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Orius digital camera

Manufactured by Ametek
Sourced in United States

The Orius digital camera is a versatile lab equipment device designed for high-quality imaging. It features a digital sensor and offers a range of resolution and connectivity options to support various imaging applications. The core function of the Orius digital camera is to capture and digitize visual information for analysis and documentation purposes.

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24 protocols using orius digital camera

1

Ultrastructural Analysis of Sirt2 Deficient T Cells

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TEM analysis was performed at the Lisa Muma Weitz Microscopy Core,
University of South Florida.
WT vs.
Sirt2−/− CD4+ OT-II
T cells at naïve, activated and memory stages, were fixed with 2.5%
glutaraldehyde in 0.1M phosphate buffer (Electron Microscopy Sciences, EMS).
Following fixation, samples were washed in 0.2M cocodylate buffer and post
fixed in 1% osmium tetroxide (EMS). After brief washing in distilled
H2O, samples were dehydrated in increasing ethanol
concentrations and incubated in three changes of EMbed 812 resin (EMS)
before a final embedding. After curing, cut sections of 90 nm were collected
on copper grids and stained with 2% aqueous uranyl acetate and lead citrate
(EMS). Images were obtained using a JEOL 1400 transmission electron
microscope equipped with side mounted Orius digital camera (Gatan).
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2

Quantifying Synaptic Ultrastructure Through Electron Microscopy

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Electron microscopy was performed as previously described (Watanabe et al., 2013 (link)). Freezing was performed on a Leica EMpact2 (Leica, Wetzlar, Germany). To stimulate neurotransmission animals were exposed to blue (488 nm) LED light for 20ms and frozen 50ms later. Thirty-three nm serial sections were taken and imaged using a Hitachi H-7100 transmission electron microscope equipped with a Gatan Orius digital camera (Gatan, Pleasanton, CA). Micrographs were analyzed in ImageJ using a program for morphological analysis of synapses (Watanabe et al., 2020 (link)). Scripts available at: https://github.com/shigekiwatanabe/SynapsEM (copy archived at Watanabe, 2022 ).
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3

Ultrastructural Analysis of Cells

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Cells (10 × 106 per condition) were pelleted for 5 minutes at RT at 300 × g and fixed in Karnovsky's fixative, followed by standard TEM ultrastructural analyses using JEOL JEM-1400 at 120kV by Stanford Electron Microscopy Core Facility. Photographs were taken using a Gatan Orius digital camera (NIH grant # 1S10RR02678001).
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4

Negative Staining of Extracellular Vesicles

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Sample was prepared as previously reported with slight modifications [33 ]. Isolated EVs were fixed in 2% paraformaldehyde (PFA) for 5 min. For negative-staining of EVs, 5μl of the sample solution was placed on a carbon coated EM grid and EVs were immobilized for 1 min. The grid was transferred to five 100 μl drops of distilled water and letting it for 2 min on each drop. The sample was negative-stained with 1% uranyl acetate. The excess uranyl acetate was removed by contacting the grid edge with filter paper and the grid was air-dried. The grids were imaged with a JEOL 100CXII Transmission Electron Microscope operating at 100 kV. Images were captured on a Gatan Orius Digital Camera.
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5

Negative-Staining of Extracellular Vesicles

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Isolated EVs were fixed in 2% paraformaldehyde (PFA) for 5 min. For negative-staining of EVs, 5μl of the sample solution was placed on a carbon-coated EM grid and EVs were immobilized for 1 min. Next, the grid was transferred to five 100μl drops of distilled water and letting it for 2 min on each drop. The sample was negative-stained with 1% uranyl acetate. The excess uranyl acetate was removed by contacting the grid edge with filter paper and the grid was air-dried. The grids were imaged with a JEOL 100CXII Transmission Electron Microscope operating at 100 kV. Images were captured on a Gatan Orius Digital Camera.
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6

Negative Staining of Proteins

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Negative staining was performed using substrate carbon-coated nickel grids (Proscitech Kirwan, Australia). Protein was loaded onto the grid and washed three times with milli-Q water. Subsequently, 2 % (w/v) uranyl acetate (ProsciTech Kirwan, Australia) in 0.22 μm sterile filtered milli Q water was added for 2 min to stain the proteins negatively. The grids were analysed using a JEOL 2011 TEM (Tokyo, Japan) operated at 200 kV and Images taken using a Gatan Orius digital camera (California, USA).
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7

Liposomal Suspension Characterization via TEM

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Liposomal suspensions were processed using carbon grids prior to staining with 1 % uranyl acetate solution for 1 min and drying. Observation of specimens was achieved using a transmission electron microscope (TEM) (Jeol-1010, JEOL) operated at 100 kV, with images acquired using a Orius digital camera (Gatan).
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8

Ultrastructural Analysis of Mouse and Human Pancreata

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Mouse and human pancreata were fixed in 2% glutaraldehyde in 0.1M PO4/100mM sucrose, overnight at 4°C. The next day, samples were rinsed with 0.15M PO4 three times, then post-fixed in 1% phosphate buffered osmium tetroxide overnight at 4°C. After fixation, samples were rinsed with 0.15M PO4 three times then dehydrated in an ascending series of cold ethanolic alcohols to 100% and infiltrated with a 1:1 mixture of propylene oxide and Epon-Araldite resin overnight at room temperature. The next day, the 1:1 mixture was replaced with fresh Epon-Araldite resin, left in the desiccator for 4 hours prior to being transferred to embedding molds and left to polymerize in a 64°C oven overnight. The resin blocks were removed from the molds, trimmed and cut using a Leica UC7 ultra-microtome. 100nm-sections were collected on Formvar coated copper grids and stained with uranyl acetate and lead citrate for contrast. Sections were scanned using a JEOL JEM-1400 transmission electron microscope equipped with a Gatan Orius digital camera.
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9

Ultrastructural Analysis of ACC Myelination

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TEM microscopy was conducted by following our previous established method (Hasan et al., 2019). Briefly, rats were perfused with 0.1 M PB followed by 2% glutaraldehyde/4% PFAin sodium cacodylate buffer. A block of approximately 1 × 1 × 2mm3 from the right ACC was dissected out and then post fixed with the primary fixative, then contrasted with 1% osmium tetroxide (v/v) in PBS. Tissues were dehydrated in an ethanol graded from 50 to 100% and embedded in Epon. Ultra-thin Slices (80 nm) was cut and stained with 2% uranyl acetate (v/v) and Reynold’s lead citrate and analyzed imaged with Gatan Orius digital camera. G-ratio is calculated by dividing the diameter of an axon by that of total fiber diameter (axon + myelin sheath) from 150-180 fibers in ACC.
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10

Immunolocalization of IP3 Receptors

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Briefly, cells were fixed with 3% paraformaldehyde/0.05% glutaraldehyde in 0.1 M phosphate buffer for 10 min, stained with uranyl acetate (2% w/v in distilled water), dehydrated through increasing concentrations of methanol (70%–100%), and embedded in LR Gold (London Resin Company). Ultrathin sections (50–80 nm) were prepared by use of a Reichert Ultracut S ultramicrotome (Leica), mounted on 200-mesh nickel grids, incubated at room temperature for 2 hr with a monoclonal anti-InsP3 receptor type I antibody (dilution 1:100; Abcam) and for 1 hr with anti-mouse IgG −15 nm gold complex (British Biocell International). All antisera were diluted in 0.1 M phosphate buffer containing 0.1% egg albumin (pH 7.2). As a control the primary antibody was replaced with non-immune sera. After immunolabeling, sections were lightly counterstained with lead citrate and uranyl acetate and examined with a JEOL transmission electron microscope (JEM-1010, JEOL), and images were collected with a Gatan Orius digital camera (Gatan).
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