1400 plus electron microscope

Manufactured by JEOL

Sourced in United States, Japan

The JEOL 1400 plus electron microscope is a transmission electron microscope (TEM) designed for high-resolution imaging and analysis of a wide range of materials. The instrument utilizes an electron beam to produce magnified images of samples, enabling researchers to study the structural and compositional details at the nanoscale. The JEOL 1400 plus provides a stable and reliable platform for a variety of applications, including materials science, life science, and nanotechnology research.

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Lab products found in correlation

Nicolet 6700 ft ir instrument, by Thermo Fisher Scientific (2 mentions) Zetasizer zs90, by Malvern Panalytical (1 mentions) Oneview camera, by Ametek (1 mentions) Spectramax id5 multi mode microplate reader, by Molecular Devices (1 mentions) Malvern zetasizer nano, by Malvern Panalytical (1 mentions) Genesys 150 uv vis spectrophotometer, by Thermo Fisher Scientific (1 mentions) Formvar carbon 400 mesh copper grids, by Ted Pella (1 mentions) Gatan oneview camera, by Ametek (1 mentions) 90 plus particle size analyzer, by Brookhaven Instruments (1 mentions) Zetasizer zs, by Malvern Panalytical (1 mentions) Jem 1400 electron microscope, by JEOL (1 mentions) Temcam f216 camera, by TVIPS (1 mentions) Cacodylate buffer, by Electron Microscopy Sciences (1 mentions) Sodium cacodylate buffer, by Electron Microscopy Sciences (1 mentions) 0.4 μm pore polyester membrane insert, by Corning (1 mentions)

Close spelling variants of this product

JEM-1400 Plus transmission electron microscope JEM-1400 Plus TEM transmission electron microscope TEM-1400 Plus transmission electron microscope JEM-1400 Plus electron microscope JEOL 1400 Plus transmission electron microscope JEM-1400(PLUS) 120 kV transmission electron microscope JEOL 1400 electron microscope JEOL 1400 Plus JEOL 1400 microscope

11 protocols using 1400 plus electron microscope

Mannose-6-Phosphate Receptor Expression in Fabry Disease

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For histological analysis, the endomyocardial and gastric and duodenal biopsy samples were fixed in 10% buffered formalin and paraffin embedded. Five microns–thick sections were stained with hematoxylin and eosin and Masson trichrome. For electron microscopy studies, additional biopsy samples were fixed in 2% glutaraldehyde in a 0.1 M phosphate buffer, at pH 7.3, post-fixed in osmium tetroxide and processed by following a standard protocol for embedding in Epon resin. Ultrathin sections were stained with uranyl acetate substitute and lead hydroxide and analyzed by a JEOL-1400-plus electron microscope.
Assessment and comparison of mannose-6-phosphate receptors in the myocardial and intestinal tissues in Fabry disease patients:
To evaluate a possible receptor-mediated different ERT delivery in the myocardium and intestine, we determined the expression of mannose-6-phosphate receptor in frozen intestinal and myocardial tissue in all six patients before and after 2 years on ERT. Results were compared with values from normal myocardium and intestine.

Frustaci A., Najafian B., Donato G., Verardo R., Chimenti C., Sansone L., Belli M., Vernucci E, & Russo M.A. (2022). Divergent Impact of Enzyme Replacement Therapy on Human Cardiomyocytes and Enterocytes Affected by Fabry Disease: Correlation with Mannose-6-phosphate Receptor Expression. Journal of Clinical Medicine, 11(5), 1344.

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Comprehensive Characterization of pSiNPs

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Both the hydrodynamic diameter and the ζ-potential measurements were obtained on a Zetasizer, Zs90 (Malvern Instruments). Subsequent pSiNP size measurements were taken with particles dispersed in Dulbecco phosphate-buffer saline (DPBS), pH 7.4, while ζ-potential measurements were measured with particles dispersed in ethanol. The FTIR spectra of the particles were obtained by a Thermo Scientific Nicolet 6700 FTIR instrument fitted with a Smart iTR diamond ATR fixture. TEM images were obtained using a JEOL 1400 plus electron microscope (JEOL USA, Inc.) at 80KeV and subsequently imaged with a Gatan Oneview camera (Gatan, Inc.). Thermogravimetric analysis (TGA) data were obtained using a TA Instruments^™ Discovery SDT 650^™. Nanoparticle samples were heated from 100°C-800°C at a ramp rate of 10°C/min in nitrogen. Both weight (%) change and derivative heat flow values were assessed. Dye-loaded particle constructs were assessed using a Molecular Devices^™ SpectraMax^® iD5 Multi-Mode Microplate Reader. N₂ adsorption/desorption isotherms were obtained using dry nanoparticles at a temperature of 77 K using a Micromeritics ASAP 202 instrument.

Vijayakumar S., Nasr S.H., Davis J.E., Wang E., Zuidema J.M., Lu Y.S., Lo Y.H., Sicklick J.K., Sailor M.J, & Ray P. (2022). Anti-KIT DNA Aptamer-conjugated Porous Silicon Nanoparticles for the Targeted Detection of Gastrointestinal Stromal Tumors. Nanoscale, 14(47), 17700-17713.

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Nanoparticle Characterization and Degradation

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A Malvern Zetasizer Nano (Malvern Panalytical Ltd.) was used to determine the hydrodynamic diameter and zeta potential of the nanoparticles. A Thermo Scientific Nicolet 6700 FTIR instrument fitted with a Smart iTR diamond ATR fixture was used to determine the FTIR spectra of the nanoparticles. A Genesys 150 UV/VIS Spectrophotometer (Thermo Fisher Scientific, Inc.) was used to evaluate the absorbance of FAM-peptide and a NanoSight LM10-HSB/GFT14 (Malvern Panalytical Ltd.) was used to determine the concentration of pSiNPs to calculate the number of peptides conjugated per pSiNP. For degradation studies, 0.5 mg/mL of lysozyme-loaded pSiNPs surface modified with PEG and CAQK were incubated in PBS at 37 °C. At 0, 12, 24, and 48 hours, aliquots of degraded nanoparticles were removed from the stock, pelleted, and resuspended into ethanol and loaded onto 42 μm formvar/carbon 400 mesh copper grids (Ted Pella, Inc.) and dried. The stock nanoparticles were similarly pelleted at each timepoint and resuspended in fresh PBS to ensure that degradation would not be stalled by the solubility of silicic acid in the supernatant.^{29 (link)} TEM images were obtained on a JEOL 1400 plus electron microscope (JEOL USA, Inc.) operated at 80KeV and equipped with a Gatan Oneview camera (Gatan, Inc.).

Waggoner L.E., Kang J., Zuidema J.M., Vijayakumar S., Hurtado A.A., Sailor M.J, & Kwon E.J. (2022). Porous Silicon Nanoparticles Targeted to the Extracellular Matrix for Therapeutic Protein Delivery in Traumatic Brain Injury. Bioconjugate chemistry.

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Characterization of Nanoparticle Size and Zeta Potential

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The size and distribution of the NPs were determined, at 25.0 ± 0.1 °C, by dynamic light scattering (DLS) analysis using a 90 Plus Particle Size Analyzer (Brookhaven Instruments Corporation, New York, USA). The samples were analyzed 24 h after preparation with a dilution ratio of 1/100 in distilled water, and the data were elaborated with the Contin method [34 (link)]. Each sample was measured six times, and the results were expressed as means ± standard deviation (SD). The zeta potential values of NPs were determined using the Zeta-sizer ZS (Malvern Instruments Ltd., Malvern, U.K.), at 25.0 ± 0.1 °C. The measurements were obtained after a dilution of 1/50 in distilled water, and the data were reported as the means of three independent experiments performed in triplicate. The morphology and size of the NPs were analyzed using transmission electron microscopy (TEM) (Jeol 1400 Plus electron microscope, JEOL ltd., Milano, Italy) after treatment with a 2% phosphotungstic acid solution.

Mazzotta E., De Benedittis S., Qualtieri A, & Muzzalupo R. (2019). Actively Targeted and Redox Responsive Delivery of Anticancer Drug by Chitosan Nanoparticles. Pharmaceutics, 12(1), 26.

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Visualization of Purified Parvovirus Particles

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Purifed PRV samples were inspected by transmission electron microscopy. Negative staining was performed by adsorbtion of the virus particles to 100 mesh carbon coated Formvar copper grids for 1 min, washed and stained with 4% aqueous uranyl acetate for 1–3 sec. Immunogold labelling was performed at room temperature using the following rabbit sera; Anti-σ1 #K275 [9 (link)] and Anti-σ3 #K267 [6 (link)]. Briefly, the samples were adsorbed to 100 mesh carbon coated Formvar copper grids for 1 min, incubated with primary antibody for 20 min (diluted 1/50 in 1% fish skin gelatine in PBS) followed by 20 min of proteinA gold (10 nm). Subsequently the grids were stained with 4% aqueous uranyl-acetate. Samples were examined either using a JEM 1400 Electron Microscope (JEOL Ltd, Tokyo, Japan) equipped with a TVIPS TemCam-F216 camera (TVIPS GmbH, Gauting, Germany) or a JEOL 1400Plus Electron Microscope (JEOL Ltd, Tokyo, Japan) equipped with a Ruby camera.

Wessel Ø., Braaen S., Alarcon M., Haatveit H., Roos N., Markussen T., Tengs T., Dahle M.K, & Rimstad E. (2017). Infection with purified Piscine orthoreovirus demonstrates a causal relationship with heart and skeletal muscle inflammation in Atlantic salmon. PLoS ONE, 12(8), e0183781.

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SP Micelle Morphology Characterization by TEM

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The size and morphology of SP micelles in various concentrations were inspected by transmission electron microscopy (TEM) using negative staining with uranyl acetate.
Negative staining was performed by placing a carbon-coated Fromvar copper grid (treated with glow discharge for 60 s) over a 40-µL drop of a sample of SP (0.5, 5, 10 and 15% (w/w) in water) for 5 min. Afterwards, the grid was washed with Milli-Q water and placed over a 20-µL drop of uranyl acetate (2% (w/w) in water) for 2 min. The excess of the uranyl acetate was blotted away with filter paper. After drying, the sample was examined using a JEOL 1400Plus Electron Microscope (JEOL Ltd, Tokyo, Japan) equipped with a Ruby camera at 120 kV.

Alopaeus J.F., Hagesæther E, & Tho I. (2019). Micellisation Mechanism and Behaviour of Soluplus®–Furosemide Micelles: Preformulation Studies of an Oral Nanocarrier-Based System. Pharmaceuticals, 12(1), 15.

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Electron Microscopy of Mouse Cerebellum

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Mice were anesthetized and perfused with 3% glutaraldehyde, 3% formaldehyde in 0.1 M cacodylate buffer (Electron Microscopy Sciences). Cerebellum was cut into small pieces and fixed overnight at 4 °C in 3% glutaraldehyde, 3% formaldehyde in 0.1 M Sorenson’s buffer (Electron Microscopy Sciences). The tissues were then embedded and sectioned at the University of Michigan Histology and Imaging Core. Samples were stained with uranyl acetate/lead citrate and high-resolution images were acquired with a JEOL 1400-plus electron microscope (JEOL).

Lin L.L., Wang H.H., Pederson B., Wei X., Torres M., Lu Y., Li Z.J., Liu X., Mao H., Wang H., Zhou L.E., Zhao Z., Sun S, & Qi L. (2024). SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex. Nature Communications, 15, 1440.

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Negative Staining of Protein Samples

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Peptide or protein solutions were placed on collodion-coated copper EM grids. Excess solutions were removed with filter paper, and the coated side on the grids was washed with filtered ultra-pure water. The samples were negatively stained by Nano-W^®, followed by washing with filtered ultra-pure water and dried. All images were obtained by using a JEOL 1400Plus electron microscope.

Miki T., Nakai T., Hashimoto M., Kajiwara K., Tsutsumi H, & Mihara H. (2021). Intracellular artificial supramolecules based on de novo designed Y15 peptides. Nature Communications, 12, 3412.

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Visualizing Amyloid Fibril Formation

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Five microliter aliquots of various samples measured for fibril formation as described in 4.2 were taken, diluted 20- to 30-fold with fresh buffer that matched the conditions for each sample and applied to collodion-covered carbon mesh electron microscopy sample grids (Nisshin EM Co., Tokyo, Japan). After 90 s, the aliquots were removed from the grids, washed with 5 µL Milli-Q and negatively stained using EM-Stainer solution. TEM micrographs were taken on a JEOL 1400Plus electron microscope (Tokyo, Japan) operating at 80 kV.

Nakata Y., Kitazaki Y., Kanaoka H., Shingen E., Uehara R., Hongo K., Kawata Y, & Mizobata T. (2022). Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from Escherichia coli. International Journal of Molecular Sciences, 23(21), 13243.

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Transmission Electron Microscopy of Adipose Tissue

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The TEM of adipose tissue was performed as described in ref. ^{39 (link)}. Briefly, mice were anesthetized and perfused with 2.5% glutaraldehyde, 4% formaldehyde in 0.1 M sodium cacodylate buffer (Electron Microscopy Sciences). WAT and BAT were immediately dissected and fixed overnight at 4 °C in the perfusion buffer. In some experiments, WAT was quickly removed without perfusion and fully immersed in the fixation buffer (2.5% glutaraldehyde and 4% paraformaldehyde in 0.1 M sodium cacodylate) for 1-h incubation at room temperature and overnight incubation at 4 °C. The fixed tissue was cut into small pieces (about 1-2 mm cubes) and then submitted to the University of Michigan Microscopy Core for washing, embedding and sectioning at 70 nm. The grid containing tissue sections was imaged by a JEOL 1400-plus electron microscope (JEOL) at the University of Michigan Microscopy Core.

Wu S.A., Shen C., Wei X., Zhang X., Wang S., Chen X., Torres M., Lu Y., Lin L.L., Wang H.H., Hunter A.H., Fang D., Sun S., Ivanova M.I., Lin Y, & Qi L. (2023). The mechanisms to dispose of misfolded proteins in the endoplasmic reticulum of adipocytes. Nature Communications, 14, 3132.

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