Digital camera

Manufactured by Hamamatsu Photonics

Sourced in Japan, United States

The digital camera is an electronic device designed to capture and record visual images. It converts light into electrical signals, which are then processed and stored in a digital format. The camera's core function is to enable the user to capture and store visual information for various purposes.

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Lab products found in correlation

Embed 812, by Electron Microscopy Sciences (5 mentions) Cell lysis buffer, by Cell Signaling Technology (3 mentions) Chemiluminescence detection kit, by Hamamatsu Photonics (3 mentions) Vectashield, by Vector Laboratories (2 mentions) Em ace600 coater, by Hitachi (2 mentions) Ht7700, by Hitachi (2 mentions) Su3500, by Hitachi (2 mentions) Advantage image capture software, by Hamamatsu Photonics (2 mentions) Em 208 microscope, by Hamamatsu Photonics (2 mentions) Em uc6 ultramicrotome, by Leica (2 mentions) Ix 81 optical microscope, by Olympus (2 mentions) 4 6 diamidino 2 phenylindole (dapi), by Thermo Fisher Scientific (2 mentions) Bicinchoninic acid assay, by Thermo Fisher Scientific (2 mentions) Fura 2 am, by Thermo Fisher Scientific (2 mentions) Rabbit anti myogenin, by Santa Cruz Biotechnology (1 mentions) Toto 3, by Thermo Fisher Scientific (1 mentions) Tcs2 confocal microscope, by Leica (1 mentions) Eclipse e1000 microscope, by Nikon (1 mentions) Axioplan 2 epifluorescence microscope, by Zeiss (1 mentions) Mitotracker red cmxros, by Thermo Fisher Scientific (1 mentions)

46 protocols using digital camera

Immunofluorescence Staining of Muscle Cells

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Cells were fixed in 4% paraformaldehyde for 10 min, permeabilized with 0.1% Triton X-100 for 10 min, blocked with PBS containing 2% bovine serum albumin (BSA) plus 5% normal goat serum for 1 h, and incubated overnight at 4°C with mouse anti-desmin antibody (1:50; DakoCytomation, Carpinteria, CA), rabbit anti-myogenin (1:50; Santa Cruz Biotechnology), or mouse anti–myosin heavy chain (1:20; Developmental Studies Hybridoma Bank). After three washes with PBS, cells were incubated with Alexa Fluor 546–conjugated or Alexa Fluor 488–conjugated secondary antibodies (Molecular Probes, Eugene, OR) for 1 h at room temperature and washed with PBS. Nuclei were counterstained with either 4′,6-diamidino-2-phenylindole (DAPI; 100 ng/ml) or TOTO-3 (2.4 nM; Molecular Probes). Slides were then mounted in Vectashield (Vector Laboratories, Burlingame, CA). Cells were visualized using an Eclipse E-1000 microscope (Nikon, Melville, NY) and photographed using a Hamamatsu digital camera (Hamamatsu, Bridgewater, NJ), and images were acquired using Openlab software, version 3.1.5 (Improvision, PerkinElmer, Waltham, MA). For confocal imaging, all images were acquired with a 40×/1.25 numerical aperture oil immersion objective using a TCS2 confocal microscope (Leica, Wetzlar, Germany).

Teng S., Stegner D., Chen Q., Hongu T., Hasegawa H., Chen L., Kanaho Y., Nieswandt B., Frohman M.A, & Huang P. (2015). Phospholipase D1 facilitates second-phase myoblast fusion and skeletal muscle regeneration. Molecular Biology of the Cell, 26(3), 506-517.

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Visualizing Msp1 localization in yeast

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Localization studies were performed with GFP-tagged Msp1 on a YCplac33 plasmid in diploid W303-1 S. cerevisiae, which were haploid for chromosomal Msp1 and Get3. Yeast cultures were grown in SD-Ura medium overnight and then 1 mL of culture was mixed with 10 μL of 10 μM MitoTracker Red CMXRos (Thermo Scientific). Culture was incubated at 30° C for 15 min, pelleted, washed in SD-Ura, and then resuspended in SD-Ura. Static images were captured with living cells that were compressed beneath a coverslip without fixation and then immediately viewed. To capture static images by widefield microscopy, we used an Axioplan2 epifluorescence microscope (Zeiss) equipped with a 1.4-NA 100x Plan Apo objective and a digital camera (Hamamatsu) (Papanikou et al., 2015 ). ImageJ (Schneider et al., 2012 (link)) was used to colorize, adjust brightness, and merge the images.

Wohlever M.L., Mateja A., McGilvray P.T., Day K.J, & Keenan R.J. (2017). Msp1 is a membrane protein dislocase for tail-anchored proteins. Molecular cell, 67(2), 194-202.e6.

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Immunocytochemical Analysis of Glial Cells

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The cells were fixed in 4% paraformaldehyde (Sigma) in 1× PBS for 20 min, washed three times in PBS, and then blocked with 1× PBS containing 1% bovine serum albumin and 0.25% Triton X-100. The same solution was used during the incubations with the primary antibodies. The cells were incubated with antibodies overnight at 4°C. Fluorochrome-conjugated secondary antibodies were used for immunodetection. The primary antibodies were mouse antiglial fibrillary acidic protein (anti-GFAP) 1:1000 (Abcam) and rabbit anti-Galactocerebroside (anti-GalC) 1:500 (Abcam). The secondary antibodies were donkey anti-mouse conjugated with Alexa Fluor 568 1:1000 (Invitrogen); donkey anti-rabbit conjugated with Alexa Fluor 488 1:1000 (Dianova). Nuclear counterstaining was performed with 4′,6′-diamidino-2-phenylindole dihydrochloride hydrate at 0.25 μg/ml (Sigma). Coverslips were mounted onto glass slides using a Prolong Antifade kit (Invitrogen). The cells were quantified and photographed using an Olympus IX81 fluorescent microscope equipped with a Hamamatsu digital camera. For each culture condition, ten randomly selected fields were photographed, and the frequency of selected cellular markers was determined for every condition in three independent experiments.

Song P., Xia X., Han T., Fang H., Wang Y., Dong F., Zhang R., Ge P, & Shen C. (2018). BMSCs promote the differentiation of NSCs into oligodendrocytes via mediating Id2 and Olig expression through BMP/Smad signaling pathway. Bioscience Reports, 38(5), BSR20180303.

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Ultrastructural Analysis of Spinal Cord Axons

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Spinal cords from 16 animals were surveyed by light microscopy, of which 6 spinal cords were examined by EM to find 33 axon tips. Spinal cords were immersion-fixed with 4.0% paraformaldehyde in 0.1 M sodium cacodylate buffer (pH 7.4) overnight at 4°C. After subsequent buffer washes, the samples were post-fixed in 2.0% osmium tetroxide for 1 hour at room temperature, and rinsed in dH₂O. After dehydration through serial ethanols, the tissue was infiltrated and embedded in EMbed-812 (Electron Microscopy Sciences). The spinal cords containing labeled axon tips were sectioned longitudinally with a Leica ultramicrotome. Semithin (1 μm) sections were stained with toluidine blue to aid in orientation. Thin sections were mounted on Formvar-coated slot grids, stained with uranyl acetate-lead citrate and examined under the EM (JEOL JEM 1010, Japan) fitted with a Hamamatsu digital camera and AMT Advantage image capture software.

Jin L.Q., Pennise C.R., Rodemer W., Jahn K.S, & Selzer M.E. (2016). Protein Synthetic Machinery and mRNA in Regenerating Tips of Spinal Cord Axons in Lamprey. The Journal of comparative neurology, 524(17), 3614-3640.

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Immunofluorescence Staining of Stress Proteins

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Cells, plated with test agents in 8-well chamber slides, were first fixed using 4% formalin, lightly permeabilised with 0.1% Triton X100 for 5 min and blocked with a Tris buffer (25 mM, pH 8.4) that contained 7.5% pre-immuned goat serum for 1 h. Primary antibodies (including anti-HSP27, anti-phospho-HSP27 (S86), anti-caspases), diluted in the blocking buffer was added to the respective slides which were kept in the dark at full humidity on a slow moving platform for 1 h, and then washed thoroughly. FITC-tagged secondary antibodies were then added. After 1 h, the slides were washed thoroughly and mounted using FluorSave™ (Calbiochem, Nottingham, UK). TRITC-conjugated phalloidin was diluted at final concentration of 10 μg/ml and added to the cells together with the secondary antibodies. The slides were examined on an Olympus microscope and photographed using a Hamamatsu digital camera. The staining intensity was determined using ImageJ software.

Owen S., Zhao H., Dart A., Wang Y., Ruge F., Gao Y., Wei C., Wu Y, & Jiang W.G. (2016). Heat shock protein 27 is a potential indicator for response to YangZheng XiaoJi and chemotherapy agents in cancer cells. International Journal of Oncology, 49(5), 1839-1847.

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TEM Imaging of Peptide Aggregates

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TEM samples were prepared by placing ~3 μL of an aggregated peptide solution on a thin carbon film (deposited on a copper grid) which was initially made hydrophilic through glow discharging. After 1 minute, the solution was gently blotted with filter paper and then ~3 μL of a 1% uranyl acetate solution (pH 4.5) was added to stain the sample. The resultant solution was then blotted, which was followed by another round of staining using the same procedure. TEM image was obtained with a JEOL 1010 transmission electron microscope operated at 80 KV, equipped with a Hamamatsu digital camera (250,000 magnification) and the images were processed using the free AMT Advantage Image Capture software.

Hilaire M.R., Ding B., Mukherjee D., Chen J, & Gai F. (2018). Possible Existence of α-Sheets in the Amyloid Fibrils Formed by a TTR105–115 Mutant. Journal of the American Chemical Society, 140(2), 629-635.

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Quantifying Intracellular Oxidative Stress in OSNs

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The membrane-permeable probe 5-(6)-chloromethyl-2′,7′-dichloro-dihydro-fluorescein diacetate (CM-H₂DCFDA) (Molecular Probes, Eugene, OR, USA) enters the cells and produces a fluorescent signal after intracellular oxidation by ROS (Chernyak et al., 2006 (link)). We monitored intracellular oxidative stress by measurement of intracellular fluorescence intensity of CM-H₂DCFDA in a Wallac 1420 Victor multilabel counter (Wallac, Turku, Finland) using excitation and emission wavelengths of 485 and 535 nm, respectively. Fluorescence measurements were taken using Wallac 1420 Workstation software (version 2.00). H₂O₂ was used as a standard for intracellular ROS production. For fluorescence microscopic observation of intracellular ROS production upon odorant stimulation in OSN cultures, OSNs were loaded with 10 μM CM-H₂DCFDA for 30 min at 37°C and washed with phosphate-buffered saline buffer. OSNs were sampled randomly using a Zeiss Axiovert 200 fluorescence microscope (Carl Zeiss MicroImaging Inc., Thomsonwood, NY, USA) equipped with a Hamamatsu digital camera (Hamamatsu, Bridgewater, NJ, USA) and Openlab image analysis software (Improvision Inc., Lexington MA, USA).

Kim S.Y., Mammen A., Yoo S.J., Cho B.K., Kim E.K., Park J.I., Moon C, & Ronnett G.V. (2015). Phosphoinositide and Erk signaling pathways mediate activity-driven rodent olfactory sensory neuronal survival and stress mitigation. Journal of neurochemistry, 134(3), 486-498.

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Time-lapse Imaging of Laminin Dynamics

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Phase contrast images were obtained using a Nikon Eclipse TE2000-E inverted microscope equipped with a 37°C and 5% CO₂ incubation chamber, 63x oil objective, and a motorized stage (Prior Scientific). Metamorph software (Molecular Devices) with the multidimensional acquisition plugin was used to capture images and control all hardware. Images were acquired using a 63x oil objective and digital camera (Hamamatsu Photonics). Regular time-lapse imaging was performed in ~20 locations at 5min intervals over two 24-hour periods, while high time-resolution imaging was performed in one location at 5s intervals. Laminin fluorescence was detected using epifluorescence illumination with a mercury lamp and a 488 nm filter cube.

Smirnov M.S., Cabral K.A., Geller H.M, & Urbach J.S. (2014). The effects of confinement on neuronalgrowth cone morphology and velocity. Biomaterials, 35(25), 6750-6757.

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Phosphorylation of Syk and Src Kinases

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After stimulation platelets were immediately lysed on ice using cell lysis buffer (Cell Signaling Technology, USA). Protein concentration was determined using BCA (bicinchoninic acid) protein assay reagent kit according to the manufacturer’s protocol. Equal amounts of protein were separated by gel electrophoresis (SDS-PAGE) and blotted onto a nitrocellulose membrane. Membranes were blocked by incubation 5% (w/v) BSA in Tris-buffered saline with Tween (TBST) for 30 min prior to incubation at 4 °C overnight with indicated antibodies. Rabbit anti-human phospho-Syk Tyr525/526 (clone C87C1, Cat No. 2710), anti-human Syk (polyclonal, Cat No. 2712), anti-human p-Src Tyr416 (clone D49G4, Cat No. 6943), anti-human Src (clone 36D10, Cat No. 2109), and anti-beta-actin (clone D6A8, Cat No. 8457) were from Cell Signaling Technology. Anti-phospho-PLCγ2 (clone #1016D, Cat No. MAB74542) was from R&D Systems. After washing with TBST the membrane was incubated with a horseradish peroxidase conjugated secondary antibody for 1 h at room temperature. Enzymatic activity was detected with a chemiluminescence detection kit according to the supplier’s protocol and recorded with a digital camera (Hamamatsu). Densitometric analysis of the blots was carried out digitally using HOKAWO Software.

Pircher J., Czermak T., Ehrlich A., Eberle C., Gaitzsch E., Margraf A., Grommes J., Saha P., Titova A., Ishikawa-Ankerhold H., Stark K., Petzold T., Stocker T., Weckbach L.T., Novotny J., Sperandio M., Nieswandt B., Smith A., Mannell H., Walzog B., Horst D., Soehnlein O., Massberg S, & Schulz C. (2018). Cathelicidins prime platelets to mediate arterial thrombosis and tissue inflammation. Nature Communications, 9, 1523.

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TNFR2 Expression Analysis in HMEC

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Western blot analysis was performed as previously described [19] (link). HMEC were grown to subconfluence and starved for 24 hours in cell medium containing 1% FCS prior to stimulation with poly (I:C) for the indicated time intervals. After washing with PBS the cells were lysed on ice using cell lysis buffer (Cell Signaling Technology, USA) and protein concentration was determined using BCA (bicinchoninic acid) protein assay reagent kit according to the manufacturer's protocol. Equal amounts of protein were separated by gel electrophoresis (SDS-PAGE) and blotted onto a nitrocellulose membrane. Membranes were blocked by incubation 5% (w/v) BSA in TBSt (Tris-buffered saline with Tween) for 30 minutes prior to incubation with a rabbit anti-human-TNFR2-antibody (Cell signaling Technology, USA) at 4°C overnight. After washing with TBSt the membrane was incubated with a horseradish peroxidase conjugated secondary antibody for 1 hour at room temperature. Enzymatic activity was detected with a chemiluminescence detection kit according to the supplier's protocol and recorded with a digital camera (Hamamatsu). GAPDH served as loading control. Densiometric analysis of the blots was performed digitally using WASABI Software.

Pircher J., Czermak T., Merkle M., Mannell H., Krötz F., Ribeiro A., Vielhauer V., Nadjiri J., Gaitzsch E., Niemeyer M., Porubsky S., Gröne H.J, & Wörnle M. (2014). Hepatitis C Virus Induced Endothelial Inflammatory Response Depends on the Functional Expression of TNFα Receptor Subtype 2. PLoS ONE, 9(11), e113351.

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