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src sirna  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology src sirna
    Oleic acid induces β-catenin–CAV1 interaction and nuclear localization. ( A ) Immunofluorescence of IGR39 cells using antibodies against the indicated proteins in cells exposed to 100 μM oleic (OA). Scale bars: top six panels, 50 µm; bottom three panels, 20 µm . ( B ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA over time. GAPDH and TBP were used as markers of the cytoplasmic and nuclear fractions. ( C ) Immunofluorescence of IGR39 cells for the indicated proteins after exposure or not to 100 μM OA or palmitic acid (PA) for 6 h. Scale bars, 25 µm. ( D ) Western blot of fractionated IGR39 cells treated with oleic acid for the indicated times. ( E ) Luciferase reporter assays in the indicated cell lines showing the ratio of luciferase activity from the TOP:FOP-flash β-catenin activity reporters in melanoma cells exposed to 100 μM OA or PA for the indicated times. LiCl (10 mM) was used as a positive control. N = 3. Error bars indicate SEM. (*) P < 0.05, (**) P < 0.01, (***) P < 0.001; one-way ANOVA statistical test. ( F ) Western blot for the indicated proteins immunoprecipitated from IGR39 nuclear extract using anti-β-catenin antibody from cells treated or not with 100 μM OA or PA for the indicated times. The blot shows both immunoprecipitation (IP) and flowthrough (FT). ( G ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA for the indicated times and transfected with either control or CAV1-specific <t>siRNA.</t> ( Left ) Nuclear fraction. ( Right ) Cytoplasmic fraction.
    Src Sirna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 95 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Fatty acid uptake activates an AXL–CAV1–β-catenin axis to drive melanoma progression"

    Article Title: Fatty acid uptake activates an AXL–CAV1–β-catenin axis to drive melanoma progression

    Journal: Genes & Development

    doi: 10.1101/gad.351985.124

    Oleic acid induces β-catenin–CAV1 interaction and nuclear localization. ( A ) Immunofluorescence of IGR39 cells using antibodies against the indicated proteins in cells exposed to 100 μM oleic (OA). Scale bars: top six panels, 50 µm; bottom three panels, 20 µm . ( B ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA over time. GAPDH and TBP were used as markers of the cytoplasmic and nuclear fractions. ( C ) Immunofluorescence of IGR39 cells for the indicated proteins after exposure or not to 100 μM OA or palmitic acid (PA) for 6 h. Scale bars, 25 µm. ( D ) Western blot of fractionated IGR39 cells treated with oleic acid for the indicated times. ( E ) Luciferase reporter assays in the indicated cell lines showing the ratio of luciferase activity from the TOP:FOP-flash β-catenin activity reporters in melanoma cells exposed to 100 μM OA or PA for the indicated times. LiCl (10 mM) was used as a positive control. N = 3. Error bars indicate SEM. (*) P < 0.05, (**) P < 0.01, (***) P < 0.001; one-way ANOVA statistical test. ( F ) Western blot for the indicated proteins immunoprecipitated from IGR39 nuclear extract using anti-β-catenin antibody from cells treated or not with 100 μM OA or PA for the indicated times. The blot shows both immunoprecipitation (IP) and flowthrough (FT). ( G ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA for the indicated times and transfected with either control or CAV1-specific siRNA. ( Left ) Nuclear fraction. ( Right ) Cytoplasmic fraction.
    Figure Legend Snippet: Oleic acid induces β-catenin–CAV1 interaction and nuclear localization. ( A ) Immunofluorescence of IGR39 cells using antibodies against the indicated proteins in cells exposed to 100 μM oleic (OA). Scale bars: top six panels, 50 µm; bottom three panels, 20 µm . ( B ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA over time. GAPDH and TBP were used as markers of the cytoplasmic and nuclear fractions. ( C ) Immunofluorescence of IGR39 cells for the indicated proteins after exposure or not to 100 μM OA or palmitic acid (PA) for 6 h. Scale bars, 25 µm. ( D ) Western blot of fractionated IGR39 cells treated with oleic acid for the indicated times. ( E ) Luciferase reporter assays in the indicated cell lines showing the ratio of luciferase activity from the TOP:FOP-flash β-catenin activity reporters in melanoma cells exposed to 100 μM OA or PA for the indicated times. LiCl (10 mM) was used as a positive control. N = 3. Error bars indicate SEM. (*) P < 0.05, (**) P < 0.01, (***) P < 0.001; one-way ANOVA statistical test. ( F ) Western blot for the indicated proteins immunoprecipitated from IGR39 nuclear extract using anti-β-catenin antibody from cells treated or not with 100 μM OA or PA for the indicated times. The blot shows both immunoprecipitation (IP) and flowthrough (FT). ( G ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA for the indicated times and transfected with either control or CAV1-specific siRNA. ( Left ) Nuclear fraction. ( Right ) Cytoplasmic fraction.

    Techniques Used: Immunofluorescence, Western Blot, Luciferase, Activity Assay, Positive Control, Immunoprecipitation, Transfection, Control

    Reagents used in this study
    Figure Legend Snippet: Reagents used in this study

    Techniques Used: Software, Transduction, Virus, Subcloning, Bacteria, Recombinant, Bradford Assay, Protease Inhibitor, RNA Extraction, Reporter Assay, Bicinchoninic Acid Protein Assay, Quantitative RT-PCR, Negative Control



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    Oleic acid induces β-catenin–CAV1 interaction and nuclear localization. ( A ) Immunofluorescence of IGR39 cells using antibodies against the indicated proteins in cells exposed to 100 μM oleic (OA). Scale bars: top six panels, 50 µm; bottom three panels, 20 µm . ( B ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA over time. GAPDH and TBP were used as markers of the cytoplasmic and nuclear fractions. ( C ) Immunofluorescence of IGR39 cells for the indicated proteins after exposure or not to 100 μM OA or palmitic acid (PA) for 6 h. Scale bars, 25 µm. ( D ) Western blot of fractionated IGR39 cells treated with oleic acid for the indicated times. ( E ) Luciferase reporter assays in the indicated cell lines showing the ratio of luciferase activity from the TOP:FOP-flash β-catenin activity reporters in melanoma cells exposed to 100 μM OA or PA for the indicated times. LiCl (10 mM) was used as a positive control. N = 3. Error bars indicate SEM. (*) P < 0.05, (**) P < 0.01, (***) P < 0.001; one-way ANOVA statistical test. ( F ) Western blot for the indicated proteins immunoprecipitated from IGR39 nuclear extract using anti-β-catenin antibody from cells treated or not with 100 μM OA or PA for the indicated times. The blot shows both immunoprecipitation (IP) and flowthrough (FT). ( G ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA for the indicated times and transfected with either control or CAV1-specific <t>siRNA.</t> ( Left ) Nuclear fraction. ( Right ) Cytoplasmic fraction.
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    Oleic acid induces β-catenin–CAV1 interaction and nuclear localization. ( A ) Immunofluorescence of IGR39 cells using antibodies against the indicated proteins in cells exposed to 100 μM oleic (OA). Scale bars: top six panels, 50 µm; bottom three panels, 20 µm . ( B ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA over time. GAPDH and TBP were used as markers of the cytoplasmic and nuclear fractions. ( C ) Immunofluorescence of IGR39 cells for the indicated proteins after exposure or not to 100 μM OA or palmitic acid (PA) for 6 h. Scale bars, 25 µm. ( D ) Western blot of fractionated IGR39 cells treated with oleic acid for the indicated times. ( E ) Luciferase reporter assays in the indicated cell lines showing the ratio of luciferase activity from the TOP:FOP-flash β-catenin activity reporters in melanoma cells exposed to 100 μM OA or PA for the indicated times. LiCl (10 mM) was used as a positive control. N = 3. Error bars indicate SEM. (*) P < 0.05, (**) P < 0.01, (***) P < 0.001; one-way ANOVA statistical test. ( F ) Western blot for the indicated proteins immunoprecipitated from IGR39 nuclear extract using anti-β-catenin antibody from cells treated or not with 100 μM OA or PA for the indicated times. The blot shows both immunoprecipitation (IP) and flowthrough (FT). ( G ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA for the indicated times and transfected with either control or CAV1-specific <t>siRNA.</t> ( Left ) Nuclear fraction. ( Right ) Cytoplasmic fraction.
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    Oleic acid induces β-catenin–CAV1 interaction and nuclear localization. ( A ) Immunofluorescence of IGR39 cells using antibodies against the indicated proteins in cells exposed to 100 μM oleic (OA). Scale bars: top six panels, 50 µm; bottom three panels, 20 µm . ( B ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA over time. GAPDH and TBP were used as markers of the cytoplasmic and nuclear fractions. ( C ) Immunofluorescence of IGR39 cells for the indicated proteins after exposure or not to 100 μM OA or palmitic acid (PA) for 6 h. Scale bars, 25 µm. ( D ) Western blot of fractionated IGR39 cells treated with oleic acid for the indicated times. ( E ) Luciferase reporter assays in the indicated cell lines showing the ratio of luciferase activity from the TOP:FOP-flash β-catenin activity reporters in melanoma cells exposed to 100 μM OA or PA for the indicated times. LiCl (10 mM) was used as a positive control. N = 3. Error bars indicate SEM. (*) P < 0.05, (**) P < 0.01, (***) P < 0.001; one-way ANOVA statistical test. ( F ) Western blot for the indicated proteins immunoprecipitated from IGR39 nuclear extract using anti-β-catenin antibody from cells treated or not with 100 μM OA or PA for the indicated times. The blot shows both immunoprecipitation (IP) and flowthrough (FT). ( G ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA for the indicated times and transfected with either control or CAV1-specific <t>siRNA.</t> ( Left ) Nuclear fraction. ( Right ) Cytoplasmic fraction.
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    Image Search Results


    Oleic acid induces β-catenin–CAV1 interaction and nuclear localization. ( A ) Immunofluorescence of IGR39 cells using antibodies against the indicated proteins in cells exposed to 100 μM oleic (OA). Scale bars: top six panels, 50 µm; bottom three panels, 20 µm . ( B ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA over time. GAPDH and TBP were used as markers of the cytoplasmic and nuclear fractions. ( C ) Immunofluorescence of IGR39 cells for the indicated proteins after exposure or not to 100 μM OA or palmitic acid (PA) for 6 h. Scale bars, 25 µm. ( D ) Western blot of fractionated IGR39 cells treated with oleic acid for the indicated times. ( E ) Luciferase reporter assays in the indicated cell lines showing the ratio of luciferase activity from the TOP:FOP-flash β-catenin activity reporters in melanoma cells exposed to 100 μM OA or PA for the indicated times. LiCl (10 mM) was used as a positive control. N = 3. Error bars indicate SEM. (*) P < 0.05, (**) P < 0.01, (***) P < 0.001; one-way ANOVA statistical test. ( F ) Western blot for the indicated proteins immunoprecipitated from IGR39 nuclear extract using anti-β-catenin antibody from cells treated or not with 100 μM OA or PA for the indicated times. The blot shows both immunoprecipitation (IP) and flowthrough (FT). ( G ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA for the indicated times and transfected with either control or CAV1-specific siRNA. ( Left ) Nuclear fraction. ( Right ) Cytoplasmic fraction.

    Journal: Genes & Development

    Article Title: Fatty acid uptake activates an AXL–CAV1–β-catenin axis to drive melanoma progression

    doi: 10.1101/gad.351985.124

    Figure Lengend Snippet: Oleic acid induces β-catenin–CAV1 interaction and nuclear localization. ( A ) Immunofluorescence of IGR39 cells using antibodies against the indicated proteins in cells exposed to 100 μM oleic (OA). Scale bars: top six panels, 50 µm; bottom three panels, 20 µm . ( B ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA over time. GAPDH and TBP were used as markers of the cytoplasmic and nuclear fractions. ( C ) Immunofluorescence of IGR39 cells for the indicated proteins after exposure or not to 100 μM OA or palmitic acid (PA) for 6 h. Scale bars, 25 µm. ( D ) Western blot of fractionated IGR39 cells treated with oleic acid for the indicated times. ( E ) Luciferase reporter assays in the indicated cell lines showing the ratio of luciferase activity from the TOP:FOP-flash β-catenin activity reporters in melanoma cells exposed to 100 μM OA or PA for the indicated times. LiCl (10 mM) was used as a positive control. N = 3. Error bars indicate SEM. (*) P < 0.05, (**) P < 0.01, (***) P < 0.001; one-way ANOVA statistical test. ( F ) Western blot for the indicated proteins immunoprecipitated from IGR39 nuclear extract using anti-β-catenin antibody from cells treated or not with 100 μM OA or PA for the indicated times. The blot shows both immunoprecipitation (IP) and flowthrough (FT). ( G ) Western blots for the indicated proteins from fractionated IGR39 cells treated or not with 100 μM OA for the indicated times and transfected with either control or CAV1-specific siRNA. ( Left ) Nuclear fraction. ( Right ) Cytoplasmic fraction.

    Article Snippet: Specific siRNA oligonucleotides for β-catenin and control siRNA were obtained from Qiagen, Caveolin-1 and SRC siRNA were from Santa Cruz Biotechnology, and SRC siRNA were from Dharmacon, Inc.

    Techniques: Immunofluorescence, Western Blot, Luciferase, Activity Assay, Positive Control, Immunoprecipitation, Transfection, Control

    Reagents used in this study

    Journal: Genes & Development

    Article Title: Fatty acid uptake activates an AXL–CAV1–β-catenin axis to drive melanoma progression

    doi: 10.1101/gad.351985.124

    Figure Lengend Snippet: Reagents used in this study

    Article Snippet: Specific siRNA oligonucleotides for β-catenin and control siRNA were obtained from Qiagen, Caveolin-1 and SRC siRNA were from Santa Cruz Biotechnology, and SRC siRNA were from Dharmacon, Inc.

    Techniques: Software, Transduction, Virus, Subcloning, Bacteria, Recombinant, Bradford Assay, Protease Inhibitor, RNA Extraction, Reporter Assay, Bicinchoninic Acid Protein Assay, Quantitative RT-PCR, Negative Control