Dynamic light scattering (DLS) and zeta potential measurements were conducted using a Zetasizer Nano ZS (Malvern). Scanning electron microscopy (SEM) was conducted using a Zeiss Supra 25 Field Emission scanning electron microscope. SEM samples were prepared by gold sputtering and critical point drying. For AFM measurements, nanoparticles were observed on a freshly cleaved mica surface using an Asylum MFP 3D Bio AFM with an Olympus AC240TS probe. For transmission electron microscopy (TEM), a carbon-coated copper TEM grid (Ted Pella) was used with a JEOL 1200 EX transmission electron microscope operated at 80 kV.
Ac240ts probe
Manufactured by Olympus
Sourced in United Kingdom
The AC240TS probe is a laboratory equipment designed for various scientific applications. It serves as a tool for measuring and analyzing samples. The core function of the AC240TS probe is to provide accurate and reliable data for research and experimentation purposes.
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Lab products found in correlation
4 protocols using ac240ts probe
1
Nanoparticle Characterization via Multimodal Analysis
2
Atomic Force Microscopy of Tumor Stiffness
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5 μm slides from frozen lung tissue were transferred on coverslips and analysed for stiffness of primary tumours by AFM. For in vitro three‐dimensional stiffness analyses, 2 × 105 H1299 cells expressing either pcDNA3 H1299control or re‐expressing RASSF1A H1299RASSF1A were embedded into 3D rat tail collagen type I matrix and allowed them modified ECM for 5 days in 8 wells (Labtech). 3D collagen gels were transferred onto slides and subjected to mechanical testing by scanning probe microscopy. Scanning probe microscopy was performed on a MFP‐3D Atomic Force Microscope (Asylum Research, High Wycombe, UK), with an AC240TS probe (k = 2.0 Nm−1, Olympus, Japan). AMFM nanomechanical mapping and loss tangent imaging (Proksch & Yablon, 2012 ) were applied, with measurements based on the shift in the probe's resonant frequencies dependent on the strength of the interaction, or tip‐sample contact force (Giessibl, 1997 ).
A tip correction factor was calculated based on the known compressive Young's modulus of a polycaprolactone calibration sample (300 MPa). Three 5 × 5 μm areas were then randomly selected and measured from each material. 512 × 512 pixel maps of height, Young's modulus and loss tangent were recorded for each image.
A tip correction factor was calculated based on the known compressive Young's modulus of a polycaprolactone calibration sample (300 MPa). Three 5 × 5 μm areas were then randomly selected and measured from each material. 512 × 512 pixel maps of height, Young's modulus and loss tangent were recorded for each image.
3
Nanoparticle Characterization via Multimodal Analysis
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Dynamic light scattering (DLS) and zeta potential measurements were conducted using a Zetasizer Nano ZS (Malvern). Scanning electron microscopy (SEM) was conducted using a Zeiss Supra 25 Field Emission scanning electron microscope. SEM samples were prepared by gold sputtering and critical point drying. For AFM measurements, nanoparticles were observed on a freshly cleaved mica surface using an Asylum MFP 3D Bio AFM with an Olympus AC240TS probe. For transmission electron microscopy (TEM), a carbon-coated copper TEM grid (Ted Pella) was used with a JEOL 1200 EX transmission electron microscope operated at 80 kV.
4
Characterizing DNA-Protein Complexes by AFM
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DNA-protein complexes were imaged using an Asylum MFP 3D Bio AFM (Oxford Instruments, Goleta CA) with an Olympus AC240TS probe in tapping mode at room temperature. The samples were prepared a suitable concentration (0.5–1.0 ng/μL), then 40 uL of prepared samples were slowly deposited to a freshly cleaved AP-mica for 5 minutes and rinsed with 1 mL ultrapure deionized water twice before being gently dried with UHP argon gas.
AFM images were collected at a speed of 0.5–1 Hz at 512 × 512-pixel resolution, with an image size of 2 μm. For analysis, raw images were exported into 8-bit grayscale Tiff images using the Asylum Research’s Igor Pro software and imported into FIJI/ImageJ (NIH) for detection of single particles and quantification of volume, surface area, and volume/surface area ratio using as has been done previously for studies of chromatin compaction via AFM23 . In order to assess single chromatin particles, rather than potential clusters of multiple fibers or residual MMTV mononucleosomes, only particles with volumes measuring between 2,000 and 15,000 nm3 were included in analyses.
AFM images were collected at a speed of 0.5–1 Hz at 512 × 512-pixel resolution, with an image size of 2 μm. For analysis, raw images were exported into 8-bit grayscale Tiff images using the Asylum Research’s Igor Pro software and imported into FIJI/ImageJ (NIH) for detection of single particles and quantification of volume, surface area, and volume/surface area ratio using as has been done previously for studies of chromatin compaction via AFM23 . In order to assess single chromatin particles, rather than potential clusters of multiple fibers or residual MMTV mononucleosomes, only particles with volumes measuring between 2,000 and 15,000 nm3 were included in analyses.
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