The largest database of trusted experimental protocols

300 mesh copper grid

Manufactured by Ted Pella
Sourced in United States

The 300-mesh copper grid is a laboratory equipment item used for sample preparation in various microscopy techniques. It provides a support structure for thin samples, allowing for efficient and precise analysis. The grid is made of copper and features a 300-mesh pattern, which refers to the number of openings per square inch. This product is designed to meet the needs of researchers and technicians working in fields that require high-resolution imaging and analysis of samples.

Automatically generated - may contain errors

10 protocols using 300 mesh copper grid

1

Morphological Characterization of Electrospun Fibers

Check if the same lab product or an alternative is used in the 5 most similar protocols
The morphology of the electrospun fibers was investigated by scanning electron microscopy (SEM), using a Jeol JSM 6610 (Jeol Ltd., Tokyo, Japan) with an accelerated voltage of 15kV. The samples were sputtered with a gold layer just before analysis. AzTec software Ver. 2.1. (Springfield, NJ, USA) was used for making figures and processing the results. The average diameter and dispersity of diameters were estimated on the basis of SEM images by using the freely accessible online software ImageJ Ver. 1.53e (LOCI, University of Wisconsin, Madison, WI, USA). The fiber diameter is expressed as average diameter ± standard deviation. One hundred fiber segments were analyzed randomly on 3 independently prepared samples to obtain a mean diameter for each type of nonwoven sample.
The measurements of the beads’ dimensions were carried out at the coarsest place on the individual beads. The average diameter was obtained from 50 measurements on 50 different beads.
Transmission electron microscopy (TEM) analysis was carried out with a Hitachi High-Tech HT7700 (Tokyo, Japan) instrument, operated in high contrast mode at 100 kV accelerating voltage. The samples were prepared by sandwiching the filaments between two uncovered 300 mesh copper grids (Ted Pella, Redding, CA, USA).
The proof of mechanical integrity was provided by using the Canon PowerShot SX130 camera (Tokyo, Japan).
+ Open protocol
+ Expand
2

Ultrastructural Analysis of Cell Lines

Check if the same lab product or an alternative is used in the 5 most similar protocols
The ultrastructure features were evaluated by transmission electron microscopy (TEM). SCC-25 and L929 cells (4.5 × 105 cells/well) were cultured in a 12-well plate for 24 h. Subsequently, they were incubated with a hydrogel solution and with their re-spective controls in full medium (equivalent to 500 µg/mL of dry V. album for SCC-25 and L929 cell lines). After 24 h, treated and untreated cells were centrifuged, the supernatant discarded, and the cells were fixed for 1 h in glutaraldehyde 2.5% containing sodium cacodylate buffer 0.1 M (pH 7.2). Subsequently, the material was washed in the same buffer, post fixed in osmium tetroxide 1% for 1 h, and washed with 0.1 M cacodylate buffer. Finally, all cells were dehydrated in acetone series and the material was embedded in Polybed 812. Ultrathin sectioning was performed on an EM UC6 microtome (Leica Microsystems GmbH, Wetzlar, Germany). Samples were recovered on 300-mesh copper grids (Ted Pella, Inc.), stained with uranyl acetate and lead citrate, and observed on an FEI Morgagni transmission electron microscope (FEI Company, Hillsboro, OR, USA) operating at 80 kV.
+ Open protocol
+ Expand
3

Characterization of Gold Nanoparticles

Check if the same lab product or an alternative is used in the 5 most similar protocols
AuNS solution
(3 mL) was placed in a 1 cm plastic Brookhaven cuvette, and the absorbance
spectra were measured from 400 to 1400 nm using a Cary 5000 UV–vis–NIR
spectrophotometer (Agilent Technologies).
For TEM grid preparation,
carbon Type B, 300 mesh copper grids (Ted Pella) were treated with
0.1% (w/v) poly-l-lysine (Sigma Aldrich) for 5 min. Then,
40 μL of 10× concentrated Au nanoparticle solution was
left to rest on the treated grids for 30–60 s and then wicked
away with filter paper. A JEOL 1230 TEM was used for imaging the particles.
The representative images were collected from different areas of the
grid. Structural features, such as circularity and Feret diameter,
were characterized using the Analyze Particles plugin on ImageJ for
at least 500 particles per sample. A circularity threshold of 0.9
was used to define spherical particles, and the Feret diameter corresponds
to the largest tip-to-tip distance on a particle. The branch length
was measured manually from the tip to the base of the branch.
+ Open protocol
+ Expand
4

Cryo-EM Imaging of Protein Nanoparticles

Check if the same lab product or an alternative is used in the 5 most similar protocols
6 μl of purified protein (I53-50-v0, I53-50-v1, I53-50-v2,
I53-50-v3, I53-50-v4, I53-50-Btat, I53-47-v0, I53-47-v1, I53-47-Btat) at 0.04
– 0.3 mg/mL were applied to glow discharged, carbon-coated 300-mesh
copper grids (Ted Pella), washed with Milli-Q water and stained with
0.75% uranyl formate as described previously27 . Screening and sample optimization was
performed on a 100 kV Morgagni M268 transmission electron microscope (FEI)
equipped with an Orius charge-coupled device (CCD) camera (Gatan). Data were
collected with Leginon automatic data-collection software28 (link) on a 120 kV Tecnai G2 Spirit
transmission electron microscope (FEI) using a defocus of 1 μm with a
total exposure of 30 e-/A2. All final images were recorded using an
Ultrascan 4000 4k × 4k CCD camera (Gatan) at 52,000×
magnification at the specimen level. For data collection used in two-dimensional
class averaging, the dose of the electron beam was 80 e-/Å2,
and micrographs were collected with a defocus range between 1.0 and 2.0
μm. Coordinates for unique particles (7,979 for I53-50-v0 and 7,130 for
I53-50-v4) were obtained for averaging using EMAN229 (link). Boxed particles were used to obtain
two-dimensional class averages by refinement in EMAN2.
+ Open protocol
+ Expand
5

SPIO-Au NPs Morphology and Stability

Check if the same lab product or an alternative is used in the 5 most similar protocols
To observe the morphology of the synthesized SPIO-Au NPs, the Transmission electron microscopy (TEM) imaging was performed on a JEOL JEM 1400 Transmission Electron Microscope at an operating voltage of 120 kV. Briefly, 100 μL droplets of each sample were dropped onto a 300-mesh copper grid (Ted Pella Inc., Redding, CA) and then left to dry in the air. To examine the influence of the cell growth medium on the stabilities of NPs, the UV-Vis absorption spectroscopy and the zeta potential characterization were conducted. The solution of SPIO-Au NPs at the concentration of 80 μg/mL was suspended in MC3T3-E1 cell growth medium and in deionized water, respectively. At different time points, the light absorption spectra were recorded at wavelengths between 400 nm and 800 nm at room temperature with a FLAME-S-XR1-ES spectrometer and the SpectraSuite software from Ocean Optics Inc. The zeta potential test was performed with a Malvern Zetasizer Nano ZS (Malvern Instruments Inc.) at 25 °C.
+ Open protocol
+ Expand
6

Negative Staining of Protein Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
A sample volume of 3 μL at a concentration of 70 μg/mL protein in 50 mM Tris pH 8, 150 mM NaCl, 5% v/v glycerol was applied to a freshly glow-discharged 300-mesh copper grid (Ted Pella) and incubated on the grid for 1 min. The grid was then dipped in a 40 μL droplet of water, excess liquid was blotted away with filter paper (Whatman), the grid was dipped into 3 μL of 0.75% w/v uranyl formate stain, stain was immediately blotted off with filter paper, then the grid was dipped again into another 3 μL of stain and incubated for ∼30 seconds. Finally, the stain was blotted away and the grids were allowed to dry for 1 minute prior to storage or imaging. Prepared grids were imaged in a Talos model L120C transmission electron microscope using a Gatan camera at 57,000×.
+ Open protocol
+ Expand
7

Negative Staining of Protein Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
A sample volume of 3 μL at a concentration of 70 μg/mL protein in 50 mM Tris pH 8, 150 mM NaCl, 5% v/v glycerol was applied to a freshly glow-discharged 300-mesh copper grid (Ted Pella) and incubated on the grid for 1 min. The grid was then dipped in a 40 μL droplet of water, excess liquid was blotted away with filter paper (Whatman), the grid was dipped into 3 μL of 0.75% w/v uranyl formate stain, stain was immediately blotted off with filter paper, then the grid was dipped again into another 3 μL of stain and incubated for ~30 s. Finally, the stain was blotted away and the grids were allowed to dry for 1 min prior to storage or imaging. Prepared grids were imaged in a Talos model L120C transmission electron microscope using a Gatan camera at 57,000×.
+ Open protocol
+ Expand
8

Negative Staining of Protein Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
A sample volume of 3 μL at a concentration of 70 μg/mL protein in 50 mM Tris pH 8, 150 mM NaCl, 5% v/v glycerol was applied to a freshly glow-discharged 300-mesh copper grid (Ted Pella) and incubated on the grid for 1 min. The grid was then dipped in a 40 μL droplet of water, excess liquid was blotted away with filter paper (Whatman), the grid was dipped into 3 μL of 0.75% w/v uranyl formate stain, stain was immediately blotted off with filter paper, then the grid was dipped again into another 3 μL of stain and incubated for ~30 s. Finally, the stain was blotted away and the grids were allowed to dry for 1 min prior to storage or imaging. Prepared grids were imaged in a Talos model L120C transmission electron microscope using a Gatan camera at 57,000×.
+ Open protocol
+ Expand
9

Comprehensive Nanoparticle Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
The mean hydrodynamic diameter (MHD) and polydispersity index (PDI) of NPs were determined by dynamic light scattering (DLS, 90Plus/BI_MAS, Brookhaven Instruments Corp., Holtsville, NY, USA) at 25 °C with a scattering angle of 90° in a neutral pH aqueous solution. Zeta potential (ZP) was measured by a Zeta Plus Analyzer (Zeta Plus, Brookhaven Instruments, Holtsville, NY, USA) using the electrophoretic mode under neutral pH. To study NP morphology, particles were subjected to transmission electron microscopy (TEM) and analyzed by JEOL 1200 EX at 80 kV in a 300-mesh copper grid (Ted Pella, Inc, Redding, CA, USA) without staining. Mean diameter (MD) was calculated by considering all NPs as spheres and measuring size (while taking the scale bar into consideration) in 10 different, random fields.
+ Open protocol
+ Expand
10

Characterization of Quantum Dot Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
A negatively stained TEM protein particle analysis was employed to characterize the Qdot samples.29 About 8 μL of sQdot (0.8 μM) and QNC (0.5 μM) were loaded separately onto ultrathin holey carbon film supported by a 300-mesh copper grid (Ted Pella Inc.) and incubated for 5 min. The grids were glow-discharged before the addition of samples. The incubated grids containing the samples were subsequently blot-dried with a clean filter paper, followed by staining with 2% (v/v) uranyl acetate for 1 min to enhance particle contrast, as described previously.29,30 The sQdot and QNC were imaged with FEI Tecnai G2 T20 at 120 kV accelerating voltage using the inbuilt Gatan Orius SC600 (bottom-mounted camera). Further image processing was done using ImageJ software (NIH). Size characterizations were performed on Zetasizer Nano (Malvern Panalytical).
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!