Cm12 transmission electron microscope

Manufactured by Philips

Sourced in Netherlands, Germany

The Philips CM12 is a transmission electron microscope. It is designed to magnify and image very small samples by transmitting a beam of electrons through the specimen. The CM12 captures high-resolution images of the internal structure and composition of materials at the nanoscale.

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Lab products found in correlation

Uc6 ultramicrotome, by Leica (7 mentions) Em uc6 ultramicrotome, by Leica (4 mentions) Sis megaview 3, by Olympus (4 mentions) Trypsin edta, by Thermo Fisher Scientific (3 mentions) Ultracut s microtome, by Reichert Technologies (2 mentions) Glutaraldehyde, by Merck Group (2 mentions) Diamond knife, by Electron Microscopy Sciences (2 mentions) Spurr s resin, by Electron Microscopy Sciences (2 mentions) Ultracut e, by Philips (2 mentions) Ultracut microtome, by Leica (2 mentions) 2vu software, by Advanced Microscopy Techniques (2 mentions) Xr60 camera, by Advanced Microscopy Techniques (2 mentions) Em stain, by Leica (2 mentions) Lsm 700 confocal microscope, by Zeiss (2 mentions) Lsm 510, by Zeiss (2 mentions) Zetasizer nano z, by Malvern Panalytical (1 mentions) Formvar coated slot grids, by Electron Microscopy Sciences (1 mentions) Ac240ts cantilevers, by Olympus (1 mentions) Bx51 optical microscope, by Olympus (1 mentions) Glutaraldehyde, by Euromedex (1 mentions)

72 protocols using cm12 transmission electron microscope

Biotin-Labeled PCBP2 siRNA Nanocomplex

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PCBP2 siRNA duplex with a sticky end was annealed with complementary PNA-s-s-biotin and incubated at 37°C for 30 min to form the PCBP2 siRNA/PNA-biotin hybrid (Figure 1A). A low molecular weight polyethylene glycol (PEG) (1 kDa) was used as a linker between peptide-431 and biotin. The biotin-PEG-peptide-431 was synthesized as described before.^{[6b (link)]} Various molar ratios of PCBP2 siRNA/PNA-biotin : neutravidin : biotin-PEG-peptide-431, such as 2:1:2, 3:1:1, 3.5:1:0.5, 3.8:1:0.2, 3.9:1:0.1 and 3.99:1:0.01 were mixed at room temperature for 10 min to form the siRNA complex, followed by condensation with protamine at an N/P ratio of 2.5 to form the siRNA nanocomplex with a final siRNA concentration of 100 nM (Figure 1B).
siRNA nanocomplexes diluted in HEPES buffer (pH 7.4) were analyzed for mean particle diameter (nm) and zeta potential (mV) using Malvern Zetasizer Nano-ZS (Malvern Instruments, MA). Morphology of the nanocomplexes was examined with a CM12 transmission electron microscope (TEM) (Philips, Germany) after staining with 1% phosphotungstic acid.

Jain A., Barve A., Zhao Z., Fetse J.P., Liu H., Li Y, & Cheng K. (2019). Targeted Delivery of an siRNA/PNA Hybrid Nanocomplex Reverses Carbon Tetrachloride‐Induced Liver Fibrosis. Advanced therapeutics, 2(8), 1900046.

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Characterization of TiO2 Nanoparticles

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TiO₂ isolates were re-suspended in sterile Nanopure^™ water at a concentration of 10 ppm (i.e., 10 μg/mL) and drop-casted onto formvar-coated slot grids (Electron Microscopy Sciences, FF-2010-Cu). The grids were dried overnight and imaged with a Philips CM-12 transmission electron microscope (TEM) fitted with a Gatan 791 sidemount CCD at an accelerating voltage of 80 kV. At least 10 images were collected per sample. Images were analyzed with ImageJ [5 (link), 25 (link)], and primary particle sizes were calculated by measuring the edge-to-edge particle length and the length normal to this (i.e., X and Y direction) from each particle in the field of view. The two measurements were averaged for each single particle to obtain an average particle size. The sample primary particle size reported was calculated from 300‒1,000 average particle sizes.
A scanning electron microscope (SEM) fitted with a field emission gun (XL-30; FEI, Oregon, USA) and equipped with energy dispersive x-ray (EDX) microanalysis was used to obtain images of the isolated particles and their composition, respectively. Samples were prepared on conductive carbon tape. At least three EDX analyses were performed for each sample on areas approximately 250–500 nm in width and height.

Faust J.J., Doudrick K., Yang Y., Capco D.G, & Westerhoff P. (2016). A Facile Method for Separating and Enriching Nano and Submicron Particles from Titanium Dioxide Found in Food and Pharmaceutical Products. PLoS ONE, 11(10), e0164712.

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Microscopic Characterization of Propionibacteria

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Propionibacteria were routinely examined as wet-mount fresh cultures using an immersion phase contrast × 100 objective on an Olympus BX51 optical microscope. As an alternative, cultures were dried on a mica slide prior to analysis using AFM (Atomic Force Microscopy, as previously described (Deutsch et al., 2012 (link)). Briefly, the bacteria were washed in HEPES-NaCl buffer, deposited onto a freshly cleaved disk of mica and allowed to dry for 24 h in a desiccator. AFM imaging was performed in air, at a controlled temperature of 20°C and using a MFP-3D-BIO microscope (Oxford Instruments, Asylum Research, Santa Barbara, CA, United States). Images were acquired in tapping mode using AC240TS cantilevers (Olympus, Tokyo, Japan). Transmission Electron Microscopy (TEM) was performed as described previously (Deutsch et al., 2010 (link)). Briefly, bacteria were washed in PBS, fixed using glutaraldehyde, postfixed using osmium tetroxide/potassium cyanoferrate/uranyl acetate and dehydrated in ethanol (30–100%) prior to embedding in Epon. Thin sections (70 nm) were collected on 200-mesh copper grids and counterstained with lead citrate before examination using a Philips CM12 transmission electron microscope.

Tarnaud F., Gaucher F., do Carmo F.L., Illikoud N., Jardin J., Briard-Bion V., Guyomarc’h F., Gagnaire V, & Jan G. (2020). Differential Adaptation of Propionibacterium freudenreichii CIRM-BIA129 to Cow’s Milk Versus Soymilk Environments Modulates Its Stress Tolerance and Proteome. Frontiers in Microbiology, 11, 549027.

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Protein Sample Preparation for TEM

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For transmission EM, a 4 μl drop containing ~0.1 mg/ml protein and varying amounts of lipid in standard buffer was deposited onto an EM grid. The grids were stained with 2% uranyl acetate and blotted as previously described (Gursky et al., 2002 (link)). Electron micrographs were collected at a 45,000 magnification using a CM12 transmission electron microscope (Philips Electron Optics, the Netherlands) equipped with a Teitz 2Kx2K CCD camera (TVIPS, Germany).
Unless otherwise stated, all experiments reported in this study were repeated three to six times using three different protein batches to ensure reproducibility.

Frame N.M., Jayaraman S., Gantz D.L, & Gursky O. (2017). Serum amyloid A self-assembles with phospholipids to form stable protein-rich nanoparticles with a distinct structure: A hypothetical function of SAA as a ‘‘molecular mop” in immune response. Journal of structural biology, 200(3), 293-302.

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Transmission Electron Microscopy Fixation Protocol

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Cells were pelleted and fixed for 4 h in 2.5% glutaraldehyde (Euromedex, Mundolsheim, France) in 0.1 M sodium cacodylate buffer, pH 7.2 (Euromedex). Cells were then rinsed with sodium cacodylate buffer and postfixed in 1% osmium tetroxide (Euromedex) for 1 h at RT. Samples were washed and then dehydrated through a graded series of ethanol solutions to water followed by propylene oxide and then infiltrated in 1:1 propylene oxide/poly Bed 812 (Euromedex). Samples were kept overnight embedded in Poly Bed 812, mounted in molds, and left to polymerize in an oven at 56°C for 48 h. Ultrathin Sects. (70–90 nm) were obtained with a Reichert-Jung Ultracut S microtome (Wien, Austria). Sections were stained with uranyl acetate and lead citrate and examined with a CM12 transmission electron microscope (Philips, Eindhoven, The Netherlands).

Orlikova-Boyer B., Lorant A., Gajulapalli S.R., Cerella C., Schnekenburger M., Lee J.Y., Paik J.Y., Lee Y., Siegel D., Ross D., Han B.W., Nguyen T.K., Christov C., Kang H.J., Dicato M, & Diederich M. (2024). Antileukemic potential of methylated indolequinone MAC681 through immunogenic necroptosis and PARP1 degradation. Biomarker Research, 12, 47.

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Exosome Visualization and Sizing

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Exosomes were placed on 200-mesh carbon-coated copper grids at RT for 2 min. The excess suspension was removed using filter paper. The exosomes were negatively stained with uranyl acetate at RT for 5 min, washed twice with PBS, and dried. The exosomes were examined using a Philips CM12 transmission electron microscope operating at 80 kV, and their images were captured. The size distribution of exosomes was analyzed using the qNano Gold Particle Sizing Instrument (Izon Science, OX, UK).

Li J., Huang F., Jiang Y., Zhao J., Wan J, & Hao S. (2022). A novel costimulatory molecule gene-modified leukemia cell-derived exosome-targeted CD4+ T cell vaccine efficiently enhances anti-leukemia immunity. Frontiers in Immunology, 13, 1043484.

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Characterization of Mesenchymal Exosomes

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Exosomal proteins (20µg) were separated on 12% SDS-PAGE and transferred to PVDF membranes. Then, the membrane was blocked with 5% non-fat dry milk at room temperature for 1 h, probed with primary antibodies to exosomal signature proteins (CD63, CD9, and TSG101) overnight at 4°C, and then incubated with horseradish peroxidase (HRP)-conjugated secondary antibodies (Beyotime Biotech, Shanghai, China) at room temperature for 1 h. Chemiluminescent reagents were used to visualize the immunoreactive bands on the membranes. GAPDH served as a loading control. MEXs were poured dropwise onto a 200-mesh carbon-coated copper mesh and set incubated at room temperature for 2 min, washed twice with PBS, and negatively stained with uranyl acetate for 5 min. The images of the exosomes were captured using a Philips CM12 transmission electron microscope at 80 kV. The qNano gold particle sizer was used to investigate the size distribution of MEXs.

Jiang Y., Zhao J., Wang M., Huang F., Li J., Liu R., Wan J, & Hao S. (2023). Mesenchymal stem cell-derived exosomes can alleviate GVHD and preserve the GVL effect in allogeneic stem cell transplantation animal models. Frontiers in Immunology, 14, 1284936.

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Investigating CRTAC1 Aggregation Propensity

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Before TEM analysis hCRTAC1, dlCrtac1a1 and dlCrtac1b were incubated in Tris buffer 100 mM, 250 mM NaCl for 3 weeks at 37°C, samples were taken before incubation (T = 0) and after each week and immediately used to prepare TEM grids. Salts (50 mM and higher) are reported to increase the aggregation propensity of Alzheimer's related Aβ peptide 42 . Since CRTAC1 is a putative calcium-binding protein 10 we evaluated the impact of calcium on its aggregation propensity by incubating hCRTAC1, dlCrtac1a and dlCrtac1b for 1 week with 50 mM CaCl2. TEM analysis was carried out using the negative stain method and a CM12 transmission electron microscope (Philips Electron Optics) operated at 80 kV. Samples were prepared by applying 4 µl droplets of each CRTAC1 protein solution onto glow-discharged carbon formvar-coated copper grids and incubated for 30 sec or 1 min (dlCrtac1b), 4 min (hCRTAC1) or 3 min (dlCrtac1a), washed with a 4 µl water droplet for 1 min and counterstained with a 4 µl droplet of a freshly filtered solution of 2% (w/v) uranyl acetate. Grids were left to air dry for 3 min after staining.
Protein concentrations were as follows: dlCrtac1b 2.7 mg/ml (39 µM); hCRTAC1 0.7 mg/ml (10 µM); dlCrtac1a 1.3 mg/ml (20 µM).

Anjos L., Morgado I., Guerreiro M., Cardoso J.C., Melo E.P, & Power D.M. (2017). Cartilage acidic protein 1, a new member of the beta-propeller protein family with amyloid propensity. Proteins, 85(2).

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Optimized Corneal Sample Preparation for TEM

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Samples were further imaged by a CM12 Transmission Electron Microscope (Philips, Amsterdam, the Netherlands), operating at 80 kV and equipped with a MegaViewG2 camera (Olympus Corporation, Tokyo, Japan). For TEM imaging, corneal samples were divided into 1 mm² surface area fragments, which were washed twice with phosphate-buffered saline (0.1 M, pH 7.2) and then fixed with fresh glutaraldehyde (2.5%) in the same buffer at 4 °C for 12 h. Then all samples were sequentially washed three times (15 min) with phosphate-buffered saline, post-fixed with osmium tetroxide (1.0%) in the same buffer for 1 h, washed twice with the same buffer (15 min each), dehydrated with 30, 40 and 50% ethanol for 10 min, then 70% ethanol for 20 min, then 80, 95% and pure ethanol for 10 min and with pure propylene oxide for 10 min and finally infiltrated in a Spurr resin^{60 (link)}. Ultrathin sections of infiltrated samples were collected and deposited onto carbon-coated copper grids with 200 mesh size, stained with uranyl acetate in methanol (50%) for 5 min and with lead citrate for 8 min^{61 (link)}. Lead citrate was prepared as prescribed by Venable and Goggeshall^{62 (link)}. All washing procedures were carried out with CO₂-free water upon bubbling with nitrogen for 30 min.

Mercatelli R., Mattana S., Capozzoli L., Ratto F., Rossi F., Pini R., Fioretto D., Pavone F.S., Caponi S, & Cicchi R. (2019). Morpho-mechanics of human collagen superstructures revealed by all-optical correlative micro-spectroscopies. Communications Biology, 2, 117.

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Light and Electron Microscopy Sample Preparation

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For analysis in light microscopy, samples were dehydrated with 2-methoxyethanol (three changes), ethanol, n-propanol, and n-butanol (Feder and O'Brien 1968) and embedded in Technovit 7100 (Kulzer HistoTechnik). Semi-thin cuttings (2 lm) were sectioned using a Reichert UltraCut S ultramicrotome, stained (Table 3) and mounted in DPX. All sections were observed using a Leica microscope Leitz DM/RB, 59 to 1009 objectives and either diascopic or episcopic (fluorescence) light illumination. Micrographs were taken using either the digital Leica DC 500 camera interfaced by the Leica DC500 TWAIN software under control of the Image Access Enterprise 5 (Imagic, Glattbrugg, Switzerland) image management system (transmitted light microscopy), or the analogous micrograph system Wild MPS 48/52 using Kodak Ektachrome 400 Asa films (fluorescence microscopy). EMgrade fixed samples were post-fixed in buffered 2 % OsO4, dehydrated by a series of graded ethanol, infiltrated by a series of graded propylene oxide/Epon 812 mixture (with DDSA, NMA and DMP hardener) and embedded in Epon. Ultra-thin cuttings (70 nm) were sectioned using the aforementioned ultramicrotome, mounted on copper grids and contrasted using saturated uranyl acetate in 50 % ethanol and lead citrate (Reynolds procedure). Sections were observed using a Philips CM 12 transmission electron microscope.

Vollenweider P., Menard T., Arend M., Kuster T.M, & Günthardt-Goerg M.S. (2016). Structural changes associated with drought stress symptoms in foliage of Central European oaks. Trees., 30(3).

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