Bl ac40ts probes

Manufactured by Olympus

Sourced in Japan

The BL-AC40TS probes are a type of laboratory equipment designed for electrical measurements. They feature a voltage range of 40V and a current range of 4A, enabling users to conduct various electrical tests and analyses. The probes are durable and reliable, engineered to provide accurate and consistent readings. No further interpretation or extrapolation on the intended use of this product is provided.

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Lab products found in correlation

Nanoscope 5 controller, by Bruker (2 mentions) Nanoscope software, by Bruker (2 mentions) Originpro, by OriginLab (2 mentions) Multimode 8, by Bruker (1 mentions) Ac160ts probes, by Olympus (1 mentions) Multimode 8 instrument, by Bruker (1 mentions)

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BL-AC40TS (12 citations)

3 protocols using bl ac40ts probes

Characterizing Patterned Protein Surfaces by AFM

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The AFM data
were collected on a Multimode 8 instrument equipped with a 15 μm
scanner (E-scanner) coupled to a NanoScope V controller (Bruker).
NanoScope software (v8.15, Bruker) was used for data collection, and
Gwyddion (v2.32, open source software covered by GNU general public
license, www.gwyddion.net) and OriginPro (v8.5.1, OriginLab
Corp.) software packages were used for data processing and analysis.
The measurements of the patterned SAMs were performed in tapping mode
in air at ambient conditions by use of AC160TS probes (Olympus) with
a nominal spring constant of approximately 40 N·m^–1 and a nominal resonant frequency of around 300 kHz.
The chemically
patterned surfaces with the immobilized protein molecules on them
were imaged in peak force tapping mode at nearly physiological conditions
in buffer (PBS, pH 7.4), at room temperature by use of BL-AC40TS probes
(Olympus). In this case, the Z-modulation amplitude
was adjusted to values in the range 20–24 nm, while the Z-modulation frequency was 2 kHz and the contact tip-sample
force was kept in the range 80–100 pN.

Vasilev C., Johnson M.P., Gonzales E., Wang L., Ruban A.V., Montano G., Cadby A.J, & Hunter C.N. (2014). Reversible Switching between Nonquenched and Quenched States in Nanoscale Linear Arrays of Plant Light-Harvesting Antenna Complexes. Langmuir, 30(28), 8481-8490.

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Nanoscale Protein Profiling of Thyroid Conditions

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Freshly cleaved mica disks (TedPella Inc., USA) were treated with three amino propyl-trimethoxysilane (APTMS) at 0.1% v/v in Milli Q water for 3 min, removing the silane excess with 3 mL of water. Before deposition, five secretome samples, belonging to three groups (healthy (A), thyroiditis (B), and in thyroid carcinoma (C)) were concentrated three times, by evaporating 100 µL of the sample for 24 h at 25 °C, and were then incubated for 60 min on positively charged mica disks obtained as described above. Just before imaging, 70 µL of Milli Q water were added to the samples. Images have been acquired using an Oxford Instrument Cypher instrument, equipped with an Environmental Scanner. All acquisitions have been obtained by scanning in liquid at a temperature of 20 °C, using BL-AC40TS probes (Olympus Corporation, Japan) with a nominal resonance frequency in air of 110 kHz. At least four 15 × 15 µm² scans for every sample has been acquired for statistical analysis. Sample details have been acquired as scanning areas of ~300 × 300 nm². Data have been imported in ImageJ for imaging and data analysis. Particles were detected in ImageJ by thresholding (height > 10 nm, area > 100 nm²), and their normalized height distribution has been plotted using a bin width of 5 nm.

Coluccio M.L., Presta I., Greco M., Gervasi R., La Torre D., Renne M., Voci C.P., Lunelli L., Donato G, & Malara N. (2020). Microenvironment Molecular Profile Combining Glycation Adducts and Cytokines Patterns on Secretome of Short-term Blood-derived Cultures during Tumour Progression. International Journal of Molecular Sciences, 21(13), 4711.

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Protein Immobilization on Patterned Surfaces

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The AFM data was collected on a Multimode 8 instrument equipped with a 15 μm scanner (E-scanner) coupled to a NanoScope V controller (Bruker). NanoScope software (v9.2, Bruker) was used for data collection and Gwyddion (v2.52, open source software covered by GNU general public license, www.gwyddion.net) and OriginPro (v8.5.1, OriginLab Corp.) software packages were used for data processing and analysis. The patterned surfaces with the immobilized protein molecules on them were imaged in PeakForce Tapping mode at nearly-physiological conditions in buffer (20 mM HEPES, pH 7.8), at room temperature using BL-AC40TS probes (Olympus). In this case, the Z-modulation amplitude was adjusted to values in the range 20-24 nm, while the Z-modulation frequency was 1 kHz and the contact tip-sample force was kept in the range 80-100 pN.

Huang X., Vasilev C, & Hunter C.N. (2020). Excitation energy transfer between monomolecular layers of light harvesting LH2 and LH1-reaction centre complexes printed on a glass substrate. Lab on a chip, 20(14).

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