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    Millipore cdo shrna
    Dehydrocorydaline (DHC) rescues myogenic differentiation in <t>Cdo-depleted</t> C2C12 cells. (A) C2C12 cells were transfected with control or Cdo short hairpin (sh)RNA vectors, and lysates were analyzed for Cdo expression. Pan-Cadherin was used as a loading control. (B) C2C12/pSuper and C2C12/Cdo <t>shRNA</t> cells were treated with dimethyl sulfoxide (DMSO) or DHC. The lysates were subjected to western blotting with antibodies against myosin heavy chain (MHC), MyoD, myogenin, phosphorylated-p38 mitoren-activated protein kinases (MAPK) (p-p38) and p38. (C) C2C12/pSuper and C2C12/Cdo shRNA cells were fixed and stained with antibodies against MHC, followed by 4′,6-diamidino-2-phenylindole (DAPI) staining to visualize cell nuclei. Scale bar, 10 μ m. (D) Quantification of myotube formation as presented in (C). Data are presented as the mean ± standard deviation of triplicate determinations. The experiment was repeated three times with similar results. * P
    Cdo Shrna, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Santa Cruz Biotechnology cdo sirna
    Characterization and consequences of GPC3–lhh interaction. ( A – C ) Ihh binds to GPC3. ( A ) Binding of 125 I-Ihh to human embryonic kidney (HEK)293T cells transfected with GPC3 expressing vector or vector controls (EF). A representative experiment of three is shown: points, average of triplicates; bars, ±s.d. ( B ) The specific binding of 125 I-Ihh to HEK293T cells transfected with GPC3 or EF was determined in the presence of 100 × unlabelled Ihh. Bars: average of triplicates+s.d.; asterisk: statistically significant difference. ( C ) SRP analysis of the GPC3–Ihh interaction. GPC3ΔGPI was immobilized in the flow cell into streptavidin-coated SA sensor chips, and various concentrations of Ihh (bottom to top: 15, 30, 60, 120 and 240 nM) were injected on the surface of flow cells. The nonspecific binding was subtracted from the sensogram. Inset: ka , kd and Kd values were determined using a 1:1 Languimuir binding model. Each value is expressed as the mean±s.e. of five different concentrations. ( D ) GPC3 inhibits Hh signalling independently of <t>CDO</t> and HIP. Top: NIH 3T3 cells were transfected with a GPC3 or EF along with a luciferase reporter vector driven by an Hh responsive promoter (8Xgli) and β-galactosidase. As indicated, <t>siRNA</t> for silencing CDO siRNA, HIP siRNA or non-targeting control siRNA was also transfected. Cells were stimulated for 48 h with Shh- or control-conditioned medium and luciferase and β-galactosidase assays carried out. For each siRNA condition, the fold stimulation induced by Hh in EF-transfected cells was considered to be 100%. Bars represent the luciferase activity as percentage of the control (average+s.d. of triplicates). Bottom: Western blot for CDO and HIP in NIH 3T3 cells treated as indicated, using actin as loading control. ( E , F ) Increased Ihh levels in GPC3-null mice. ( E ) Western blot analysis of Ihh levels in whole-embryo lysates using actin as loading control was carried out. Bands were then scanned and quantified by densitometry. Average density+s.d. of Ihh/actin ratio is shown. In all three independent litters were analysed. ( F ) Relative levels of Ihh transcripts determined by real-time PCR using β-actin transcript levels as reference. Two independent litters were analysed. Bars represent mean+s.d. for the indicated genotypes. CDO, CAM-related/downregulated by oncogenes; EF, elongation factor; GPC3, Glypican 3; Hh, hedgehog; HIP, Hedgehog-interacting protein; Ihh, Indian hedgehog; mRNA, messenger RNA; PCR, polymerase chain reaction; RU, relative units; Shh, sonic hedgehog; siRNA, small interference RNA; SRP, small plasmon resonance; WT, wild type.
    Cdo Sirna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    Dehydrocorydaline (DHC) rescues myogenic differentiation in Cdo-depleted C2C12 cells. (A) C2C12 cells were transfected with control or Cdo short hairpin (sh)RNA vectors, and lysates were analyzed for Cdo expression. Pan-Cadherin was used as a loading control. (B) C2C12/pSuper and C2C12/Cdo shRNA cells were treated with dimethyl sulfoxide (DMSO) or DHC. The lysates were subjected to western blotting with antibodies against myosin heavy chain (MHC), MyoD, myogenin, phosphorylated-p38 mitoren-activated protein kinases (MAPK) (p-p38) and p38. (C) C2C12/pSuper and C2C12/Cdo shRNA cells were fixed and stained with antibodies against MHC, followed by 4′,6-diamidino-2-phenylindole (DAPI) staining to visualize cell nuclei. Scale bar, 10 μ m. (D) Quantification of myotube formation as presented in (C). Data are presented as the mean ± standard deviation of triplicate determinations. The experiment was repeated three times with similar results. * P

    Journal: Molecular Medicine Reports

    Article Title: Dehydrocorydaline promotes myogenic differentiation via p38 MAPK activation

    doi: 10.3892/mmr.2016.5653

    Figure Lengend Snippet: Dehydrocorydaline (DHC) rescues myogenic differentiation in Cdo-depleted C2C12 cells. (A) C2C12 cells were transfected with control or Cdo short hairpin (sh)RNA vectors, and lysates were analyzed for Cdo expression. Pan-Cadherin was used as a loading control. (B) C2C12/pSuper and C2C12/Cdo shRNA cells were treated with dimethyl sulfoxide (DMSO) or DHC. The lysates were subjected to western blotting with antibodies against myosin heavy chain (MHC), MyoD, myogenin, phosphorylated-p38 mitoren-activated protein kinases (MAPK) (p-p38) and p38. (C) C2C12/pSuper and C2C12/Cdo shRNA cells were fixed and stained with antibodies against MHC, followed by 4′,6-diamidino-2-phenylindole (DAPI) staining to visualize cell nuclei. Scale bar, 10 μ m. (D) Quantification of myotube formation as presented in (C). Data are presented as the mean ± standard deviation of triplicate determinations. The experiment was repeated three times with similar results. * P

    Article Snippet: Cdo shRNA was purchased from Sigma-Aldrich (Merck Millipore, Darmstadt, Germany) and its sequence is 5′-CAGCGTTGGTGCCGTTGTG-3′. pSuper was obtained from Oligoengine (Seattle, WA, USA).

    Techniques: Transfection, Expressing, shRNA, Western Blot, Staining, Standard Deviation

    Characterization and consequences of GPC3–lhh interaction. ( A – C ) Ihh binds to GPC3. ( A ) Binding of 125 I-Ihh to human embryonic kidney (HEK)293T cells transfected with GPC3 expressing vector or vector controls (EF). A representative experiment of three is shown: points, average of triplicates; bars, ±s.d. ( B ) The specific binding of 125 I-Ihh to HEK293T cells transfected with GPC3 or EF was determined in the presence of 100 × unlabelled Ihh. Bars: average of triplicates+s.d.; asterisk: statistically significant difference. ( C ) SRP analysis of the GPC3–Ihh interaction. GPC3ΔGPI was immobilized in the flow cell into streptavidin-coated SA sensor chips, and various concentrations of Ihh (bottom to top: 15, 30, 60, 120 and 240 nM) were injected on the surface of flow cells. The nonspecific binding was subtracted from the sensogram. Inset: ka , kd and Kd values were determined using a 1:1 Languimuir binding model. Each value is expressed as the mean±s.e. of five different concentrations. ( D ) GPC3 inhibits Hh signalling independently of CDO and HIP. Top: NIH 3T3 cells were transfected with a GPC3 or EF along with a luciferase reporter vector driven by an Hh responsive promoter (8Xgli) and β-galactosidase. As indicated, siRNA for silencing CDO siRNA, HIP siRNA or non-targeting control siRNA was also transfected. Cells were stimulated for 48 h with Shh- or control-conditioned medium and luciferase and β-galactosidase assays carried out. For each siRNA condition, the fold stimulation induced by Hh in EF-transfected cells was considered to be 100%. Bars represent the luciferase activity as percentage of the control (average+s.d. of triplicates). Bottom: Western blot for CDO and HIP in NIH 3T3 cells treated as indicated, using actin as loading control. ( E , F ) Increased Ihh levels in GPC3-null mice. ( E ) Western blot analysis of Ihh levels in whole-embryo lysates using actin as loading control was carried out. Bands were then scanned and quantified by densitometry. Average density+s.d. of Ihh/actin ratio is shown. In all three independent litters were analysed. ( F ) Relative levels of Ihh transcripts determined by real-time PCR using β-actin transcript levels as reference. Two independent litters were analysed. Bars represent mean+s.d. for the indicated genotypes. CDO, CAM-related/downregulated by oncogenes; EF, elongation factor; GPC3, Glypican 3; Hh, hedgehog; HIP, Hedgehog-interacting protein; Ihh, Indian hedgehog; mRNA, messenger RNA; PCR, polymerase chain reaction; RU, relative units; Shh, sonic hedgehog; siRNA, small interference RNA; SRP, small plasmon resonance; WT, wild type.

    Journal: EMBO Reports

    Article Title: Overgrowth of a mouse model of Simpson- Golabi-Behmel syndrome is partly mediated by Indian Hedgehog

    doi: 10.1038/embor.2009.98

    Figure Lengend Snippet: Characterization and consequences of GPC3–lhh interaction. ( A – C ) Ihh binds to GPC3. ( A ) Binding of 125 I-Ihh to human embryonic kidney (HEK)293T cells transfected with GPC3 expressing vector or vector controls (EF). A representative experiment of three is shown: points, average of triplicates; bars, ±s.d. ( B ) The specific binding of 125 I-Ihh to HEK293T cells transfected with GPC3 or EF was determined in the presence of 100 × unlabelled Ihh. Bars: average of triplicates+s.d.; asterisk: statistically significant difference. ( C ) SRP analysis of the GPC3–Ihh interaction. GPC3ΔGPI was immobilized in the flow cell into streptavidin-coated SA sensor chips, and various concentrations of Ihh (bottom to top: 15, 30, 60, 120 and 240 nM) were injected on the surface of flow cells. The nonspecific binding was subtracted from the sensogram. Inset: ka , kd and Kd values were determined using a 1:1 Languimuir binding model. Each value is expressed as the mean±s.e. of five different concentrations. ( D ) GPC3 inhibits Hh signalling independently of CDO and HIP. Top: NIH 3T3 cells were transfected with a GPC3 or EF along with a luciferase reporter vector driven by an Hh responsive promoter (8Xgli) and β-galactosidase. As indicated, siRNA for silencing CDO siRNA, HIP siRNA or non-targeting control siRNA was also transfected. Cells were stimulated for 48 h with Shh- or control-conditioned medium and luciferase and β-galactosidase assays carried out. For each siRNA condition, the fold stimulation induced by Hh in EF-transfected cells was considered to be 100%. Bars represent the luciferase activity as percentage of the control (average+s.d. of triplicates). Bottom: Western blot for CDO and HIP in NIH 3T3 cells treated as indicated, using actin as loading control. ( E , F ) Increased Ihh levels in GPC3-null mice. ( E ) Western blot analysis of Ihh levels in whole-embryo lysates using actin as loading control was carried out. Bands were then scanned and quantified by densitometry. Average density+s.d. of Ihh/actin ratio is shown. In all three independent litters were analysed. ( F ) Relative levels of Ihh transcripts determined by real-time PCR using β-actin transcript levels as reference. Two independent litters were analysed. Bars represent mean+s.d. for the indicated genotypes. CDO, CAM-related/downregulated by oncogenes; EF, elongation factor; GPC3, Glypican 3; Hh, hedgehog; HIP, Hedgehog-interacting protein; Ihh, Indian hedgehog; mRNA, messenger RNA; PCR, polymerase chain reaction; RU, relative units; Shh, sonic hedgehog; siRNA, small interference RNA; SRP, small plasmon resonance; WT, wild type.

    Article Snippet: To silence CDO or HIP, 100 nM of CDO siRNA (sc-60346, Santa Cruz), HIP siRNA (sc-40164, Santa Cruz) or non-targeting control siRNA A (sc-37007, Santa Cruz) was transfected using DharmaFECT-1 transfection reagent (Dharmacon, Chicago, IL, USA). β-Galactosidase activity was used to normalize the transfection efficiencies.

    Techniques: Binding Assay, Transfection, Expressing, Plasmid Preparation, Flow Cytometry, Injection, Luciferase, Activity Assay, Western Blot, Mouse Assay, Real-time Polymerase Chain Reaction, Chick Chorioallantoic Membrane Assay, Polymerase Chain Reaction