landseer dog Search Results


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  • 99
    Thermo Fisher protein g agarose beads
    Protein G Agarose Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3716 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protein g agarose beads/product/Thermo Fisher
    Average 99 stars, based on 3716 article reviews
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    protein g agarose beads - by Bioz Stars, 2020-08
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    94
    Millipore monoclonal anti plakoglobin catenin gamma antibody
    Monoclonal Anti Plakoglobin Catenin Gamma Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 57 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal anti plakoglobin catenin gamma antibody/product/Millipore
    Average 94 stars, based on 57 article reviews
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    92
    Becton Dickinson anti p120 catenin tritc
    Loss of <t>α‐catenin</t> induces loss of epithelial cell morphology and leads to aberrant localization of AJ members. (A) Inducible knockdown of α‐catenin (α‐cat iKD) does not lead to inhibition of AJ complex member expression levels. Western blot showing the extent of α‐catenin iKD (+ Dox) on E‐cadherin, <t>p120,</t> and β‐catenin. Right lanes (+ Rescue) show the effects of an α‐catenin‐GFP cDNA reconstitution. Gapdh levels were used as loading control. (B) Loss of α‐catenin induces a rounded and non‐adherent cell morphology. Phase‐contrast images of α‐catenin iKD and rescue cell lines. Scale bar = 50 μm. (C) Dysfunctional formation of the AJ upon α‐catenin loss. Immunofluorescence images for the AJ complex members α‐catenin, E‐cadherin, p120, and β‐catenin in control (− Dox), α‐catenin iKD (+ Dox), and Rescue cells (+ Rescue) are shown. Note the distinct clustering of the AJ in membrane‐localized puncta upon α‐catenin loss (arrows) and the cytosolic localization of E‐cadherin (arrowheads). Scale bar = 10 μm.
    Anti P120 Catenin Tritc, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p120 catenin tritc/product/Becton Dickinson
    Average 92 stars, based on 8 article reviews
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    88
    Waters Corporation european continent
    Loss of <t>α‐catenin</t> induces loss of epithelial cell morphology and leads to aberrant localization of AJ members. (A) Inducible knockdown of α‐catenin (α‐cat iKD) does not lead to inhibition of AJ complex member expression levels. Western blot showing the extent of α‐catenin iKD (+ Dox) on E‐cadherin, <t>p120,</t> and β‐catenin. Right lanes (+ Rescue) show the effects of an α‐catenin‐GFP cDNA reconstitution. Gapdh levels were used as loading control. (B) Loss of α‐catenin induces a rounded and non‐adherent cell morphology. Phase‐contrast images of α‐catenin iKD and rescue cell lines. Scale bar = 50 μm. (C) Dysfunctional formation of the AJ upon α‐catenin loss. Immunofluorescence images for the AJ complex members α‐catenin, E‐cadherin, p120, and β‐catenin in control (− Dox), α‐catenin iKD (+ Dox), and Rescue cells (+ Rescue) are shown. Note the distinct clustering of the AJ in membrane‐localized puncta upon α‐catenin loss (arrows) and the cytosolic localization of E‐cadherin (arrowheads). Scale bar = 10 μm.
    European Continent, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/european continent/product/Waters Corporation
    Average 88 stars, based on 1 article reviews
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    91
    Illumina Inc 300 bp insert size
    Loss of <t>α‐catenin</t> induces loss of epithelial cell morphology and leads to aberrant localization of AJ members. (A) Inducible knockdown of α‐catenin (α‐cat iKD) does not lead to inhibition of AJ complex member expression levels. Western blot showing the extent of α‐catenin iKD (+ Dox) on E‐cadherin, <t>p120,</t> and β‐catenin. Right lanes (+ Rescue) show the effects of an α‐catenin‐GFP cDNA reconstitution. Gapdh levels were used as loading control. (B) Loss of α‐catenin induces a rounded and non‐adherent cell morphology. Phase‐contrast images of α‐catenin iKD and rescue cell lines. Scale bar = 50 μm. (C) Dysfunctional formation of the AJ upon α‐catenin loss. Immunofluorescence images for the AJ complex members α‐catenin, E‐cadherin, p120, and β‐catenin in control (− Dox), α‐catenin iKD (+ Dox), and Rescue cells (+ Rescue) are shown. Note the distinct clustering of the AJ in membrane‐localized puncta upon α‐catenin loss (arrows) and the cytosolic localization of E‐cadherin (arrowheads). Scale bar = 10 μm.
    300 Bp Insert Size, supplied by Illumina Inc, used in various techniques. Bioz Stars score: 91/100, based on 80 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/300 bp insert size/product/Illumina Inc
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    89
    Illumina Inc hiseq2500 paired end reads
    Loss of <t>α‐catenin</t> induces loss of epithelial cell morphology and leads to aberrant localization of AJ members. (A) Inducible knockdown of α‐catenin (α‐cat iKD) does not lead to inhibition of AJ complex member expression levels. Western blot showing the extent of α‐catenin iKD (+ Dox) on E‐cadherin, <t>p120,</t> and β‐catenin. Right lanes (+ Rescue) show the effects of an α‐catenin‐GFP cDNA reconstitution. Gapdh levels were used as loading control. (B) Loss of α‐catenin induces a rounded and non‐adherent cell morphology. Phase‐contrast images of α‐catenin iKD and rescue cell lines. Scale bar = 50 μm. (C) Dysfunctional formation of the AJ upon α‐catenin loss. Immunofluorescence images for the AJ complex members α‐catenin, E‐cadherin, p120, and β‐catenin in control (− Dox), α‐catenin iKD (+ Dox), and Rescue cells (+ Rescue) are shown. Note the distinct clustering of the AJ in membrane‐localized puncta upon α‐catenin loss (arrows) and the cytosolic localization of E‐cadherin (arrowheads). Scale bar = 10 μm.
    Hiseq2500 Paired End Reads, supplied by Illumina Inc, used in various techniques. Bioz Stars score: 89/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hiseq2500 paired end reads/product/Illumina Inc
    Average 89 stars, based on 30 article reviews
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    88
    Illumina Inc polymerase chain reaction pcr free fragment library
    Electropherograms of the COL6A1:c.289G > T variant. A fragment harboring exon 3 and flanking sequences of the COL6A1 gene was amplified by polymerase chain reaction and sequenced with the Sanger method. Shown are representative traces from <t>Landseer</t> dogs with the three different genotypes. The position of the variant is indicated by an arrow.
    Polymerase Chain Reaction Pcr Free Fragment Library, supplied by Illumina Inc, used in various techniques. Bioz Stars score: 88/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polymerase chain reaction pcr free fragment library/product/Illumina Inc
    Average 88 stars, based on 9 article reviews
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    96
    PeproTech human recombinant tgfβ1
    Spectrins do not regulate αSMA stress fiber formation. (a) mRNA expression of ACTA2 (αSMA) after 4 days of stimulation with <t>TGFβ1</t> on αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) KD cells. Two-way ANOVA; ** p
    Human Recombinant Tgfβ1, supplied by PeproTech, used in various techniques. Bioz Stars score: 96/100, based on 79 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 96 stars, based on 79 article reviews
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    Image Search Results


    Loss of α‐catenin induces loss of epithelial cell morphology and leads to aberrant localization of AJ members. (A) Inducible knockdown of α‐catenin (α‐cat iKD) does not lead to inhibition of AJ complex member expression levels. Western blot showing the extent of α‐catenin iKD (+ Dox) on E‐cadherin, p120, and β‐catenin. Right lanes (+ Rescue) show the effects of an α‐catenin‐GFP cDNA reconstitution. Gapdh levels were used as loading control. (B) Loss of α‐catenin induces a rounded and non‐adherent cell morphology. Phase‐contrast images of α‐catenin iKD and rescue cell lines. Scale bar = 50 μm. (C) Dysfunctional formation of the AJ upon α‐catenin loss. Immunofluorescence images for the AJ complex members α‐catenin, E‐cadherin, p120, and β‐catenin in control (− Dox), α‐catenin iKD (+ Dox), and Rescue cells (+ Rescue) are shown. Note the distinct clustering of the AJ in membrane‐localized puncta upon α‐catenin loss (arrows) and the cytosolic localization of E‐cadherin (arrowheads). Scale bar = 10 μm.

    Journal: The Journal of Pathology

    Article Title: αE‐catenin is a candidate tumor suppressor for the development of E‐cadherin‐expressing lobular‐type breast cancer

    doi: 10.1002/path.5099

    Figure Lengend Snippet: Loss of α‐catenin induces loss of epithelial cell morphology and leads to aberrant localization of AJ members. (A) Inducible knockdown of α‐catenin (α‐cat iKD) does not lead to inhibition of AJ complex member expression levels. Western blot showing the extent of α‐catenin iKD (+ Dox) on E‐cadherin, p120, and β‐catenin. Right lanes (+ Rescue) show the effects of an α‐catenin‐GFP cDNA reconstitution. Gapdh levels were used as loading control. (B) Loss of α‐catenin induces a rounded and non‐adherent cell morphology. Phase‐contrast images of α‐catenin iKD and rescue cell lines. Scale bar = 50 μm. (C) Dysfunctional formation of the AJ upon α‐catenin loss. Immunofluorescence images for the AJ complex members α‐catenin, E‐cadherin, p120, and β‐catenin in control (− Dox), α‐catenin iKD (+ Dox), and Rescue cells (+ Rescue) are shown. Note the distinct clustering of the AJ in membrane‐localized puncta upon α‐catenin loss (arrows) and the cytosolic localization of E‐cadherin (arrowheads). Scale bar = 10 μm.

    Article Snippet: Samples were incubated with antibodies against α‐catenin (1:1000; Sigma‐Aldrich; C2081), or clone 15D1 (1:100; Enzo Life Sciences, Farmingdale, NY, USA; Alx‐804‐101), anti‐E‐cadherin‐TRITC (1:300; BD Biosciences; 612130), anti‐p120‐catenin‐TRITC (1:300; BD Biosciences; 610137) or mouse anti‐β‐catenin (1:50; BD Biosciences; 610154) overnight at 4 °C.

    Techniques: Inhibition, Expressing, Western Blot, Immunofluorescence

    Electropherograms of the COL6A1:c.289G > T variant. A fragment harboring exon 3 and flanking sequences of the COL6A1 gene was amplified by polymerase chain reaction and sequenced with the Sanger method. Shown are representative traces from Landseer dogs with the three different genotypes. The position of the variant is indicated by an arrow.

    Journal: G3: Genes|Genomes|Genetics

    Article Title: A Nonsense Variant in COL6A1 in Landseer Dogs with Muscular Dystrophy

    doi: 10.1534/g3.115.021923

    Figure Lengend Snippet: Electropherograms of the COL6A1:c.289G > T variant. A fragment harboring exon 3 and flanking sequences of the COL6A1 gene was amplified by polymerase chain reaction and sequenced with the Sanger method. Shown are representative traces from Landseer dogs with the three different genotypes. The position of the variant is indicated by an arrow.

    Article Snippet: Whole-genome sequencing of an affected Landseer dog We prepared a polymerase chain reaction (PCR)-free fragment library with 300-bp insert size and collected 330,331,465 Illumina HiSeq2500 paired-end reads (2 × 100 bp) or roughly 14.2× coverage.

    Techniques: Variant Assay, Amplification, Polymerase Chain Reaction

    Spectrins do not regulate αSMA stress fiber formation. (a) mRNA expression of ACTA2 (αSMA) after 4 days of stimulation with TGFβ1 on αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) KD cells. Two-way ANOVA; ** p

    Journal: Cell and Tissue Research

    Article Title: αII-spectrin and βII-spectrin do not affect TGFβ1-induced myofibroblast differentiation

    doi: 10.1007/s00441-018-2842-x

    Figure Lengend Snippet: Spectrins do not regulate αSMA stress fiber formation. (a) mRNA expression of ACTA2 (αSMA) after 4 days of stimulation with TGFβ1 on αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) KD cells. Two-way ANOVA; ** p

    Article Snippet: Reagents were as follows: human plasma fibronectin (20 μg/mL, F1056; Sigma-Aldrich, Munich, Germany), human recombinant TGFβ1 (10 ng/mL, 100-21C; Peprotech, London, UK), αII-spectrin siRNA (25 ng/cm2 , EHU093741; Sigma-Aldrich), βII-spectrin siRNA (25 ng/cm2 , EHU081451; Sigma-Aldrich), Renilla luciferase siRNA (25 ng/cm2 , EHURLUC; Sigma-Aldrich), Alexa647-labeled streptavidin (8 μg/mL, ; Thermo Fisher Scientific, Landsmeer, The Netherlands), TRITC labeled-Phalloidin (100 nM, P1951; Sigma-Aldrich).

    Techniques: Expressing

    TGFβ1 stimulation decreases αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) gene expression. a , b mRNA expression of αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) after TGFβ1 stimulation. Two-way ANOVA; * p

    Journal: Cell and Tissue Research

    Article Title: αII-spectrin and βII-spectrin do not affect TGFβ1-induced myofibroblast differentiation

    doi: 10.1007/s00441-018-2842-x

    Figure Lengend Snippet: TGFβ1 stimulation decreases αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) gene expression. a , b mRNA expression of αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) after TGFβ1 stimulation. Two-way ANOVA; * p

    Article Snippet: Reagents were as follows: human plasma fibronectin (20 μg/mL, F1056; Sigma-Aldrich, Munich, Germany), human recombinant TGFβ1 (10 ng/mL, 100-21C; Peprotech, London, UK), αII-spectrin siRNA (25 ng/cm2 , EHU093741; Sigma-Aldrich), βII-spectrin siRNA (25 ng/cm2 , EHU081451; Sigma-Aldrich), Renilla luciferase siRNA (25 ng/cm2 , EHURLUC; Sigma-Aldrich), Alexa647-labeled streptavidin (8 μg/mL, ; Thermo Fisher Scientific, Landsmeer, The Netherlands), TRITC labeled-Phalloidin (100 nM, P1951; Sigma-Aldrich).

    Techniques: Expressing

    Spectrins do not regulate collagen type I synthesis. (a) mRNA expression of COL1A1 after 4 days of stimulation with TGFβ1 on αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) KD cells. Two-way ANOVA; * p

    Journal: Cell and Tissue Research

    Article Title: αII-spectrin and βII-spectrin do not affect TGFβ1-induced myofibroblast differentiation

    doi: 10.1007/s00441-018-2842-x

    Figure Lengend Snippet: Spectrins do not regulate collagen type I synthesis. (a) mRNA expression of COL1A1 after 4 days of stimulation with TGFβ1 on αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) KD cells. Two-way ANOVA; * p

    Article Snippet: Reagents were as follows: human plasma fibronectin (20 μg/mL, F1056; Sigma-Aldrich, Munich, Germany), human recombinant TGFβ1 (10 ng/mL, 100-21C; Peprotech, London, UK), αII-spectrin siRNA (25 ng/cm2 , EHU093741; Sigma-Aldrich), βII-spectrin siRNA (25 ng/cm2 , EHU081451; Sigma-Aldrich), Renilla luciferase siRNA (25 ng/cm2 , EHURLUC; Sigma-Aldrich), Alexa647-labeled streptavidin (8 μg/mL, ; Thermo Fisher Scientific, Landsmeer, The Netherlands), TRITC labeled-Phalloidin (100 nM, P1951; Sigma-Aldrich).

    Techniques: Expressing

    αII- and βII-spectrin do not control vinculin adhesions. (a–f) Representative immunofluorescent images of vinculin after 4 days of stimulation with TGFβ1 in αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) KD cells. Original magnification × 200. DAPI, 4′,6-diamidino-2-phenylindole; TGF, transforming growth factor

    Journal: Cell and Tissue Research

    Article Title: αII-spectrin and βII-spectrin do not affect TGFβ1-induced myofibroblast differentiation

    doi: 10.1007/s00441-018-2842-x

    Figure Lengend Snippet: αII- and βII-spectrin do not control vinculin adhesions. (a–f) Representative immunofluorescent images of vinculin after 4 days of stimulation with TGFβ1 in αII-spectrin ( SPTAN1 ) and βII-spectrin ( SPTBN1 ) KD cells. Original magnification × 200. DAPI, 4′,6-diamidino-2-phenylindole; TGF, transforming growth factor

    Article Snippet: Reagents were as follows: human plasma fibronectin (20 μg/mL, F1056; Sigma-Aldrich, Munich, Germany), human recombinant TGFβ1 (10 ng/mL, 100-21C; Peprotech, London, UK), αII-spectrin siRNA (25 ng/cm2 , EHU093741; Sigma-Aldrich), βII-spectrin siRNA (25 ng/cm2 , EHU081451; Sigma-Aldrich), Renilla luciferase siRNA (25 ng/cm2 , EHURLUC; Sigma-Aldrich), Alexa647-labeled streptavidin (8 μg/mL, ; Thermo Fisher Scientific, Landsmeer, The Netherlands), TRITC labeled-Phalloidin (100 nM, P1951; Sigma-Aldrich).

    Techniques:

    αII- and βII-spectrin do not influence wound gap closure. (a–l) Cells seeded at high density were left to repopulate the wound gap for 24 h in the presence or absence of TGFβ1 stimulation. (m) Quantification of panels a–l. Original magnification × 100. TGF, transforming growth factor

    Journal: Cell and Tissue Research

    Article Title: αII-spectrin and βII-spectrin do not affect TGFβ1-induced myofibroblast differentiation

    doi: 10.1007/s00441-018-2842-x

    Figure Lengend Snippet: αII- and βII-spectrin do not influence wound gap closure. (a–l) Cells seeded at high density were left to repopulate the wound gap for 24 h in the presence or absence of TGFβ1 stimulation. (m) Quantification of panels a–l. Original magnification × 100. TGF, transforming growth factor

    Article Snippet: Reagents were as follows: human plasma fibronectin (20 μg/mL, F1056; Sigma-Aldrich, Munich, Germany), human recombinant TGFβ1 (10 ng/mL, 100-21C; Peprotech, London, UK), αII-spectrin siRNA (25 ng/cm2 , EHU093741; Sigma-Aldrich), βII-spectrin siRNA (25 ng/cm2 , EHU081451; Sigma-Aldrich), Renilla luciferase siRNA (25 ng/cm2 , EHURLUC; Sigma-Aldrich), Alexa647-labeled streptavidin (8 μg/mL, ; Thermo Fisher Scientific, Landsmeer, The Netherlands), TRITC labeled-Phalloidin (100 nM, P1951; Sigma-Aldrich).

    Techniques: