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src targeting sirna sc 5266  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology src targeting sirna sc 5266
    Src Targeting Sirna Sc 5266, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 97/100, based on 1297 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/src+sirna/c-Src+Antibody/pmc13046926-253-2-8
    Average 97 stars, based on 1297 article reviews
    src targeting sirna sc 5266 - by Bioz Stars, 2026-11
    97/100 stars

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    Related Articles

    Control:

    Article Title: Induction of Fibroblast Growth Factor Receptor 4 by Helicobacter pylori via Signal Transducer and Activator of Transcription 3 With a Feedforward Activation Loop Involving SRC Signaling in Gastric Cancer
    Article Snippet: Department of General Surgery, The First Affiliated Hospital of Nanjing Medical University, Nanjing, Jiangsu, China; Department of Surgery, University of Miami Miller School of Medicine, Miami, Florida; Department of Thoracic Surgery, Jiangsu Cancer Hospital, Jiangsu Institute of Cancer Research, the Affiliated Cancer Hospital of Nanjing Medical University, Nanjing, Jiangsu, China; Cancer and Inflammation Laboratory, Olivia Newton-John Cancer Research Institute and School of Cancer Medicine, La Trobe University, Heidelberg, Victoria, Australia; Jiangsu Key Lab of Cancer Biomarkers, Prevention and Treatment, Jiangsu Collaborative Innovation Center for Cancer Personalized Medicine, School of Public Health, Nanjing Medical University, Nanjing, Jiangsu, China; Department of Veterans Affairs, Miami Healthcare System, Miami, Florida; and Sylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, Florida

    Article Title: Fatty acid uptake activates an AXL–CAV1–β-catenin axis to drive melanoma progression
    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. .. Caveolin-1 WT or Y14F was subcloned from CAV1-mRFP plasmid ( ) by PCR amplification with the indicated primers ( ) followed by a digestion with Bam HI and Xba I enzymes (New England Biolabs) for 2 h at 37°C.

    Article Title: Fatty acid uptake activates an AXL-CAV1-β-catenin axis to drive melanoma progression.
    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. .. Caveolin-1WT or Y14F was subcloned from CAV1-mRFP plasmid (Tagawa et al. 2005) by PCR amplification with the indicated primers (Table 1) followed by a digestion with Bam HI and Xba I enzymes (New England Biolabs) for 2 h at 37°C.

    Article Title: Phenotype-specific melanoma uptake of fatty acid from human adipocytes activates AXL and CAV1-dependent β-catenin nuclear accumulation
    Article Snippet: .. Specific siRNA oligonucleotides for β-catenin and control siRNA were obtained from Qiagen, Caveolin-1, and SRC siRNA from Santa Cruz Biotechnology and SRC siRNA Dharmacon Inc. .. Caveolin-1 WT or Y14F were subcloned from CAV1-mRFP plasmid ( ) by PCR amplification with the indicated primers (Key Resources table) followed by a digestion with Bam HI and Xba I enzymes (New England Biolabs) for 37°C 2 h. The fragments were gel-purified with a kit (Qiagen, Crawley, UK) were cloned into pcDNA3.1-myc-His plasmid (Promega).

    Negative Control:

    Article Title: Induction of Fibroblast Growth Factor Receptor 4 by Helicobacter pylori via Signal Transducer and Activator of Transcription 3 With a Feedforward Activation Loop Involving SRC Signaling in Gastric Cancer
    Article Snippet: Department of General Surgery, The First Affiliated Hospital of Nanjing Medical University, Nanjing, Jiangsu, China; Department of Surgery, University of Miami Miller School of Medicine, Miami, Florida; Department of Thoracic Surgery, Jiangsu Cancer Hospital, Jiangsu Institute of Cancer Research, the Affiliated Cancer Hospital of Nanjing Medical University, Nanjing, Jiangsu, China; Cancer and Inflammation Laboratory, Olivia Newton-John Cancer Research Institute and School of Cancer Medicine, La Trobe University, Heidelberg, Victoria, Australia; Jiangsu Key Lab of Cancer Biomarkers, Prevention and Treatment, Jiangsu Collaborative Innovation Center for Cancer Personalized Medicine, School of Public Health, Nanjing Medical University, Nanjing, Jiangsu, China; Department of Veterans Affairs, Miami Healthcare System, Miami, Florida; and Sylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, Florida

    Article Title: Toll-Like Receptor 4 Mediated Oxidized Low-Density Lipoprotein-Induced Foam Cell Formation in Vascular Smooth Muscle Cells via Src and Sirt1/3 Pathway.
    Article Snippet: Fetal bovine serum (Cat#16000), advanced DMEM/F-12 (Cat#12634010), and antibiotic-antimycotic (Cat#15240096) were obtained from Gibco (CA, USA). oxLDL (Cat#L34357), Nile Red (Cat#N1142), Image-ITTM LIVE Green Reactive Oxygen Species Detection Kit (Cat#I36007), MitoSOXTM Red Mitochondrial Superoxide Indicator (Cat#M36008), DAPI (Cat#D1306), TRIzolTM Reagent (Cat#15596026), Goat antiRabbit secondary antibody conjunction with Alexa Fluor Plus 555 (Cat#A-21429), Goat anti-Mouse secondary antibody conjunction with Alexa Fluor Plus 488 (Cat#A11001), and LipofectamineTM RNAi MAX transfection reagent (Cat#13778150) were purchased from Invitrogen (CA, USA). .. Tlr4 siRNA (Cat#sc-40261), Src siRNA (Catsc-29859), and negative control siRNA (Cat#sc37007) were bought from Santa Cruz (TX, USA). .. Let-blank (Cat#GCNL), Let-Sirt1 (+) (Cat#GCD0161581), and Letsirt3 (+) (Cat#GCD0201555) were acquired from Shanghai Genechem (Shanghai, China).

    other:

    Article Title: Toll-Like Receptor 4 Mediated Oxidized Low-Density Lipoprotein-Induced Foam Cell Formation in Vascular Smooth Muscle Cells via Src and Sirt1/3 Pathway
    Article Snippet: Fetal bovine serum (Cat#16000), advanced DMEM/F-12 (Cat#12634010), and antibiotic-antimycotic (Cat#15240096) were obtained from Gibco (CA, USA).



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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