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( a ) In situ hybridization analysis of Ncan mRNA on the E16.5 cerebral cortex. ( b ) Localization of NCAN protein (green) in the E16.5 cerebral cortex. Nuclei were counterstained with DAPI (blue). ( c ) Distribution of HA (green) visualized by the biotinylated HA-binding protein (b-HABP) in the E16.5 cerebral cortex. ( d ) High-magnification views of a <t>Tuj-1-positive</t> primary cultured cortical neuron (green) 5 days after plating. White arrows indicate the co-localization of NCAN (magenta) and HA (cyan). Orthogonal projections in the X-Z and Y-Z planes taken along the white lines showed the localization of NCAN and HA at the adhesion sites between the neuron and culture substrate. ( e ) Schema of the pull-down assay for analyzing binding between endogenous HA and its interactors. ( f ) Immunoblotting of the input, precipitate (P), and supernatant (S) with an anti-NCAN antibody. NCAN was precipitated with HA by adding b-HABP (b-HABP +). NCAN was not precipitated without b-HABP (b-HABP -) or after digestion with hyaluronidase (HAase +). ( g ) Co-precipitation of NCAN with exogenously added biotinylated HA (b-HA +) or endogenous HA (b-HABP +). Scale bars represent 200 μm ( a–c ) and 5 μm ( d ). Figure 2—source data 1. Original blots for .
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( a ) In situ hybridization analysis of Ncan mRNA on the E16.5 cerebral cortex. ( b ) Localization of NCAN protein (green) in the E16.5 cerebral cortex. Nuclei were counterstained with DAPI (blue). ( c ) Distribution of HA (green) visualized by the biotinylated HA-binding protein (b-HABP) in the E16.5 cerebral cortex. ( d ) High-magnification views of a <t>Tuj-1-positive</t> primary cultured cortical neuron (green) 5 days after plating. White arrows indicate the co-localization of NCAN (magenta) and HA (cyan). Orthogonal projections in the X-Z and Y-Z planes taken along the white lines showed the localization of NCAN and HA at the adhesion sites between the neuron and culture substrate. ( e ) Schema of the pull-down assay for analyzing binding between endogenous HA and its interactors. ( f ) Immunoblotting of the input, precipitate (P), and supernatant (S) with an anti-NCAN antibody. NCAN was precipitated with HA by adding b-HABP (b-HABP +). NCAN was not precipitated without b-HABP (b-HABP -) or after digestion with hyaluronidase (HAase +). ( g ) Co-precipitation of NCAN with exogenously added biotinylated HA (b-HA +) or endogenous HA (b-HABP +). Scale bars represent 200 μm ( a–c ) and 5 μm ( d ). Figure 2—source data 1. Original blots for .
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( a ) In situ hybridization analysis of Ncan mRNA on the E16.5 cerebral cortex. ( b ) Localization of NCAN protein (green) in the E16.5 cerebral cortex. Nuclei were counterstained with DAPI (blue). ( c ) Distribution of HA (green) visualized by the biotinylated HA-binding protein (b-HABP) in the E16.5 cerebral cortex. ( d ) High-magnification views of a Tuj-1-positive primary cultured cortical neuron (green) 5 days after plating. White arrows indicate the co-localization of NCAN (magenta) and HA (cyan). Orthogonal projections in the X-Z and Y-Z planes taken along the white lines showed the localization of NCAN and HA at the adhesion sites between the neuron and culture substrate. ( e ) Schema of the pull-down assay for analyzing binding between endogenous HA and its interactors. ( f ) Immunoblotting of the input, precipitate (P), and supernatant (S) with an anti-NCAN antibody. NCAN was precipitated with HA by adding b-HABP (b-HABP +). NCAN was not precipitated without b-HABP (b-HABP -) or after digestion with hyaluronidase (HAase +). ( g ) Co-precipitation of NCAN with exogenously added biotinylated HA (b-HA +) or endogenous HA (b-HABP +). Scale bars represent 200 μm ( a–c ) and 5 μm ( d ). Figure 2—source data 1. Original blots for .

Journal: eLife

Article Title: Assembly of neuron- and radial glial-cell-derived extracellular matrix molecules promotes radial migration of developing cortical neurons

doi: 10.7554/eLife.92342

Figure Lengend Snippet: ( a ) In situ hybridization analysis of Ncan mRNA on the E16.5 cerebral cortex. ( b ) Localization of NCAN protein (green) in the E16.5 cerebral cortex. Nuclei were counterstained with DAPI (blue). ( c ) Distribution of HA (green) visualized by the biotinylated HA-binding protein (b-HABP) in the E16.5 cerebral cortex. ( d ) High-magnification views of a Tuj-1-positive primary cultured cortical neuron (green) 5 days after plating. White arrows indicate the co-localization of NCAN (magenta) and HA (cyan). Orthogonal projections in the X-Z and Y-Z planes taken along the white lines showed the localization of NCAN and HA at the adhesion sites between the neuron and culture substrate. ( e ) Schema of the pull-down assay for analyzing binding between endogenous HA and its interactors. ( f ) Immunoblotting of the input, precipitate (P), and supernatant (S) with an anti-NCAN antibody. NCAN was precipitated with HA by adding b-HABP (b-HABP +). NCAN was not precipitated without b-HABP (b-HABP -) or after digestion with hyaluronidase (HAase +). ( g ) Co-precipitation of NCAN with exogenously added biotinylated HA (b-HA +) or endogenous HA (b-HABP +). Scale bars represent 200 μm ( a–c ) and 5 μm ( d ). Figure 2—source data 1. Original blots for .

Article Snippet: Antibody , Anti-β-Tubulin (Tuj-1) Mouse IgG1(clone TUB 2.1) , Sigma , T4026 RRID: AB_477577 , IF(1:1000).

Techniques: In Situ Hybridization, Binding Assay, Cell Culture, Pull Down Assay, Western Blot

Journal: eLife

Article Title: Assembly of neuron- and radial glial-cell-derived extracellular matrix molecules promotes radial migration of developing cortical neurons

doi: 10.7554/eLife.92342

Figure Lengend Snippet:

Article Snippet: Antibody , Anti-β-Tubulin (Tuj-1) Mouse IgG1(clone TUB 2.1) , Sigma , T4026 RRID: AB_477577 , IF(1:1000).

Techniques: Recombinant, Plasmid Preparation, Sequencing, BIA-KA, SYBR Green Assay, Labeling, Clone Assay, Mutagenesis, Software, Protease Inhibitor, Magnetic Beads, Membrane, Western Blot, Enzyme-linked Immunosorbent Assay, Blocking Assay, Binding Assay, Chromatography, Laser-Scanning Microscopy, Fluorescence, Real-time Polymerase Chain Reaction, Mass Spectrometry