anti-mouse Search Results


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  • 99
    Thermo Fisher anti mouse antibodies
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Anti Mouse Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2811 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore anti mouse antibodies
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Anti Mouse Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 669 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    BioLegend anti mouse i ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Anti Mouse I Ab, supplied by BioLegend, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    BioLegend apc anti mouse i ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Apc Anti Mouse I Ab, supplied by BioLegend, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    BioLegend biotin anti mouse i ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Biotin Anti Mouse I Ab, supplied by BioLegend, used in various techniques. Bioz Stars score: 88/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    BioLegend fitc anti mouse i ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Fitc Anti Mouse I Ab, supplied by BioLegend, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    BioLegend pe cy7 anti mouse i ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Pe Cy7 Anti Mouse I Ab, supplied by BioLegend, used in various techniques. Bioz Stars score: 94/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    BioLegend mouse purified anti mouse i ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Mouse Purified Anti Mouse I Ab, supplied by BioLegend, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Pharmingen anti mouse fc ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Anti Mouse Fc Ab, supplied by Pharmingen, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Becton Dickinson anti mouse i ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Anti Mouse I Ab, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 88/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher anti mouse ifnar1 ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Anti Mouse Ifnar1 Ab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Becton Dickinson anti mouse phosphocd3ξ ab
    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or <t>anti–mouse</t> antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.
    Anti Mouse Phosphocd3ξ Ab, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Jackson Immuno anti mouse ab s
    Immunoprecipitation of myristoylated calmyrin and localization of calmyrin to the membrane fraction. (A) Fluorography of myristoylated proteins immunoprecipitated with rabbit  anti-calmyrin from HeLa cells after transfection with N-myc  calmyrin (lane 1 and 2), C-myc calmyrin (lane 3 and 4), or wild-type calmyrin (lane 5 and 6) and 24 h incubation with  3 H-myristic  acid. The cell lysates (L) and immunoprecipitated (IP) samples  are shown. The myristoylated calmyrin band is present in lanes 4  and 6 (indicated by the arrows), but absent from lane 2. The  lower panel shows an immunoblot of the supernatants (S) and  immunoprecipitants (IP) of these same transfected cell lysates to  confirm the expression level and successful immunoprecipitation  of calmyrin. (B) Immunoblotting of calmyrin-expressing HeLa  cell lysates for lamins A and C (68 and 66 kD) and calmyrin (22  kD) after fractionation in the absence (−) of detergent (lanes 1  and 2) or in the presence (+) of 1% Triton X-100 (lane 3 and 4)  into a soluble supernatant (S) and an insoluble pellet (P). The  lower panel shows the identical fractionation of endogenous  calmyrin in mouse kidney primary cell culture.
    Anti Mouse Ab S, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    GE Healthcare anti mouse secondary antibody
    Immunoprecipitation of myristoylated calmyrin and localization of calmyrin to the membrane fraction. (A) Fluorography of myristoylated proteins immunoprecipitated with rabbit  anti-calmyrin from HeLa cells after transfection with N-myc  calmyrin (lane 1 and 2), C-myc calmyrin (lane 3 and 4), or wild-type calmyrin (lane 5 and 6) and 24 h incubation with  3 H-myristic  acid. The cell lysates (L) and immunoprecipitated (IP) samples  are shown. The myristoylated calmyrin band is present in lanes 4  and 6 (indicated by the arrows), but absent from lane 2. The  lower panel shows an immunoblot of the supernatants (S) and  immunoprecipitants (IP) of these same transfected cell lysates to  confirm the expression level and successful immunoprecipitation  of calmyrin. (B) Immunoblotting of calmyrin-expressing HeLa  cell lysates for lamins A and C (68 and 66 kD) and calmyrin (22  kD) after fractionation in the absence (−) of detergent (lanes 1  and 2) or in the presence (+) of 1% Triton X-100 (lane 3 and 4)  into a soluble supernatant (S) and an insoluble pellet (P). The  lower panel shows the identical fractionation of endogenous  calmyrin in mouse kidney primary cell culture.
    Anti Mouse Secondary Antibody, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 984 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Becton Dickinson anti mouse st2 ab
    Immunoprecipitation of myristoylated calmyrin and localization of calmyrin to the membrane fraction. (A) Fluorography of myristoylated proteins immunoprecipitated with rabbit  anti-calmyrin from HeLa cells after transfection with N-myc  calmyrin (lane 1 and 2), C-myc calmyrin (lane 3 and 4), or wild-type calmyrin (lane 5 and 6) and 24 h incubation with  3 H-myristic  acid. The cell lysates (L) and immunoprecipitated (IP) samples  are shown. The myristoylated calmyrin band is present in lanes 4  and 6 (indicated by the arrows), but absent from lane 2. The  lower panel shows an immunoblot of the supernatants (S) and  immunoprecipitants (IP) of these same transfected cell lysates to  confirm the expression level and successful immunoprecipitation  of calmyrin. (B) Immunoblotting of calmyrin-expressing HeLa  cell lysates for lamins A and C (68 and 66 kD) and calmyrin (22  kD) after fractionation in the absence (−) of detergent (lanes 1  and 2) or in the presence (+) of 1% Triton X-100 (lane 3 and 4)  into a soluble supernatant (S) and an insoluble pellet (P). The  lower panel shows the identical fractionation of endogenous  calmyrin in mouse kidney primary cell culture.
    Anti Mouse St2 Ab, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Cell Signaling Technology Inc anti mouse gli1 ab
    <t>GLI1</t> protein levels are unchanged following S6K1 knockdown. Western blot analysis of GLI1 and S6K1 protein expression in SK-N-AS cells, following siRNA-mediated knockdown of GLI1 and S6K1. Note the reduction of the GLI1 and S6K1 protein bands by the siRNAs targeting GLI1 (siGLI1) and S6K1 (siS6), respectively. siCN indicates the control siRNA treatment and β-Actin was used as the endogenous protein control. Quantitation of protein expression, using the ImageJ software, is shown in the bar graphs. Each bar represents the mean ± SEM of triplicate values from a representative experiment. *, Statistical significant, P
    Anti Mouse Gli1 Ab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    PerkinElmer anti mouse secondary antibodies
    <t>GLI1</t> protein levels are unchanged following S6K1 knockdown. Western blot analysis of GLI1 and S6K1 protein expression in SK-N-AS cells, following siRNA-mediated knockdown of GLI1 and S6K1. Note the reduction of the GLI1 and S6K1 protein bands by the siRNAs targeting GLI1 (siGLI1) and S6K1 (siS6), respectively. siCN indicates the control siRNA treatment and β-Actin was used as the endogenous protein control. Quantitation of protein expression, using the ImageJ software, is shown in the bar graphs. Each bar represents the mean ± SEM of triplicate values from a representative experiment. *, Statistical significant, P
    Anti Mouse Secondary Antibodies, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 85/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Promega anti mouse secondary ab
    <t>GLI1</t> protein levels are unchanged following S6K1 knockdown. Western blot analysis of GLI1 and S6K1 protein expression in SK-N-AS cells, following siRNA-mediated knockdown of GLI1 and S6K1. Note the reduction of the GLI1 and S6K1 protein bands by the siRNAs targeting GLI1 (siGLI1) and S6K1 (siS6), respectively. siCN indicates the control siRNA treatment and β-Actin was used as the endogenous protein control. Quantitation of protein expression, using the ImageJ software, is shown in the bar graphs. Each bar represents the mean ± SEM of triplicate values from a representative experiment. *, Statistical significant, P
    Anti Mouse Secondary Ab, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad anti mouse antibody
    <t>GLI1</t> protein levels are unchanged following S6K1 knockdown. Western blot analysis of GLI1 and S6K1 protein expression in SK-N-AS cells, following siRNA-mediated knockdown of GLI1 and S6K1. Note the reduction of the GLI1 and S6K1 protein bands by the siRNAs targeting GLI1 (siGLI1) and S6K1 (siS6), respectively. siCN indicates the control siRNA treatment and β-Actin was used as the endogenous protein control. Quantitation of protein expression, using the ImageJ software, is shown in the bar graphs. Each bar represents the mean ± SEM of triplicate values from a representative experiment. *, Statistical significant, P
    Anti Mouse Antibody, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 197 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher anti mouse fcεriα ab
    Effect of PU.1 siRNA on mouse MCs. ( a ) mRNA level of PU.1. *1, p = 0.00064; *2, p = 0.00061; *3, p = 0.0011. n = 3–4. ( b ) Cell surface expression level of FcεRI. MFI; Mean fluorescence intensity. *, p = 0.000016. n = 5. ( c) mRNA levels of the α−, β−, and γ-chains of FcεRI. *1, p = 0.0000056; *2, p = 0.0000017; *3, p = 0.00000055. n = 8. ( d ) mRNA levels of intracellular molecules. *1, p = 0.029; *2, p = 0.0025; *3, p = 0.0018. n = 3. ( e ) Western blotting analyses of whole cell lysates. Full-length blots are included in Supplemental Fig. S1. *1, p = 0.024; *2, p = 0.012; *3, p = 0.023. n = 3–4. ( f ) Intracellular staining of <t>FcεRIα.</t> A typical result is shown at left. Quantitative analysis data of MFI obtained in three independent experiments are shown at right. * p = 0.0017. ( g ) IgE-mediated degranulation degree. * p = 0.032. n = 11. ( h ) IgE-mediated TNF-α release. * p = 0.037. n = 3. The data in Fig. 1 represent the mean ± SD of independent experiments (“n” times repeated) performed with duplicate samples.
    Anti Mouse Fcεriα Ab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Santa Cruz Biotechnology anti mouse tlr4 ab
    Quantification of cytokines by ELISA. MΦ obtained from C57BL/6 and C3H/HeJ mice were cultured in absence and presence of HlyA or with <t>anti-TLR4</t> Ab/anti-TLR2 Ab plus HlyA. The supernatants were assayed for TNF-α after 24 h and IL-10/IL-12
    Anti Mouse Tlr4 Ab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or anti–mouse antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.

    Journal: The Journal of Cell Biology

    Article Title: Structural requirements for localization and activation of protein kinase C ? (PKC?) at the Golgi compartment

    doi: 10.1083/jcb.200110047

    Figure Lengend Snippet: Subcellular localization of PKC μ -GFP mutants. The indicated PKCμ-GFP mutants were transiently expressed in HeLa cells and analyzed by confocal laser scanning microscopy. 40 h after transfection cells were fixed and stained for p24 or p230 with an anti-p24 rabbit antiserum or an anti-p230 monoclonal antibody followed by an incubation with Alexa 546–labeled anti–rabbit or anti–mouse antibodies. Intact cell morphology was controlled by transmission light microscopy. PKCμ-GFP (green) and p24/p230 (red) stains were combined (right). The overlay is indicated by the yellow color. (A) Localization of wild-type PKCμ and a kinase-dead K612W mutant. (B) Localization of deletion mutants and selective domains. (C) Localization of NH 2 -terminal PKCμ deletion mutants and the respective NH 2 -terminal domains. Enlargement of the indicated section is shown. (D) Localization of endogenous PKCμ in HEK293 cells. Cells were stained with a PKCμ-specific antibody and with anti-GM130 as a Golgi compartment–specific marker.

    Article Snippet: The Alexa 546–conjugated goat anti–rabbit and anti–mouse antibodies were purchased from Molecular Probes.

    Techniques: Confocal Laser Scanning Microscopy, Transfection, Staining, Incubation, Labeling, Transmission Assay, Light Microscopy, Mutagenesis, Marker

    Immunoprecipitation of myristoylated calmyrin and localization of calmyrin to the membrane fraction. (A) Fluorography of myristoylated proteins immunoprecipitated with rabbit  anti-calmyrin from HeLa cells after transfection with N-myc  calmyrin (lane 1 and 2), C-myc calmyrin (lane 3 and 4), or wild-type calmyrin (lane 5 and 6) and 24 h incubation with  3 H-myristic  acid. The cell lysates (L) and immunoprecipitated (IP) samples  are shown. The myristoylated calmyrin band is present in lanes 4  and 6 (indicated by the arrows), but absent from lane 2. The  lower panel shows an immunoblot of the supernatants (S) and  immunoprecipitants (IP) of these same transfected cell lysates to  confirm the expression level and successful immunoprecipitation  of calmyrin. (B) Immunoblotting of calmyrin-expressing HeLa  cell lysates for lamins A and C (68 and 66 kD) and calmyrin (22  kD) after fractionation in the absence (−) of detergent (lanes 1  and 2) or in the presence (+) of 1% Triton X-100 (lane 3 and 4)  into a soluble supernatant (S) and an insoluble pellet (P). The  lower panel shows the identical fractionation of endogenous  calmyrin in mouse kidney primary cell culture.

    Journal: The Journal of Cell Biology

    Article Title: A Myristoylated Calcium-binding Protein that Preferentially Interacts with the Alzheimer's Disease Presenilin 2 Protein

    doi:

    Figure Lengend Snippet: Immunoprecipitation of myristoylated calmyrin and localization of calmyrin to the membrane fraction. (A) Fluorography of myristoylated proteins immunoprecipitated with rabbit anti-calmyrin from HeLa cells after transfection with N-myc calmyrin (lane 1 and 2), C-myc calmyrin (lane 3 and 4), or wild-type calmyrin (lane 5 and 6) and 24 h incubation with 3 H-myristic acid. The cell lysates (L) and immunoprecipitated (IP) samples are shown. The myristoylated calmyrin band is present in lanes 4 and 6 (indicated by the arrows), but absent from lane 2. The lower panel shows an immunoblot of the supernatants (S) and immunoprecipitants (IP) of these same transfected cell lysates to confirm the expression level and successful immunoprecipitation of calmyrin. (B) Immunoblotting of calmyrin-expressing HeLa cell lysates for lamins A and C (68 and 66 kD) and calmyrin (22 kD) after fractionation in the absence (−) of detergent (lanes 1 and 2) or in the presence (+) of 1% Triton X-100 (lane 3 and 4) into a soluble supernatant (S) and an insoluble pellet (P). The lower panel shows the identical fractionation of endogenous calmyrin in mouse kidney primary cell culture.

    Article Snippet: Antibodies used were rabbit anti-calmyrin serum (diluted 1:250), goat anti-PS2(NH2 -terminal) antibody (diluted 1:150; Santa Cruz Biotechnology, Inc. ), rabbit anti-lamin serum (diluted 1:200; ), rabbit anti-NFL serum (diluted 1:250; generated in this lab using recombinant-purified, bacterially expressed, mouse neurofilament light chain), M30 CytoDEATH mouse anti-cytokeratin 18 antibody (diluted 1:50; Boehringer Mannheim ), fluorescein- and rhodamine-conjugated donkey anti–rabbit, anti–goat, and anti–mouse antibodies (Jackson ImmunoResearch Laboratories, Inc.).

    Techniques: Immunoprecipitation, Transfection, Incubation, Expressing, Fractionation, Cell Culture

    GLI1 protein levels are unchanged following S6K1 knockdown. Western blot analysis of GLI1 and S6K1 protein expression in SK-N-AS cells, following siRNA-mediated knockdown of GLI1 and S6K1. Note the reduction of the GLI1 and S6K1 protein bands by the siRNAs targeting GLI1 (siGLI1) and S6K1 (siS6), respectively. siCN indicates the control siRNA treatment and β-Actin was used as the endogenous protein control. Quantitation of protein expression, using the ImageJ software, is shown in the bar graphs. Each bar represents the mean ± SEM of triplicate values from a representative experiment. *, Statistical significant, P

    Journal: BMC Cancer

    Article Title: The impact of S6K1 kinase on neuroblastoma cell proliferation is independent of GLI1 signaling

    doi: 10.1186/1471-2407-14-600

    Figure Lengend Snippet: GLI1 protein levels are unchanged following S6K1 knockdown. Western blot analysis of GLI1 and S6K1 protein expression in SK-N-AS cells, following siRNA-mediated knockdown of GLI1 and S6K1. Note the reduction of the GLI1 and S6K1 protein bands by the siRNAs targeting GLI1 (siGLI1) and S6K1 (siS6), respectively. siCN indicates the control siRNA treatment and β-Actin was used as the endogenous protein control. Quantitation of protein expression, using the ImageJ software, is shown in the bar graphs. Each bar represents the mean ± SEM of triplicate values from a representative experiment. *, Statistical significant, P

    Article Snippet: Cell lysates and immunoprecipitated proteins on the transferred membrane were incubated with anti-mouse GLI1 Ab (#2643, Cell Signaling) for GLI1 or anti-mouse phosphoserine/threonine Ab (612548, BD Transduction Laboratories) for phosphorylated GLI1, followed by incubation with goat anti-mouse Ab.

    Techniques: Western Blot, Expressing, Quantitation Assay, Software

    SK-N-AS cellular proliferation is insensitive to S6K1 or GLI1 overexpression. (A) SK-N-AS cells, cultured for 48 hours following transfection with control pCMV5 vector, and expression constructs for wild type S6K1 (S6K1 WT) constitutively activated S6K1 (S6K1T389E), function-loss S6K1 (S6K1T389A) and GLI1, were subjected to the EdU incorporation assay for 4 hours. (B) SK-N-AS cells, cultured for 48 hours following transfection with control siRNAs and pCMV5 vector (siCN + pCMV), S6K1 siRNAs and pCMV5 vector (siS6K1 + pCMV) and S6K1 siRNAs and GLI1 expression construct (siS6K1 + pGLI1), were subjected to the EdU incorporation assay for 4 hours. The data were analyzed with the one-way ANOVA test followed by Tukey’s multiple comparison using the GraphPad Prism software. Each bar represents the mean ± SEM of three independent experiments *, Statistical significant, P

    Journal: BMC Cancer

    Article Title: The impact of S6K1 kinase on neuroblastoma cell proliferation is independent of GLI1 signaling

    doi: 10.1186/1471-2407-14-600

    Figure Lengend Snippet: SK-N-AS cellular proliferation is insensitive to S6K1 or GLI1 overexpression. (A) SK-N-AS cells, cultured for 48 hours following transfection with control pCMV5 vector, and expression constructs for wild type S6K1 (S6K1 WT) constitutively activated S6K1 (S6K1T389E), function-loss S6K1 (S6K1T389A) and GLI1, were subjected to the EdU incorporation assay for 4 hours. (B) SK-N-AS cells, cultured for 48 hours following transfection with control siRNAs and pCMV5 vector (siCN + pCMV), S6K1 siRNAs and pCMV5 vector (siS6K1 + pCMV) and S6K1 siRNAs and GLI1 expression construct (siS6K1 + pGLI1), were subjected to the EdU incorporation assay for 4 hours. The data were analyzed with the one-way ANOVA test followed by Tukey’s multiple comparison using the GraphPad Prism software. Each bar represents the mean ± SEM of three independent experiments *, Statistical significant, P

    Article Snippet: Cell lysates and immunoprecipitated proteins on the transferred membrane were incubated with anti-mouse GLI1 Ab (#2643, Cell Signaling) for GLI1 or anti-mouse phosphoserine/threonine Ab (612548, BD Transduction Laboratories) for phosphorylated GLI1, followed by incubation with goat anti-mouse Ab.

    Techniques: Over Expression, Cell Culture, Transfection, Plasmid Preparation, Expressing, Construct, Software

    S6K1 and GLI1 knockdown reduces SK-N-AS cellular proliferation. SK-N-AS cells, cultured for 48 hours following transfection with control (siCN), GLI1 (siGLI1) or S6K1 (siS6K1) siRNAs, were subjected to the EdU incorporation assay for 4 hours. The percentage of cells labeled with Alexa Fluor 488 azide was detected by flow cytometry. The data were analyzed with the one-way ANOVA test followed by Tukey’s multiple comparison using the GraphPad Prism software. Each bar represents the mean ± SEM of three independent experiments. *, Statistical significant, P

    Journal: BMC Cancer

    Article Title: The impact of S6K1 kinase on neuroblastoma cell proliferation is independent of GLI1 signaling

    doi: 10.1186/1471-2407-14-600

    Figure Lengend Snippet: S6K1 and GLI1 knockdown reduces SK-N-AS cellular proliferation. SK-N-AS cells, cultured for 48 hours following transfection with control (siCN), GLI1 (siGLI1) or S6K1 (siS6K1) siRNAs, were subjected to the EdU incorporation assay for 4 hours. The percentage of cells labeled with Alexa Fluor 488 azide was detected by flow cytometry. The data were analyzed with the one-way ANOVA test followed by Tukey’s multiple comparison using the GraphPad Prism software. Each bar represents the mean ± SEM of three independent experiments. *, Statistical significant, P

    Article Snippet: Cell lysates and immunoprecipitated proteins on the transferred membrane were incubated with anti-mouse GLI1 Ab (#2643, Cell Signaling) for GLI1 or anti-mouse phosphoserine/threonine Ab (612548, BD Transduction Laboratories) for phosphorylated GLI1, followed by incubation with goat anti-mouse Ab.

    Techniques: Cell Culture, Transfection, Labeling, Flow Cytometry, Cytometry, Software

    GLI1 but not S6K1 knockdown reduces GLI1, GLI2, GLI3, SMO and PTCH2 expression. The expression of S6K1 (A) , GLI1 (B) , GLI2 (C) , GLI3 (D) , the signaling molecule SMO (E) and the typical GLI1 target gene PTCH2 (F) in SK-N-AS cells, following siRNA knockdown of GLI1 and S6K1, was determined by real-time PCR. Data are represented as relative expression (2 -∆∆Ct values), calculated by subtracting the Ct value of the housekeeping gene TBP from the Ct value of the interrogated transcripts (∆Ct), and normalized to the ∆Ct value obtained with siCN. Error bars indicate the standard deviation. *, Statistical significant, P

    Journal: BMC Cancer

    Article Title: The impact of S6K1 kinase on neuroblastoma cell proliferation is independent of GLI1 signaling

    doi: 10.1186/1471-2407-14-600

    Figure Lengend Snippet: GLI1 but not S6K1 knockdown reduces GLI1, GLI2, GLI3, SMO and PTCH2 expression. The expression of S6K1 (A) , GLI1 (B) , GLI2 (C) , GLI3 (D) , the signaling molecule SMO (E) and the typical GLI1 target gene PTCH2 (F) in SK-N-AS cells, following siRNA knockdown of GLI1 and S6K1, was determined by real-time PCR. Data are represented as relative expression (2 -∆∆Ct values), calculated by subtracting the Ct value of the housekeeping gene TBP from the Ct value of the interrogated transcripts (∆Ct), and normalized to the ∆Ct value obtained with siCN. Error bars indicate the standard deviation. *, Statistical significant, P

    Article Snippet: Cell lysates and immunoprecipitated proteins on the transferred membrane were incubated with anti-mouse GLI1 Ab (#2643, Cell Signaling) for GLI1 or anti-mouse phosphoserine/threonine Ab (612548, BD Transduction Laboratories) for phosphorylated GLI1, followed by incubation with goat anti-mouse Ab.

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Standard Deviation

    Effect of PU.1 siRNA on mouse MCs. ( a ) mRNA level of PU.1. *1, p = 0.00064; *2, p = 0.00061; *3, p = 0.0011. n = 3–4. ( b ) Cell surface expression level of FcεRI. MFI; Mean fluorescence intensity. *, p = 0.000016. n = 5. ( c) mRNA levels of the α−, β−, and γ-chains of FcεRI. *1, p = 0.0000056; *2, p = 0.0000017; *3, p = 0.00000055. n = 8. ( d ) mRNA levels of intracellular molecules. *1, p = 0.029; *2, p = 0.0025; *3, p = 0.0018. n = 3. ( e ) Western blotting analyses of whole cell lysates. Full-length blots are included in Supplemental Fig. S1. *1, p = 0.024; *2, p = 0.012; *3, p = 0.023. n = 3–4. ( f ) Intracellular staining of FcεRIα. A typical result is shown at left. Quantitative analysis data of MFI obtained in three independent experiments are shown at right. * p = 0.0017. ( g ) IgE-mediated degranulation degree. * p = 0.032. n = 11. ( h ) IgE-mediated TNF-α release. * p = 0.037. n = 3. The data in Fig. 1 represent the mean ± SD of independent experiments (“n” times repeated) performed with duplicate samples.

    Journal: Scientific Reports

    Article Title: The effect of PU.1 knockdown on gene expression and function of mast cells

    doi: 10.1038/s41598-018-19378-y

    Figure Lengend Snippet: Effect of PU.1 siRNA on mouse MCs. ( a ) mRNA level of PU.1. *1, p = 0.00064; *2, p = 0.00061; *3, p = 0.0011. n = 3–4. ( b ) Cell surface expression level of FcεRI. MFI; Mean fluorescence intensity. *, p = 0.000016. n = 5. ( c) mRNA levels of the α−, β−, and γ-chains of FcεRI. *1, p = 0.0000056; *2, p = 0.0000017; *3, p = 0.00000055. n = 8. ( d ) mRNA levels of intracellular molecules. *1, p = 0.029; *2, p = 0.0025; *3, p = 0.0018. n = 3. ( e ) Western blotting analyses of whole cell lysates. Full-length blots are included in Supplemental Fig. S1. *1, p = 0.024; *2, p = 0.012; *3, p = 0.023. n = 3–4. ( f ) Intracellular staining of FcεRIα. A typical result is shown at left. Quantitative analysis data of MFI obtained in three independent experiments are shown at right. * p = 0.0017. ( g ) IgE-mediated degranulation degree. * p = 0.032. n = 11. ( h ) IgE-mediated TNF-α release. * p = 0.037. n = 3. The data in Fig. 1 represent the mean ± SD of independent experiments (“n” times repeated) performed with duplicate samples.

    Article Snippet: Flow cytometry The cell surface expression level of mouse FcεRI was determined by a MACS Quant (Miltenyi Biotech, Tubingen, Germany) using an anti-mouse FcεRIα Ab (MAR-1, eBioscience).

    Techniques: Expressing, Fluorescence, Western Blot, Staining

    Quantification of cytokines by ELISA. MΦ obtained from C57BL/6 and C3H/HeJ mice were cultured in absence and presence of HlyA or with anti-TLR4 Ab/anti-TLR2 Ab plus HlyA. The supernatants were assayed for TNF-α after 24 h and IL-10/IL-12

    Journal: The Journal of Biological Chemistry

    Article Title: Hemolysin Induces Toll-like Receptor (TLR)-independent Apoptosis and Multiple TLR-associated Parallel Activation of Macrophages

    doi: 10.1074/jbc.M111.241851

    Figure Lengend Snippet: Quantification of cytokines by ELISA. MΦ obtained from C57BL/6 and C3H/HeJ mice were cultured in absence and presence of HlyA or with anti-TLR4 Ab/anti-TLR2 Ab plus HlyA. The supernatants were assayed for TNF-α after 24 h and IL-10/IL-12

    Article Snippet: For inhibition studies, MΦ were incubated with either 10 μg/ml purified anti-mouse TLR2 mAb (Functional Grade; eBioscience), 5 μg/ml purified anti-mouse TLR4 Ab (Santa Cruz Biotechnology), or both for 30 min prior to the addition of HlyA.

    Techniques: Enzyme-linked Immunosorbent Assay, Mouse Assay, Cell Culture

    Jacalin- and VCC 50 -induced expression of TLRs, co-stimulatory and activation molecules. MΦ obtained from C3H/HeJ and C57BL/6 mice were cultured with ( black line ) and without ( shaded ) jacalin or VCC 50 . Up-regulation of TLR4, TLR2, CD86, and CD40

    Journal: The Journal of Biological Chemistry

    Article Title: Hemolysin Induces Toll-like Receptor (TLR)-independent Apoptosis and Multiple TLR-associated Parallel Activation of Macrophages

    doi: 10.1074/jbc.M111.241851

    Figure Lengend Snippet: Jacalin- and VCC 50 -induced expression of TLRs, co-stimulatory and activation molecules. MΦ obtained from C3H/HeJ and C57BL/6 mice were cultured with ( black line ) and without ( shaded ) jacalin or VCC 50 . Up-regulation of TLR4, TLR2, CD86, and CD40

    Article Snippet: For inhibition studies, MΦ were incubated with either 10 μg/ml purified anti-mouse TLR2 mAb (Functional Grade; eBioscience), 5 μg/ml purified anti-mouse TLR4 Ab (Santa Cruz Biotechnology), or both for 30 min prior to the addition of HlyA.

    Techniques: Expressing, Activation Assay, Mouse Assay, Cell Culture

    TLR4-dependent, HlyA-induced expression of MyD88 and NF-κB. A , total RNA was extracted from the cells cultured with or without HlyA and subjected to RT-PCR using the corresponding primers of MyD88 and GAPDH. Ethidium bromide-stained PCR products

    Journal: The Journal of Biological Chemistry

    Article Title: Hemolysin Induces Toll-like Receptor (TLR)-independent Apoptosis and Multiple TLR-associated Parallel Activation of Macrophages

    doi: 10.1074/jbc.M111.241851

    Figure Lengend Snippet: TLR4-dependent, HlyA-induced expression of MyD88 and NF-κB. A , total RNA was extracted from the cells cultured with or without HlyA and subjected to RT-PCR using the corresponding primers of MyD88 and GAPDH. Ethidium bromide-stained PCR products

    Article Snippet: For inhibition studies, MΦ were incubated with either 10 μg/ml purified anti-mouse TLR2 mAb (Functional Grade; eBioscience), 5 μg/ml purified anti-mouse TLR4 Ab (Santa Cruz Biotechnology), or both for 30 min prior to the addition of HlyA.

    Techniques: Expressing, Cell Culture, Reverse Transcription Polymerase Chain Reaction, Staining, Polymerase Chain Reaction

    HlyA-induced time-dependent up-regulation of activation, co-stimulatory and MHC class II (I-Ab) molecules are controlled by TLR4 and 2. A and B , cells were cultured with ( black line ) and without ( shaded ) HlyA for CD80–CD86, CD40, and MHC class

    Journal: The Journal of Biological Chemistry

    Article Title: Hemolysin Induces Toll-like Receptor (TLR)-independent Apoptosis and Multiple TLR-associated Parallel Activation of Macrophages

    doi: 10.1074/jbc.M111.241851

    Figure Lengend Snippet: HlyA-induced time-dependent up-regulation of activation, co-stimulatory and MHC class II (I-Ab) molecules are controlled by TLR4 and 2. A and B , cells were cultured with ( black line ) and without ( shaded ) HlyA for CD80–CD86, CD40, and MHC class

    Article Snippet: For inhibition studies, MΦ were incubated with either 10 μg/ml purified anti-mouse TLR2 mAb (Functional Grade; eBioscience), 5 μg/ml purified anti-mouse TLR4 Ab (Santa Cruz Biotechnology), or both for 30 min prior to the addition of HlyA.

    Techniques: Activation Assay, Cell Culture