Tem microscope

Manufactured by JEOL

Sourced in Japan

The TEM microscope is a type of electron microscope that uses a beam of accelerated electrons to illuminate and image a specimen. It operates on the principle of transmitting an electron beam through a thin specimen, allowing for high-resolution imaging of the sample's internal structure and composition. The TEM microscope provides detailed information about the sample at the nanoscale level.

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Lab products found in correlation

Jsm 840 microscope, by JEOL (1 mentions)

6 protocols using tem microscope

Electron Microscopy Analysis of Remyelination

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EVs and EVPs were resuspended with PBS and used for transmission electron microscopy (TEM) images. Twenty microliters of EVs and EVPs were added to the carbon film copper grid for 10 min separately. One percent uranyl acetate was stained for 10 min at room temperature. Then, distilled water was used to clean the copper grid. After the copper grid dried in the air, images were observed using a TEM microscope (JEOL, Tokyo, Japan).
Lumbar spinal cords were fixed, and the lesion site of the dorsal spinal cord was taken for electron microscopy (Supplementary Fig. 1). It was then analyzed by TEM for assessing de/remyelination. Remyelinated axons were defined by an abnormally thin myelin sheath, which is considered the most reliable manner to identify remyelination. At least 50 myelinated axons on the figures were measured for each mouse. The g-ratio was measured by the size ratio between the diameter of the axon and the total fiber.

Xiao Y., Tian J., Wu W.C., Gao Y.H., Guo Y.X., Song S.J., Gao R., Wang L.B., Wu X.Y., Zhang Y, & Li X. (2021). Targeting central nervous system extracellular vesicles enhanced triiodothyronine remyelination effect on experimental autoimmune encephalomyelitis. Bioactive Materials, 9, 373-384.

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Transmission Electron Microscopy of Protein Aggregates

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Incubation samples of the wild type and three mutants at 40 μM were imaged at one and two weeks of the incubation in 1 mM phosphate buffer (pH 6.8), by a TEM microscope (Jeol Jem 2010f Hrtem, Japan) operating at an accelerating voltage of 200 kV. The aggregates of the wild type were prepared immediately before EM imaging, by diluting the stock protein sample in Milli-Q water (pH 4.0) into 1 mM phosphate buffer to reach a concentration of 200 μM (pH 6.8).
For EM imaging, a 5 μl aliquot of the incubation or aggregate solutions was placed onto the Cu grids (coated with carbon film; 150 mesh; 3 mm in diameter) and negatively stained with 5 μl of 2% neutral, phosphotungstic acid (PTA). This aliquot was allowed to settle on Cu grid for 30 s before the excess fluid was drained away. The Cu grid was later air-dried for another 15 mins before being imaged.

Lim L., Wei Y., Lu Y, & Song J. (2016). ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. PLoS Biology, 14(1), e1002338.

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Imaging of FUS RRM Domain Aggregation

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Incubation samples of the FUS RRM domain at 25 °C at a protein concentration of 40 µM were imaged at 3, 6 and 10 days of the incubation in 1 mM phosphate buffer (pH 6.8), by a TEM microscope (Jeol Jem 2010f Hrtem, Japan) operating at an accelerating voltage of 200 kV as previously described^{24 (link)}.
Briefly, for EM imaging, a 5 µl aliquot of the incubation or aggregate solutions was placed onto the Cu grids (coated with carbon film; 150 mesh; 3 mm in diameter) and negatively stained with 5 μl of 2% neutral, phosphotungstic acid (PTA). This aliquot was allowed to settle on Cu grid for 30 sec before the excess fluid was drained away. The Cu grid was later air-dried for another 15 mins before being imaged.

Lu Y., Lim L, & Song J. (2017). RRM domain of ALS/FTD-causing FUS characteristic of irreversible unfolding spontaneously self-assembles into amyloid fibrils. Scientific Reports, 7, 1043.

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Pollen Grain Observation by SEM and TEM

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For SEM observation, pollen grains were applied by flicking the anthers of mature flowers over mounting tape on a stub. The pollen grains were allowed to air dry for about 30 min, sputter coated with gold, and observed with a JSM-840 microscope (JEOL, Japan). For TEM observation, the same-stage inflorescences of wild type and mutant were fixed in 0.1 M phosphate buffer (pH 7.2) with 2.5% (v/v) glutaraldehyde. After 7 d of fixation, the material was washed thoroughly with phosphate buffer (pH 7.2). After that, the material was gradient dehydrated to 100% (v/v) ethyl alcohol and the inflorescences were then embedded and polymerization was performed (65°C, 24 h). Finally, ultra-thin sections (70-100 nm thick) were made and observed using a TEM microscope (JEOL).

Zhang C., Xu T., Ren M.Y., Zhu J., Shi Q.S., Zhang Y.F., Qi Y.W., Huang M.J., Song L., Xu P, & Yang Z.N. (2020). Slow Development Restores the Fertility of Photoperiod-Sensitive Male-Sterile Plant Lines. Plant physiology, 184(2).

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Characterizing Aggregate Morphology by TEM

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TEM was used to characterize morphological features of the aggregates. First, 200 mesh copper grids with carbon-coated formvar film were plasma-treated to render hydrophilic properties. Then 5 μL of the samples were spotted onto the grids and incubated for 5 min. Excess liquid was blotted out and then stained with 2% phosphotungstic acid pH 7.4 for 2 min. For the imaging, aggregates were collected at 0 h and 1 day during the aggregation process. Imaging was performed using a JEOL TEM microscope (Peabody, MA, USA) at 80 kV at the electron microscopy facility at the University of Michigan Ann Arbor medical school, USA.

Ismail M, & Kanapathipillai M. (2023). Amyloid-like RIP1/RIP3 RHIM Fragments’ Characterization and Application as a Drug Depot. Molecules, 28(3), 1480.

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Ultrastructural Mitochondrial Analysis

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The morphological changes in mitochondria were examined through transmission electron microscopy (TEM), following standardized procedures. After intervening, HK-2 cells and kidney tissue samples were fixed then subjected to a dehydration process using ethanol and acetone, each for 15 min. Subsequent to dehydration, sections of 60 nm thickness were prepared, placed on copper grids (200 mesh) and examined under a TEM microscope (JEOL, Tokyo, Japan). This method allowed for the detailed observation of mitochondrial structures and any morphological alterations induced by the treatments.

He Z., Dong C., Song T., Zhou J., Xu T., He R, & Li S. (2024). FTH1 overexpression using a dCasRx translation enhancement system protects the kidney from calcium oxalate crystal-induced injury. Cellular & Molecular Biology Letters, 29, 65.

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