants were subjected to electrophoresis on NuPAGE 4–12% Bis-Tris gradient gels (Invitrogen) according to the manufacturer's instructions and subsequently stained in Coomassie blue for 1 h, followed by destaining in 50% H2 O, 40% methanol, 10% acetic acid.

    Techniques: Western Blot, Staining

    The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% Bis-Tris NuPage® gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Soluble A? seeds are potent inducers of cerebral ?-amyloid deposition

    doi: 10.1523/JNEUROSCI.3088-11.2011

    Figure Lengend Snippet: The β-amyloid-inducing activity is partly proteinase K-resistant Brain extracts from an aged APP23 tg mouse (Tg extract), an aged non-tg mouse (Wt extract) spiked with synthetic Aβ fibrils (syn. Aβ fibrils in Wt extract; 10µM Aβ), and synthetic Aβ fibrils in PBS (syn. Aβ fibrils in PBS; 10µM) were treated with 50µg/ml proteinase K (PK) for 0min, 30min, 1h, or 2h at 37°C. ( A ) Silver staining of a 12% Bis-Tris NuPage® gel for total protein reveals the digestion of the majority of proteins in the brain extracts and of synthetic Aβ fibrils already after 30 min PK treatment. ( B ) Immunoblot analysis with an antibody specific to human Aβ (6E10) shows that Aβ in the Tg extract is largely PK-resistant for up to 2h. Aβ in the spiked Wt extract revealed some, but significantly less PK-resistance, whereas synthetic Aβ fibrils in PBS were almost completely digested by the PK treatment. ( C ) Densitometric quantification of Aβ-immunoblots after PK treatment of 5 Tg extracts [each from a different animal] and 3 independent synthetic Aβ fibril preparations are shown. Each preparation was tested at least 3 times and the mean was taken. Aβ concentration at time point 0 was designated as 100%. Indicated is the mean ± SEM. Repeated Measures 2-way ANOVA revealed a significant difference between the groups (F (2,34) = 112.2). Multiple Bonferroni post hoc tests showed significances after PK digestion for all group comparisons, *** p

    Article Snippet: Brain extracts and synthetic Aβ preparations were analyzed on NuPage® Bis-Tris mini gels using NuPage® LDS sample buffer and MES running buffer (Invitrogen, Carlsbad, CA, USA).

    Techniques: Activity Assay, Silver Staining, Western Blot, Concentration Assay