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Carbon coated 400 mesh cu rh grid

Manufactured by Ted Pella
Sourced in United States

Carbon-coated 400 mesh Cu/Rh grids are a type of laboratory equipment used for sample preparation in electron microscopy. These grids consist of a copper and rhodium alloy mesh with a thin carbon film deposited on the surface. The primary function of these grids is to provide a stable and conductive support for thin samples during imaging in electron microscopes.

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6 protocols using carbon coated 400 mesh cu rh grid

1

Exosome Imaging by Transmission Electron Microscopy

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Isolated exosomes were fixed by addition of 4% paraformaldehyde, 5 μl of the sample was dropped on a carbon coated 400 mesh Cu/Rh grid (Ted Pella, Redding, CA, USA) and stained with 5 μl of 1% uranyl acetate (Polysciences, Warrington, PA, USA) prepared in filtered distilled water. The grids were imaged with a FEI Talos L120C TEM with Gatan 4k × 4 k OneView camera.
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2

Transmission Electron Microscopy Imaging

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After complexation, 5 µL of each sample was dropped onto a carbon-coated 400 mesh Cu/Rh grid (Ted Pella, Redding, CA, USA) and stained with 5 µL of 1% uranyl acetate (Polysciences, Warrington, PA, USA) which was prepared in filtered distilled water. A FEI Talos L120C TEM with a Gatan 4 k × 4 k OneView camera was used to image the grids.
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3

Oligomeric Aβ42 Visualization by Electron Microscopy

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The presence of oligomeric forms of Aβ42 in the culture supernatants was additionally assessed by electron microscopy using our previously described protocols [8 (link), 14 (link)]. Briefly, 3 μl aliquots were placed onto carbon-coated 400-mesh Cu/Rh grids (Ted Pella, Inc., Redding, CA, USA) and stained with 1% uranyl acetate in distilled water (Polysciences, Inc., Warrington, PA, USA). Stained grids were examined in a Philips CM-12 transmission electron microscope and photographed with a Gatan (4 k × 4 k) digital camera at the NYU School of Medicine Microscopy Laboratory Core Facility.
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4

Dynamin Interactions with Liposomes Visualized by Electron Microscopy

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For negative stain EM, samples (1-3 μM dynamin and 200 μM DOPS liposomes incubated in the presence or absence of 1 mM GTP or GMPPCP for 30 min at room temperature) were absorbed onto carbon-coated 400 mesh Cu/Rh grids (Ted Pella, Inc.), stained with 2% Uranyl Acetate, and imaged in a Tecnai 12 (FEI) transmission electron microscope at 120kV using a 2 × 2 Gatan CCD camera. For cryo-EM, a 3.5 μl sample (prepared as described above) was placed on a plasma-cleaned (Fishione Inc.). Quantifoil holey carbon EM grid (SPI Supplies), blotted with filter paper, and flash-frozen in liquid ethane using a Leica EM GP (Leica Microsystems). The grids were subsequently stored in liquid nitrogen. The vitrified samples were imaged at liquid nitrogen temperature on a Tecnai 20 FEG electron microscope (FEI) operating at 200kV and images were collected with a 4 × 4 CCD camera.
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5

Dynamin Interactions with Liposomes Visualized by Electron Microscopy

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For negative stain EM, samples (1-3 μM dynamin and 200 μM DOPS liposomes incubated in the presence or absence of 1 mM GTP or GMPPCP for 30 min at room temperature) were absorbed onto carbon-coated 400 mesh Cu/Rh grids (Ted Pella, Inc.), stained with 2% Uranyl Acetate, and imaged in a Tecnai 12 (FEI) transmission electron microscope at 120kV using a 2 × 2 Gatan CCD camera. For cryo-EM, a 3.5 μl sample (prepared as described above) was placed on a plasma-cleaned (Fishione Inc.). Quantifoil holey carbon EM grid (SPI Supplies), blotted with filter paper, and flash-frozen in liquid ethane using a Leica EM GP (Leica Microsystems). The grids were subsequently stored in liquid nitrogen. The vitrified samples were imaged at liquid nitrogen temperature on a Tecnai 20 FEG electron microscope (FEI) operating at 200kV and images were collected with a 4 × 4 CCD camera.
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6

Electron Microscopy of Amyloid-Beta Peptide Oligomerization

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Peptide oligomerization was also monitored by electron microscopy, as previously described [38 (link), 66 (link), 71 (link)]. Five microliters of either monomeric or oligomeric preparations of the different Aβ peptides were placed onto carbon-coated 400 mesh Cu/Rh grids (Ted Pella, Inc., Redding, CA) and stained with 1% uranyl acetate in distilled water (Polysciences, Inc., Warrington, PA). The stained grids were examined in a Philips CM-12 transmission electron microscope and photographed with a Gatan (4 k × 2.7 k) digital camera at the Image Core Facility of the Skirball Institute of Biomedical Medicine, NYU School of Medicine, as described [66 (link), 71 (link), 72 (link)].
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