All reagents and solvents were purchased from Sigma-Aldrich (Milwaukee, WI) and used as received unless otherwise mentioned. Di-tert-butyl L-tartrate22 (link) and di-2-bocaminoethyltartramide23 were prepared as previously published. Anhydrous dimethylformamide (DMF) was dried over 4 Å molecular sieves at room temperature at least overnight prior to use. N-Boc-ethylenediamine was purchased from Alfa Aesar (Ward Hill, MA). 1-(3-dimethylaminopropy-l)-2-ethylcarbodiimide hydrochloride (EDC·HCl) was purchased from AK Scientific (Union City, CA). Silicon wafers were purchased from Ted Pella, Inc. (Redding, CA). For cell experiments, reagents include human buffy coats purchased from the New York Blood Center (Long Island City, NY), penicillin/streptomycin purchased from Lonza (Basel, Switzerland), Dulbecco’s modified eagle medium (DMEM) and Vybrant® MTT ((3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) cell proliferation assay kit purchased from ThermoFisher Scientific (Waltham, MA).
Silicon wafer
Manufactured by Ted Pella
Sourced in United States
Silicon wafers are thin, circular slices of high-purity silicon used as the foundation for semiconductor devices and integrated circuits. They serve as the substrate for the fabrication of electronic components, enabling the creation of microchips, transistors, and other electronic components.
Automatically generated - may contain errors
Lab products found in correlation
Fesem merlin, by Zeiss (10 mentions)
Merlin, by Zeiss (5 mentions)
Zetasizer nano z, by Malvern Panalytical (3 mentions)
Whatman filter paper number 1, by GE Healthcare (3 mentions)
Jem 1400, by JEOL (2 mentions)
Jem 1400 tem, by JEOL (2 mentions)
Microcentrifuge tube, by Eppendorf (2 mentions)
Mfp 3d bio, by Oxford Instruments (2 mentions)
Aptes, by Merck Group (2 mentions)
Igor pro, by Wavemetrics (2 mentions)
Dnp 10 afm tip, by Bruker (2 mentions)
Vybrant mtt, by Thermo Fisher Scientific (1 mentions)
N boc ethylenediamine, by Thermo Fisher Scientific (1 mentions)
Dulbecco s modified eagle medium dmem, by Thermo Fisher Scientific (1 mentions)
Penicillin streptomycin, by Lonza (1 mentions)
Ccd camera, by Ametek (1 mentions)
Syto9, by Thermo Fisher Scientific (1 mentions)
Pentadecylamine, by Merck Group (1 mentions)
Water purification system, by Merck Group (1 mentions)
Octadecylamine, by Merck Group (1 mentions)
33 protocols using silicon wafer
1
Synthesis and Characterization of Tartrate Derivatives
2
Ultrastructural Characterization of Intracellular and Isolated Inclusion Bodies
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Ultrastructural characterization of intracellular and isolated IBs was performed with two high-resolution electron microscopy techniques. Imaging of intracellular IBs was performed with standard Transmission Electron Microscopy (TEM) procedures adapted to this type of sample [23 (link), 58 (link), 63 (link), 64 (link)]. Briefly, pellets of bacilli with and without IBs were fixed with 2.5% glutaraldehyde in 0.1 M phosphate buffer (PB) at pH 7.2, postfixed in 1% osmium tetroxide containing 0.8% potassium ferrocyanide in PB, dehydrated in acetone, embedded in Spurr resin and polymerized at 60 °C during 48 h. Ultrathin Sect. (70 nm) obtained with an ultramicrotome UCT7 (Leica Microsystems) were placed in Cu grids (200 mesh) and contrasted following routine protocol of uranyl acetate and lead citrate solutions. Samples were observed in a TEM JEM 1400 (Jeol) equipped with an Erlangshen CCD camera (Gatan) and operating at 80 kV.
Ultrastructural morphometry (size and shape) of nanoparticles was performed and characterized at nearly native state with field emission scanning electron microscopy (FESEM). Drops of 20 µL of IBs sample were directly deposited on silicon wafers (Ted Pella Inc.) for 30 s and immediately observed without coating with a FESEM Merlin (Zeiss) operating at 1 kV and equipped with a high-resolution secondary electron detector.
Ultrastructural morphometry (size and shape) of nanoparticles was performed and characterized at nearly native state with field emission scanning electron microscopy (FESEM). Drops of 20 µL of IBs sample were directly deposited on silicon wafers (Ted Pella Inc.) for 30 s and immediately observed without coating with a FESEM Merlin (Zeiss) operating at 1 kV and equipped with a high-resolution secondary electron detector.
3
Characterizing Protein Aggregates by SEM and DLS
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Scanning electron microscopy (SEM) was used in order to analyze the morphology of ZapB and ZapB-GFP IBs. To do that, 10 µL of sample resuspended in water were deposited on silicon wafers (Ted Pella Inc., USA), air-dried and observed using a SEM Merlin (Zeiss Merlin, Germany) operating at 2 kV.
Dynamic light scattering (DLS) was used for a quantitative determination of ZapB-GFP and Aβ42-GFP IBs size. The size of these nanoparticles was determined using a Zetasizer Nano ZS (Malvern Instruments Limited, UK) at 25 °C. Three different measures of ten runs were recorded for each sample.
Dynamic light scattering (DLS) was used for a quantitative determination of ZapB-GFP and Aβ42-GFP IBs size. The size of these nanoparticles was determined using a Zetasizer Nano ZS (Malvern Instruments Limited, UK) at 25 °C. Three different measures of ten runs were recorded for each sample.
4
Particle Lithography for Nanoholes in OTS
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Particle lithography was used to prepare nanoholes within a thin film of octadecyltrichlorosilane (OTS) on Si(111). Silicon wafers (Ted Pella Inc. Redding, California) were rinsed with water and cleaned in piranha solution (3:1 sulfuric acid to hydrogen peroxide) for 1.5 h to remove surface contaminants. Caution: this solution is highly corrosive and should be handled carefully. The substrates were then rinsed with ultrapure water and dried under nitrogen. After drying, 10 µL of monodisperse silica microspheres in water was deposited on the clean silicon substrates and dried in air to produce a surface film of Si spheres. The substrate and dried microspheres were placed in an oven at 150 °C for 20 h. The annealing heating step was used to temporarily solder the silica microspheres to the silicon surface so that the beads would not be displaced in solution. The substrates containing the silica microspheres masks were then removed from the oven and placed in a 0.1% (v/v) solution of OTS in toluene for 5 h. The samples were then rinsed with ethanol and water with successive sonication in ethanol, ultrapure water, and chloroform. A rinsing and sonication step was used to fully remove the spheres from the surface. The samples were then dried under argon and characterized with AFM.
5
Visualizing Mycobacteria Emulsion Characteristics
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To confirm the O/W nature of the mycobacteria emulsion, the drop test (Supplementary Materials and Methods ) and two different microscopy techniques were performed, as described previously15 . For the light and fluorescent microscopy observation, 2% trypan blue was added to the aqueous phase, and the mycobacteria were stained with Syto® 9 (Life Technologies) when performing the emulsion in OO. Five microliters of the emulsion was placed on a slide, and the coverslip was sealed with transparent nail polish. The samples were observed at 1000X using light and fluorescent microscopes, as described in the Supplementary Material and Methods .
To observe the ultrastructure of the emulsified mycobacteria in a near-native stage, a Field Emission Scanning Electron Microscope (FESEM) was used. Emulsified and non-emulsified M. brumae were fixed with 1:1 osmium tetraoxide (4%, TAAB Lab., West Berkshire, UK) at 4 °C for 30 minutes. Then, 5 μL samples were deposited in silicon wafers (Ted Pella, Redding, CA, US) over a period of 1 minute, and excess sample was blotted with Whatman paper, air dried and observed without coating using a FESEM Zeiss Merlin (Oberkochen, Germany) that was equipped with a high-resolution in-lens secondary electron detector and operated at 0.8 kV.
To observe the ultrastructure of the emulsified mycobacteria in a near-native stage, a Field Emission Scanning Electron Microscope (FESEM) was used. Emulsified and non-emulsified M. brumae were fixed with 1:1 osmium tetraoxide (4%, TAAB Lab., West Berkshire, UK) at 4 °C for 30 minutes. Then, 5 μL samples were deposited in silicon wafers (Ted Pella, Redding, CA, US) over a period of 1 minute, and excess sample was blotted with Whatman paper, air dried and observed without coating using a FESEM Zeiss Merlin (Oberkochen, Germany) that was equipped with a high-resolution in-lens secondary electron detector and operated at 0.8 kV.
6
Cation-induced Microparticle Visualization
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High-resolution images of cation-induced microparticles were obtained by field emission scanning electron microscopy (FESEM). A volume of 10 μL of each microparticle sample (0.5 mg/mL) was deposited on silicon wafers (Ted Pella Inc., Redding, CA, USA) overnight and then observed, without coating, in a FESEM Zeiss Merlin (Zeiss, Jena, Germany) operating at 1 kV and equipped with a high-resolution secondary electron detector.
7
Synthesis and Characterization of Colloidal Nanoparticles
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Gold (III) chloride trihydrate (HAuCl4·3H2O, ≥99.9% trace metals basis), sodium citrate dihydrate (HOC(COONa)(CH2COONa)2·2H2O, ≥99%), ethanol (ACS reagent, ≥99.5%), acetone (HPLC grade, ≥99.9%), toluene (anhydrous, ≥99.8%), n-hexane (anhydrous, 95%), chloroform (anhydrous, ≥99.5%), benzene (ACS spectrophotometric grade, ≥99%), dodecylamine (CH3(CH2)11NH2, ≥99%), pentadecylamine (CH3(CH2)14NH2, 96%), octadecylamine (CH3(CH2)17NH2, 97%), oleylamine (≥98%), Rhodamine 6G (R6G, dye content 99%) and amine terminated polystyrene (average Mn = 5000, PDI ≤ 1.2) were purchased from Sigma-Aldrich and used as received. Deionized (DI) water (18.2 MΩ·cm at 25 °C) was supplied by a Millipore water purification system. Gas-tight containers (10 × 10 × 5 cm3, Snapware) were purchased from McMaster. Silicon wafers (5 × 5 mm2, purchased from Ted Pella) were thoroughly cleaned with Piranha solution at 60 °C. (Caution: Piranha solution is highly corrosive and reacts violently with organic matter!) For all experiments, glassware was cleaned in a base bath (a mixture of 1 L DI water, 4 L ethanol and 250 g NaOH). Teflon coated magnetic stir bars (VWR) were cleaned with acetone. After cleaning, all components were rinsed with DI water and dried overnight at 100 °C before use.
8
Ultrastructural Characterization of Protein Nanoparticles
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To visualize the ultrastructure of protein nanoparticles by transmission electron microscopy (TEM), 2 µl of purified protein (0.2 mg/ml) were placed on carbon-coated copper grids for 1 min. Excess of sample was bloated and 2 µl of 1 % w/v uranyl acetate were added for negative staining. Samples were immediately visualized in a TEM Jeol JEM-1400 (Jeol Ltd., Tokyo, Japan) equipped with a Gatan CCD Erlangshen ES1000 W camera (Gatan Inc, Abingdon, UK) and operating at 80 kV. Ultrastructural analyses of nanoparticle morphology were complemented with imaging in a nearly native state with a Field Emission Scanning Electron Microscope (FESEM). For that, protein samples were directly deposited over silicon wafers (Ted Pella, Reading, CA, USA), air dried and observed with a high resolution in-lens secondary electron detector through a FESEM Zeiss Merlin (Zeiss, Oberkochen, Germany), operating at 2 kV.
9
Nanoscale Morphological Analysis of Protein Nanoconjugates
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The nanoscale morphometry (size and shape) of T22-GFP-H6-MMAE MPs and of the released T22-GFP-H6-MMAE nanoconjugates was visualized at a nearly native state with a Field Emission Scanning Electron Microscope (FESEM). Samples in buffer were deposited 1 min in silicon wafers (Ted Pella, Inc Redding, CA, USA), air dried and immediately observed in a FESEM Merlin (Zeiss, Oberkochen, Germany) operating at 1 KV and equipped with both standard and in-lens secondary electron detectors. Representative images of MPs and nanoconjugates were collected at three magnifications (MPs: 10,000×, 70,000×, 100,000×; Nanoconjugates: 70,000×, 240,000×, 370,000×). The size distribution of the released protein was determined by dynamic light scattering (DLS) in a Zetasizer Nano ZS (Malvern Instruments Ltd., Malvern, UK) at 633 nm. Average values were obtained after the independent measurement of protein samples in triplicate.
10
Ultrastructural Protein Morphometry
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Ultrastructural morphometry of
proteins at the nearly native state was assessed with two high-resolution
techniques. Sample drops (5 μL) were deposited on silicon wafers
(Ted Pella Inc.) for 2 min, air-dried, and immediately observed without
coating with a Merlin field emission scanning electron microscope
(FESEM) (Zeiss), operating at 1 kV and equipped with a high-resolution
in-lens secondary electron detector. Representative images of general
fields and nanostructure details were captured at two high magnifications
(150000× and 400000×). Drops (5 μL) of the same samples
were deposited for 2 min on 200 mesh copper grids coated with carbon,
contrasted with 2% uranyl acetate for 2 min, air-dried, and observed
with an H-7000 transmission electron microscope (TEM) (Hitachi) equipped
with a CCD Gatan ES500W Erlangshen camera (Gatan). Representative
images of general fields and nanostructure details were captured at
two high magnifications (70000× and 200000×).
proteins at the nearly native state was assessed with two high-resolution
techniques. Sample drops (5 μL) were deposited on silicon wafers
(Ted Pella Inc.) for 2 min, air-dried, and immediately observed without
coating with a Merlin field emission scanning electron microscope
(FESEM) (Zeiss), operating at 1 kV and equipped with a high-resolution
in-lens secondary electron detector. Representative images of general
fields and nanostructure details were captured at two high magnifications
(150000× and 400000×). Drops (5 μL) of the same samples
were deposited for 2 min on 200 mesh copper grids coated with carbon,
contrasted with 2% uranyl acetate for 2 min, air-dried, and observed
with an H-7000 transmission electron microscope (TEM) (Hitachi) equipped
with a CCD Gatan ES500W Erlangshen camera (Gatan). Representative
images of general fields and nanostructure details were captured at
two high magnifications (70000× and 200000×).
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