4.2 scmos camera

Manufactured by Oxford Instruments

Sourced in Ireland

The 4.2 sCMOS camera is a scientific-grade imaging device designed for demanding low-light applications. It features a large active area, high-speed readout, and low-noise performance to capture high-quality images and data.

Automatically generated - may contain errors

Lab products found in correlation

Csu w1, by Yokogawa (3 mentions) Doxycycline hydrochloride, by Merck Group (2 mentions) Poly d lysine, by Thermo Fisher Scientific (2 mentions) Rna exporter, by Merck Group (2 mentions) Plan apo ph3 dm oil objective, by Oxford Instruments (2 mentions) Ix81 microscope, by Oxford Instruments (2 mentions) Eclipse ti, by Nikon (2 mentions) Highcontent screening microscope, by Oxford Instruments (2 mentions) Fura 2 am, by Thermo Fisher Scientific (2 mentions) Fibronectin, by Merck Group (1 mentions) Ab30394, by Abcam (1 mentions) Dragonfly spinning disk confocal system, by Oxford Instruments (1 mentions) Alexa fluor 488 phalloidin, by Thermo Fisher Scientific (1 mentions) Triton x 100, by Thermo Fisher Scientific (1 mentions) Eclipse ti microscope, by Oxford Instruments (1 mentions) Bovine serum albumin (bsa), by Thermo Fisher Scientific (1 mentions) L glutamine, by Thermo Fisher Scientific (1 mentions) Penicillin streptomycin, by Thermo Fisher Scientific (1 mentions) Fetal bovine serum (fbs), by Corning (1 mentions) Ix83 zdc2, by Olympus (1 mentions)

37 protocols using 4.2 scmos camera

Immunofluorescence of Integrin Receptors

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Human Foreskin Fibroblasts (HFF) were purchased from ATCC and cultured in DMEM media (Mediatech) supplemented with 10% Fetal Bovine Serum (Corning), 2 mM L-glutamine (Invitrogen) and penicillin-streptomycin (Invitrogen). HFFs were plated on glass coverslips incubated with 10 μg/mL fibronectin (EMD Millipore) for 1 hr at room temperature. Cells were fixed 1 hr after plating by rinsing them in cytoskeleton buffer (10 mM MES, 3 mM MgCl₂, 1.38 M KCl and 20 mM EGTA) and then fixed, blocked and permeabilized in 4% PFA (Electron Microscopy Sciences), 1.5% BSA (Fisher Scientific), and 0.5% Triton X-100 (Fisher Scientific) in cytoskeleton buffer at 37° for 10 minutes. Coverslips were subsequently rinsed three times in PBS and incubated with either a β₁ antibody (1:100; Abcam product #:ab30394) or β₃ antibody (1:100; Abcam product #:ab7166) followed by AlexaFluor 488 phalloidin (1:1000; Invitrogen) and a AlexaFluor647 donkey anti-mouse secondary antibody (1:200; Invitrogen).
Cells were imaged using a 1.2 NA 60X Plan Apo water immersion lens on an inverted Nikon Ti-Eclipse microscope using an Andor Dragonfly spinning disk confocal system and a Zyla 4.2 sCMOS camera. The microscope was controlled using Andor’s Fusion software.

Bidone T.C., Skeeters A.V., Oakes P.W, & Voth G.A. (2019). Multiscale model of integrin adhesion assembly. PLoS Computational Biology, 15(6), e1007077.

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Visualizing RNA Exporter Expression

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To image cells stably expressing RNA exporters, as shown in Figure S4E, we used the cell lines cFH38, which expresses the RNA exporter Gag-MCP and the reporter RNA mCherry-MS2×8, and cFH16, which expresses only the reporter RNA mCherry-MS2×8 (see “Cell line construction”). Wells of 24-well glass-bottom plates were coated with Poly-D-Lysine (ThermoFisher), then cFH38 or cFH16 cells were plated with 50,000 cells per well in media containing 1 ng/μL doxycycline hydrochloride to induce RNA exporter expression (Sigma). At 71 hours after plating, imaging was performed using a Nikon Ti Eclipse inverted confocal microscope equipped with a 50 μm pinhole spinning disk (Yokagawa), 60x Plan/Apo Ph3 DM oil objective (1.4 numerical aperture), and Andor Zyla 4.2 sCMOS camera. Background subtraction and independent rescaling of each color channel intensity to an identical range across samples was performed using scikit-image (0.19.2)^{84 (link)}.

Horns F., Martinez J.A., Fan C., Haque M., Linton J.M., Tobin V., Santat L., Maggiolo A.O., Bjorkman P.J., Lois C, & Elowitz M.B. (2023). Engineering RNA export for measurement and manipulation of living cells. Cell, 186(17), 3642-3658.e32.

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Time-Lapse Imaging of C. elegans in Microfluidics

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For microfluidics experiments, early to mid L1-staged animals were isolated through a 1-2 hours timed egg-lay approximately 12-14 hours at 20°C before an experimental time course. Animals were mounted into the microfluidic device as previously described.^{31 (link)} During the imaging process, animals were constantly fed NA22 E. coli suspended in S medium. Imaging was done with a 40x, 1.3NA objective using an Andor Zyla 4.2 scMOS camera. The temperature was kept constant at 20°C both, at the objective and the microfluidic device using a custom-built water-cooled aluminum ring (for objective) and custom-built aluminum stage inset that was directly coupled to a thermal Peltier device.^{31 (link)}

Stec N., Doerfel K., Hills-Muckey K., Ettorre V.M., Ercan S., Keil W, & Hammell C.M. (2020). An Epigenetic Priming Mechanism Mediated by Nutrient Sensing Regulates Transcriptional Output During C. elegans Development. Current biology : CB, 31(4), 809-826.e6.

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Live-cell Microscopy with Olympus IX83

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All images were recorded in a modified Olympus IX83 (Tokyo, Japan) with a 100 × 1.4 NA objective and an Andor Zyla 4.2 sCMOS camera with an effective pixel size of 65 nm in the images. CoolLED pE-4000 was used as the light source. Olympus IX83-ZDC2 was used to correct focus drift and an Olympus IX3-SSU ultrasonic stage was used for multipoint imaging. An Olympus double lamp housing U-DULHA was used to introduce a 405-nm diode laser used in microirradiation. An Okolab UNO (Naples, Italy) live-cell chamber supplied with humidified CO₂ and an objective heater was used.

Kesavan P.S., Bohra D., Roy S, & Mazumder A. (2020). Monitoring global changes in chromatin compaction states upon localized DNA damage with tools of fluorescence anisotropy. Molecular Biology of the Cell, 31(13), 1403-1410.

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Imaging Ca2+ Dynamics in Cardiomyocytes

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Ca²⁺ cycles of CMs were imaged at 20× magnification using a Nikon ECLIPSE Ti-S fluorescent microscope and recorded using an Andor Zyla 4.2 sCMOS camera at 30 frames/s for 30 s. Ca²⁺ transients are detected as fluorescent emissions using a fluorescein isothiocyanate (FITC) filter cube. Video data were analyzed using Nikon’s NIS-Elements AR to isolate single CMs as ROIs and obtain fluorescent intensity over time data for individual CMs per frame.

Pang J.K., Chia S., Zhang J., Szyniarowski P., Stewart C., Yang H., Chan W.K., Ng S.Y, & Soh B.S. (2022). Characterizing arrhythmia using machine learning analysis of Ca2+ cycling in human cardiomyocytes. Stem Cell Reports, 17(8), 1810-1823.

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Imaging Zebrafish Embryos Using Confocal Microscopy

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All imaged embryos were immobilised with tricaine (0.08 mg/ml) and mounted laterally in 1% low-melting agarose (Sigma-Aldrich, A9414-100G) for still images and 0.7% agarose for time-lapse Videos. Zebrafish embryos were imaged at the Australian Cancer Research Foundation’s Cancer Ultrastructure and Function Facility at the Institute for Molecular Bioscience in Brisbane, Australia using a Zeiss LSM 710 FCS confocal microscope and an Andor Dragonfly Spinning Disc Confocal microscope with the Zyla 4.2 sCMOS camera (exclusively for Video 2 and Figure 1—figure supplement 1F), or at the National Cerebral and Cardiovascular Center Research Institute in Osaka, Japan on an OLYMPUS confocal microscope (FluoView FV1000 and FV1200). All embryos analysed for quantification of signal intensity were heterozygous carriers for each transgene and imaged with the same imaging settings for each experiment with neuronal and muscle transplantations being the exception.

Grimm L., Nakajima H., Chaudhury S., Bower N.I., Okuda K.S., Cox A.G., Harvey N.L., Koltowska K., Mochizuki N, & Hogan B.M. (2019). Yap1 promotes sprouting and proliferation of lymphatic progenitors downstream of Vegfc in the zebrafish trunk. eLife, 8, e42881.

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Quantifying Telomere Colocalization Microscopy

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All ICC and CO-FISH micrographs were taken on a Nikon Eclipse TE2000-E with a 100× objective using an Andor Zyla 4.2 sCMOS camera. Images were acquired using Nikon NIS-Elements. For experiments in which two or more conditions were quantitatively compared, the same exposure and acquisition settings were used for each image. APB, TIF, and EdU colocalization with telomeres were automatically processed using ImageJ with ComDet plugin.

Turkalo T.K., Maffia A., Schabort J.J., Regalado S.G., Bhakta M., Blanchette M., Spierings D.C., Lansdorp P.M, & Hockemeyer D. (2023). A non-genetic switch triggers alternative telomere lengthening and cellular immortalization in ATRX deficient cells. Nature Communications, 14, 939.

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Multimodal Microscopy Imaging

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Differential interference contrast (DIC), phase-contrast, and fluorescence microscopy analyses were performed using a Nikon Eclipse 80i microscope equipped with an X-Cite TURBO multiwavelength LED illumination system and an Andor Zyla 4.2 sCMOS camera, as described previously (24 (link)). Quantitative image analyses were performed using the Oufti and MicrobeJ software packages (63 (link), 64 (link)).

Ozaki S., Wakasugi Y, & Katayama T. (2021). Z-Ring-Associated Proteins Regulate Clustering of the Replication Terminus-Binding Protein ZapT in Caulobacter crescentus. mBio, 12(1), e02196-20.

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Measuring Podocyte Calcium Dynamics

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Human podocytes AB8/13 grown on glass coverslips and glomeruli attached to poly-L-lysine covered coverslips were loaded with 2 μM Fura-2AM in the presence of 0.025% Pluronic for 40 min at room temperature. The extracellular solution contained (in mM): 140 NaCl, 5.4 KCl, 1 MgCl₂, 2 CaCl₂, 0.33 Na₂HPO₄, 10 Glucose, 10 HEPES-NaOH (pH 7.4). In experiments with 0.5 and 50 mM KCl, the concentration of NaCl was appropriately adjusted.
Cells were excited at 340 and 380 nm wavelengths for 100 ms every 2 s by using Lambda 10-B filter changer (Sutter Instruments, Novato, CA, USA). Emission fluorescence was registered at >510 nm with a Zyla 4.2 sCMOS camera operated by µManager open-source microscopy software. Further analysis was performed in FiJi/ImageJ software. The change in cytosolic Ca²⁺ concentration was estimated from the ratio of emission fluorescence intensities at 340 and 380 nm excitation wavelengths. The reagents were purchased from Sigma-Aldrich (St. Louis, MO, USA). Fura-2AM was purchased from Thermo Fisher Scientific Inc. (Waltham, MA, USA).

Gusev K., Shalygin A., Kolesnikov D., Shuyskiy L., Makeenok S., Glushankova L., Sivak K., Yakovlev K., Orshanskaya Y., Wang G., Bakhtyukov A., Derkach K., Shpakov A, & Kaznacheyeva E. (2023). Reorganization and Suppression of Store-Operated Calcium Entry in Podocytes of Type 2 Diabetic Rats. International Journal of Molecular Sciences, 24(8), 7259.

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Quantifying MCF10A Cell Proliferation

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Cell proliferation was measured over a period of 4 days after seeding cells at an initial density of 2600 cells/cm². MCF10A NLS copGFP proliferation was continuously monitored by a custom epifluorescence microscope housed in a standard tissue culture incubator (37°C, 90% humidity, 5% CO₂; 10× objective; 1-hour acquisition intervals). Cell numbers were quantified manually every 24 hours using ImageJ. To measure cell viability, cells were seeded at a density of 1300 cells/cm² on fibronectin-functionalized PA and silicone gels in a 12-well plate and assayed after 24 hours with a LIVE/DEAD Viability/Cytotoxicity kit (Thermo Fisher Scientific). Fluorescence images were acquired using GFP and TXRED filter cubes on an Olympus IX81 microscope with a 10× objective (0.25 NA; Zyla 4.2 sCMOS camera) and quantified manually in ImageJ.
Cell proliferation analysis by assaying Ki-67 protein was done as follows: MCF10A cells were seeded at an initial density of 2600 cells/cm², cultured for 48 hours after seeding, and then fixed using 4% paraformaldehyde at room temperature for 30 min. Samples were incubated with Ki-67 primary antibody, followed by Alexa Fluor–conjugated secondary antibody. Nuclei were stained with Hoechst. The number of Ki-67–positive cells and total number of cells were counted manually with ImageJ.

Cheng Z., Shurer C.R., Schmidt S., Gupta V.K., Chuang G., Su J., Watkins A.R., Shetty A., Spector J.A., Hui C.Y., Reesink H.L, & Paszek M.J. (2020). The surface stress of biomedical silicones is a stimulant of cellular response. Science Advances, 6(15), eaay0076.

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