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Jem 1210 electron microscope

Manufactured by JEOL
Sourced in Japan

The JEM-1210 is a high-performance transmission electron microscope (TEM) manufactured by JEOL. It is designed to provide high-resolution imaging and analysis of a wide range of materials at the nanoscale level. The JEM-1210 is equipped with advanced optics and a high-brightness electron source, enabling it to capture detailed images of samples with a resolution up to 0.2 nanometers.

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7 protocols using jem 1210 electron microscope

1

Electron Microscopy Tissue Preparation

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For electron microscopy assessment, the excised specimens were fixed by immersion in 4% paraformaldehyde buffer solution for 4 h at 4°C, and subsequently decalcified in ethylenediaminetetraacetic acid for 3 to 4 days at 4°C. The tissue blocks were cut into 20-μm sections, fixed with 4% paraformaldehyde and 1% glutaraldehyde buffer solution for 30 min at 4°C, and posifixed with 1% OsO4 for 30 min at 4°C. Then, the specimens were stained with 2% uranium acetate for 30 min, dehydrated in a graded ethanol series, and embedded in an epoxy resin based on Glicidether (Selva Feinbiochemica, Heidelberg, Germany). Ultrathin sections (about 70 nm) were prepared using an ultramicrotome, stained with uranium acetate and lead citrate, and subjected to observation using a JEM-1210 electron microscope (JEOL, Tokyo, Japan).
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2

Comprehensive Characterization of Amino Acid-Capped ZnS:Mn Nanoparticles

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The UV/visible spectra in Figure 1a were obtained using a Lamda-25 spectrophotometer (Perkin-Elmer, Waltham, MA, USA), and the room-temperature solution photoluminescence (PL) spectra in Figure 1b were obtained using an LS-45 spectrophotometer (Perkin-Elmer) equipped with a 500 W xenon lamp as a light source. The presented pictures of high-resolution-transmission electron microscopy (HR-TEM in Figures 2 and 3) were obtained using a JEOL JEM 1210 electron microscope, in which the magnification range was from 1000 to 800,000, and the accelerating voltage was from 40 to 120 kV. The powder X-ray diffraction (XRD) pattern diagrams of the NPs presented in Figure 4 were obtained using an X-ray diffractometer, Rigaku 300, which used a Cu-Kα (wavelengths of 1.54 Å) X-ray light source. The elemental analyses for the Gly-ZnS:Mn, Ala-ZnS:Mn, and Val-ZnS:Mn nanoparticles were performed using a Perkin-Elmer Optima-430 ICP-AES spectrometer. The surface capping ligands, i.e., amino acids (Gly, Ala, and Val), were investigated in terms of their specific vibrational modes using Fourier-transform infrared spectroscopy (FT-IR, in Figure 5) recorded using a Spectrum One spectrophotometer (Perkin-Elmer, resolution of 1.0 cm−1) having an attenuated total reflection (ATR) unit. The number of scans was set to 32 for the liquid samples of the NPs.
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3

Ultrastructural Localization of p-Tau in Rat Hippocampus

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LCR and HCR rats were perfused with saline followed by 4% paraformaldehyde in 0.1 mol/L of phosphate buffer. Rat hippocampus tissue was dissected under an operating microscope, mounted in the slot of a small screw, and snap frozen in liquid nitrogen. Ultrathin sections (70–100 nm) from rat hippocampus tissue were incubated concurrently with primary antibodies against p-Tau Ser404 (1:50) or Ser396 (1:50) for 1 h and followed by incubation with appropriate 10 nm immunogold-conjugated secondary antibodies (Jackson ImmunoResearch, Laboratory, West Grove, PA, U.S.A.) for 1 h. Sections were fixed with 2.5% glutaraldehyde, counterstained with 4% neutral uranyl acetate, embedded in 1.25% methyl cellulose, then observed using a JEOL JEM 1210 electron microscope (JEOL USA, Inc, Peabody, MA, U.S.A.) at 80 kV.
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4

Ultrastructural Analysis of Renal Tissue

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Renal tissue samples were harvested. A 1-mm3 renal cortex tissue was taken and fixed with 2.5% glutaraldehyde (Ruinan Biotechnology Center, Shanghai, China) within 1 h. 1 mm3 of renal tissue was obtained from each animal within 1 hour, including a portion of the renal cortex, and fixed in 2.5% glutaraldehyde (Ruinan Biotechnology Center, Shanghai, China). The tissues were then rinsed, fixed in 1% osmium tetroxide solution (Ruinan Biotechnology Center), and dehydrated in an ethanol-acetone series. The sections were then placed in propylene oxide and embedded before they were cut in ultrathin (50 nm) sections, which were double-stained with uranyl acetate and lead citrate, and examined with a JEM-1210 electron microscope (JEOL Ltd., Tokyo, Japan).
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5

In-Depth Nerve Injury Analysis Using SPIONs

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Cell arrival at the injured nerve was assessed 7 DPI using an Olympus BX100 epifluorescence microscope and confirmed through images obtained with an Olympus FV1000 confocal microscope.
For SPIONs size and structural characterization, transmission electron microscopy (TEM) micrographs and electron diffraction (ED) images were obtained with a JEOL JEM 1210 electron microscope operating at 120 kV. For AdMSC-SPIONs and sciatic nerve analyses, images were obtained with JEOL JEM1400 (120 kV) and TEM-Talos F200C (200 kV) electron microscopes and using low dose and a nitrogen sample cryo-holder.
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6

Characterization of SPIONs and BSA Adsorption

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Dynamic light scattering (DLS) and zeta potential measurements were performed with a Zetasizer Nano ZS (Malvern) with a He/Ne 633 nm laser at 25 o C. For each sample, three independent measurements were performed.
Transmission electron microscopy (TEM) samples were prepared by placing one drop of the corresponding SPION dispersion on the copper grid, blotting the copper grid with a filter paper and letting it evaporate completely at room temperature. C-SPIONs were imaged with a JEOL JEM-1210 electron microscope at an operating voltage of 120 KV. About 200 different particles were computed to depict the size distribution and the mean size of C-SPIONs.
Adsorption of BSA on C-SPIONs was visualized by performing negative staining TEM. 29 (link) A drop of BSA-SPIONs was placed on a carbon-coated grid and then blotted with filter paper. Subsequently, uranyl acetate (5 μL; 2%) was placed on the grid for 1 min before being blotted.
The grid was then placed in a 2011 JEOL electron microscope. About 200 different particles were counted to depict the size distribution and the mean size of the BSA-SPIONs.
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7

Nanoparticle Characterization by Spectroscopy

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NP concentration was determined by flame absorption spectroscopy (air-acetylene) with a Perkin-Elmer 2100 spectrometer. Briefly, NP dispersions were sonicated 10 min in an ultrasound bath, diluted with HCl (1%), and the resulting solution was analyzed using a Perkin-Elmer 2100 spectrometer.
All NPs were characterized by TEM, DLS, and zeta potential. Transmission electron microscopy (TEM) samples were prepared by placing one drop of the corresponding NP dispersion on the copper grid, blotting the copper grid with a filter paper, and allowing a complete evaporation at room temperature. In the case of BSA-SPIONs, an additional step of negative staining was applied to stain protein in white; 5 μL of 2% uranyl acetate were placed on the grid for 1 min before draining off. TEM samples were imaged with a JEOL JEM-1210 electron microscope at an operating voltage of 120 kV. About 200 different particles were analyzed to determine the size distribution and the mean size of nanoparticles using ImageJ.
Dynamic light scattering (DLS) and zeta potential measurements were performed with a Zetasizer Nano ZS (Malvern) with a He/Ne 633 nm laser at 25 °C. For each sample, three independent measurements were performed. Finally, the optical properties of gold nanoparticles were studied by UV-Vis spectroscopy using a Varian Cary 5000 UV-Vis-NIR spectrophotometer.
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