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scanning electron micrograph  (Hitachi Ltd)


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    Structured Review

    Hitachi Ltd scanning electron micrograph
    Scanning Electron Micrograph, supplied by Hitachi Ltd, used in various techniques. Bioz Stars score: 99/100, based on 20547 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/electron+micrographs/TM4000/pmc13162467-155-7-11
    Average 99 stars, based on 20547 article reviews
    scanning electron micrograph - by Bioz Stars, 2026-10
    99/100 stars

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    Related Articles

    Microscopy:

    Article Title: Activated Carbon Fiber Incorporated with Metal Ions: Characterization and Biological Interactions In Vitro.
    Article Snippet: .. The samples were analyzed using a Hitachi TM4000 Plus scanning electron microscope (Hitachi, Tokyo, Japan). ..

    Article Title: Development and Optimisation of an Industrial Waste-Based Additive for Improving Concrete Performance.
    Article Snippet: .. In this experiment, the analysis was performed using SEM micrographs obtained with a tabletop TM4000Plus scanning electron microscope (Hitachi, Tokyo, Japan), operating at an accelerating voltage of up to 20 kV, with a magnification range of 10× to 25,000× and a resolution of 3.5 nm for W. Evaluating the changes in composition resulting from the addition of different components is necessary to assess the performance of the additive and determine its potential suitability for improving the physicochemical properties of cement. https://doi.org/10.3390/ma19091698 The compressive and flexural strength of the samples were measured using a Press Automatic Pilot Controls machine (Milan, Italy) with a maximum compressive load of 500 kN (50 tons) at 7, 14, and 28 days, in accordance with GOST 310.4 [31] and EN 196- 1:2016 [32] (Figure 1b,c). ..

    Article Title: Incorporating air-classified quinoa flour in high moisture extruded meat analogues: Instrumental insights
    Article Snippet: .. The dried samples were mounted onto double-sided adhesive carbon stubs and examined using a Hitachi benchtop SEM TM4000Plus scanning electron microscope (Hitachi High-Tech, Tokyo, Japan). ..

    Electron Microscopy:

    Article Title: Magnetic Biocomposite Based on Aspen Biochar, Sodium Alginate, and Phaffia rhodozyma Yeast for Efficient Removal of Methylene Blue from Aqueous Solutions.
    Article Snippet: .. The surface morphology and degree of porosity development of the resulting biocomposite were analyzed using scanning electron microscopy (SEM) (Hitachi TM-3000, Tokyo, Japan). ..

    Imaging:

    Article Title: Conductive ionic liquid hydrogel filled anti-inflammatory nerve conduit repairs peripheral nerve defect
    Article Snippet: .. Before imaging using a Hitachi TM-1000 (Japan), nanofibers and hydrogels were lyophilized and then coated with gold by sputter deposition for 60 s. Statistical analysis of the fiber diameters of each group was based on measurements of at least 100 randomly selected fibers from SEM images. ..

    Adhesive:

    Article Title: Incorporating air-classified quinoa flour in high moisture extruded meat analogues: Instrumental insights
    Article Snippet: .. The dried samples were mounted onto double-sided adhesive carbon stubs and examined using a Hitachi benchtop SEM TM4000Plus scanning electron microscope (Hitachi High-Tech, Tokyo, Japan). ..



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    JEOL cryo tem micrographs
    Characterization and ATX-scavenging activity of AS-Lipo@R. <t>(A)</t> <t>Cryo-TEM</t> images of Lipo and AS-Lipo (scale bar, 100 nm). (B) Particle size and zeta potential of Lipo and AS-Lipo measured by DLS. (C) Colloidal stability of Lipo and AS-Lipo was evaluated by monitoring changes in particle size and zeta potential over 72 h in PBS using DLS. (D) Concentration-dependent inhibition of recombinant mouse ATX activity as a function of BMP-22 concentration in free BMP-22, Lipo, and AS-Lipo, evaluated using a choline release assay. (E) ATX binding to the surface of Lipo and AS-Lipo as a function of ATX concentration, quantified by ELISA. (F) HPLC chromatograms showing rapamycin (R) encapsulation in AS-Lipo@R, as indicated by the disappearance of the free R peak. (G) Cumulative release profiles of rapamycin from Lipo@R and AS-Lipo@R in PBS over 72 h measured by HPLC. (H) Fluorescence imaging showing colocalization of DiO-labeled Lipo or AS-Lipo (green), Alexa Fluor 647 (AF647)-labeled ATX (red), and LysoTracker (purple) in RAW 264.7 macrophages. AS-Lipo-bound ATX is internalized and colocalizes with lysosomes, indicating lysosomal degradation. Right panels show fluorescence intensity profiles along the indicated lines, quantifying the colocalization (scale bar, 100 and 50 μm). Statistical significance was determined by one-way ANOVA with Tukey’s post hoc test ( n = 3). * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001.
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    Image Search Results


    Characterization and ATX-scavenging activity of AS-Lipo@R. (A) Cryo-TEM images of Lipo and AS-Lipo (scale bar, 100 nm). (B) Particle size and zeta potential of Lipo and AS-Lipo measured by DLS. (C) Colloidal stability of Lipo and AS-Lipo was evaluated by monitoring changes in particle size and zeta potential over 72 h in PBS using DLS. (D) Concentration-dependent inhibition of recombinant mouse ATX activity as a function of BMP-22 concentration in free BMP-22, Lipo, and AS-Lipo, evaluated using a choline release assay. (E) ATX binding to the surface of Lipo and AS-Lipo as a function of ATX concentration, quantified by ELISA. (F) HPLC chromatograms showing rapamycin (R) encapsulation in AS-Lipo@R, as indicated by the disappearance of the free R peak. (G) Cumulative release profiles of rapamycin from Lipo@R and AS-Lipo@R in PBS over 72 h measured by HPLC. (H) Fluorescence imaging showing colocalization of DiO-labeled Lipo or AS-Lipo (green), Alexa Fluor 647 (AF647)-labeled ATX (red), and LysoTracker (purple) in RAW 264.7 macrophages. AS-Lipo-bound ATX is internalized and colocalizes with lysosomes, indicating lysosomal degradation. Right panels show fluorescence intensity profiles along the indicated lines, quantifying the colocalization (scale bar, 100 and 50 μm). Statistical significance was determined by one-way ANOVA with Tukey’s post hoc test ( n = 3). * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001.

    Journal: Biomaterials Research

    Article Title: Autotaxin-Scavenging Nanoliposomes for Prolonged Colon Retention and Autophagy-Mediated Mucosal Immune Restoration in Colitis

    doi: 10.34133/bmr.0345

    Figure Lengend Snippet: Characterization and ATX-scavenging activity of AS-Lipo@R. (A) Cryo-TEM images of Lipo and AS-Lipo (scale bar, 100 nm). (B) Particle size and zeta potential of Lipo and AS-Lipo measured by DLS. (C) Colloidal stability of Lipo and AS-Lipo was evaluated by monitoring changes in particle size and zeta potential over 72 h in PBS using DLS. (D) Concentration-dependent inhibition of recombinant mouse ATX activity as a function of BMP-22 concentration in free BMP-22, Lipo, and AS-Lipo, evaluated using a choline release assay. (E) ATX binding to the surface of Lipo and AS-Lipo as a function of ATX concentration, quantified by ELISA. (F) HPLC chromatograms showing rapamycin (R) encapsulation in AS-Lipo@R, as indicated by the disappearance of the free R peak. (G) Cumulative release profiles of rapamycin from Lipo@R and AS-Lipo@R in PBS over 72 h measured by HPLC. (H) Fluorescence imaging showing colocalization of DiO-labeled Lipo or AS-Lipo (green), Alexa Fluor 647 (AF647)-labeled ATX (red), and LysoTracker (purple) in RAW 264.7 macrophages. AS-Lipo-bound ATX is internalized and colocalizes with lysosomes, indicating lysosomal degradation. Right panels show fluorescence intensity profiles along the indicated lines, quantifying the colocalization (scale bar, 100 and 50 μm). Statistical significance was determined by one-way ANOVA with Tukey’s post hoc test ( n = 3). * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001.

    Article Snippet: Cryo-TEM micrographs were acquired using a JEM-2100F electron microscope (JEOL, Japan).

    Techniques: Activity Assay, Zeta Potential Analyzer, Concentration Assay, Inhibition, Recombinant, Release Assay, Binding Assay, Enzyme-linked Immunosorbent Assay, Encapsulation, Fluorescence, Imaging, Labeling