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Axioscope

Manufactured by Nikon
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Sourced in Germany

The Axioscope is a microscope system designed for high-quality imaging and analysis in various laboratory applications. It features advanced optics, precise focusing mechanisms, and a modular design to accommodate a range of accessories and configurations. The Axioscope provides consistent and reliable performance to support your research and analytical needs.

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Lab products found in correlation

Eclipse ni u, by Nikon (4 mentions) Tecnai g2 12, by Thermo Fisher Scientific (2 mentions) Digital sight camera, by Nikon (2 mentions) Orca er digital camera, by Hamamatsu Photonics (1 mentions) Eclipse 90i, by Nikon (1 mentions) Axioskop 2 plus microscope, by Zeiss (1 mentions) Lsm 5 exciter microscope, by Zeiss (1 mentions) Ds fi2 digital camera, by Nikon (1 mentions)

Spelling variants of this product

Axioscope microscope (4 citations) Axioscope fluorescence microscope (3 citations) Axioscope-A1 (2 citations)

7 protocols using axioscope

1

Fluorescence Microscopy Imaging of Fusion Proteins

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The distribution of various fusion proteins (or RFP fusions) was analyzed with a ×100 PlanApochromat objective (NA = 1.4) either using an Olympus IX-81 inverted microscope equipped with a Hamamatsu Orca/ER digital camera (Hamamatsu Photonics, Hamamatsu City, Japan) and an Olympus (Tokyo, Japan) CellR detection and analyzing system (GFP filter block U-MGFPHQ, exc. max. 488, em. max. 507; RFP filter block U-MWIY2, exc. max. 545–580, em. max. 610; DAPI filter block U-MNUA2, exc. max. 360–370, em. max. 420–460), a Leica TCS SP5 AOBS confocal laser scanning system (Leica Microsystems, Wetzlar, Germany) coupled to a Leica DMI 6000 Cs inverted microscope, a Carl Zeiss AG Axioscope (Oberkochen, Germany) or Nikon (Tokyo, Japan) Eclipse Ni-U equipped with a DS-Fi2 digital camera.
Bischof J., Salzmann M., Streubel M.K., Hasek J., Geltinger F., Duschl J., Bresgen N., Briza P., Haskova D., Lejskova R., Sopjani M., Richter K, & Rinnerthaler M. (2017). Clearing the outer mitochondrial membrane from harmful proteins via lipid droplets. Cell Death Discovery, 3, 17016-.
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2

Ultrastructural Analysis of Skin Samples

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Skin samples were fixed in 2% glutaraldehyde, 4% paraformaldehyde, and 2 mM CaCl2 in 0.1 M sodium cacodylate buffer (pH 7.2) for >1 hour at room temperature, post-fixed in 1% osmium tetroxide, and processed for Epon embedding; ultrathin sections (60–65 nm) were counterstained with uranyl acetate and lead citrate. Images were acquired with a transmission electron microscope (TEM, Tecnai G2–12; FEI, Hillsboro, OR) equipped with a digital camera (AMT BioSprint29). Semithin sections (800 nm) were stained with toluidine blue and photographed with a Zeiss Axio Scope equipped with a Nikon Digital Sight camera.
Cutler RE J.r., Stephens R.M., Saracino M.R, & Morrison D.K. (1998). Autoregulation of the Raf-1 serine/threonine kinase. Proceedings of the National Academy of Sciences of the United States of America, 95(16), 9214-9219.
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3

FM4-64 Staining in Yeast Cells

Cited 1 time
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FM4-64 staining with small modifications was performed as described [52 (link)]. Yeast cells were diluted to an OD600 = 0.1 and were grown for 12 h in liquid SC-medium. An aliquot (2 mL) was washed once in YEPD and resuspended in 100 µL YEPD supplemented with 20 µM FM4-64. After a 20 min incubation at 28 °C, cells were wash with SC-medium and incubated for 1 h in 100 µL liquid SC medium. Moreover, 50 µL of this cell suspension was used as a control, 50 µL was supplemented with 1 M NaCl and incubated for >30 min. Cells stained by FM4-64 were analyzed with a × 100 objective (NA = 1.4) using either a Carl Zeiss AG Axioscope (Oberkochen, Germany) or a Nikon (Tokyo, Japan) Eclipse Ni-U equipped with a DS-Fi2 digital camera.
Weber M., Basu S., González B., Greslehner G.P., Singer S., Haskova D., Hasek J., Breitenbach M., W.Gourlay C., Cullen P.J, & Rinnerthaler M. (2021). Actin Cytoskeleton Regulation by the Yeast NADPH Oxidase Yno1p Impacts Processes Controlled by MAPK Pathways. Antioxidants, 10(2), 322.
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4

Ultrastructural Analysis of Skin Samples

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Skin samples were fixed in 2% glutaraldehyde, 4% paraformaldehyde, and 2 mM CaCl2 in 0.1 M sodium cacodylate buffer (pH 7.2) for >1 hour at room temperature, post-fixed in 1% osmium tetroxide, and processed for Epon embedding; ultrathin sections (60–65 nm) were counterstained with uranyl acetate and lead citrate. Images were acquired with a transmission electron microscope (TEM, Tecnai G2–12; FEI, Hillsboro, OR) equipped with a digital camera (AMT BioSprint29). Semithin sections (800 nm) were stained with toluidine blue and photographed with a Zeiss Axio Scope equipped with a Nikon Digital Sight camera.
Liu S., Hur Y.H., Cai X., Cong Q., Yang Y., Xu C., Bilate A.M., Gonzales K.A., Parigi S.M., Cowley C.J., Hurwitz B., Luo J.D., Tseng T., Gur-Cohen S., Sribour M., Omelchenko T., Levorse J., Pasolli H.A., Thompson C.B., Mucida D, & Fuchs E. (2023). A tissue injury sensing and repair pathway distinct from host pathogen defense. Cell, 186(10), 2127-2143.e22.
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5

Quantifying Hippocampal Neurogenesis in Mice

Cited 1 time
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The slides containing the sections were coded and quantification performed by an experimenter blind to the code. BrdU-positive cells were counted within the SGZ [15] (link) on a Zeiss Axioskop-2 Plus microscope. The number of BrdU-positive cells per section was determined by assessing every sixth section across the rostro-caudal extent of the hippocampus (10 sections/animal). The number of DCX- and GFP-positive cells in the dentate gyrus was quantified (four sections per animal) using a Zeiss Axioscope and Nikon Eclipse 90i fluorescence microscope, respectively. The cell counts are plotted as a percentage of the control (vehicle-treated) for each adrenergic receptor agonist and antagonist. The numbers of cells/section for all treatment conditions are shown in Table S1.
The number of Nestin-GFP/GFAP double-positive cells was quantified by determining the percentage of GFP-positive cells that colocalized with GFAP using confocal microscopy. At least 50 GFP-positive cells from each animal (four sections per animal) were analyzed using z-plane confocal sectioning with 1 µm steps on a Zeiss LSM5 Exciter microscope.
Jhaveri D.J., Nanavaty I., Prosper B.W., Marathe S., Husain B.F., Kernie S.G., Bartlett P.F, & Vaidya V.A. (2014). Opposing Effects of α2- and β-Adrenergic Receptor Stimulation on Quiescent Neural Precursor Cell Activity and Adult Hippocampal Neurogenesis. PLoS ONE, 9(6), e98736.
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6

Fluorescent Protein Co-localization Analysis

Cited 1 time
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The fusion proteins (either GFP or RFP fusions) were analysed with a × 100 objective (NA = 1.4) using either a Carl Zeiss AG Axioscope (Oberkochen, Germany) or a Nikon (Tokyo, Japan) Eclipse Ni-U equipped with a DS-Fi2 digital camera. The grade of co-localization was quantified as described in Rinnerthaler et al. (Rinnerthaler et al., 2013 (link)) using the Co-localization Finder plugin as part of NIH ImageJ software.
Streubel M.K., Bischof J., Weiss R., Duschl J., Liedl W., Wimmer H., Breitenbach M., Weber M., Geltinger F., Richter K, & Rinnerthaler M. (2017). Behead and live long or the tale of cathepsin L. Yeast (Chichester, England), 35(2), 237-249.
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7

Quantitative Co-localization Analysis

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The fusion proteins (either GFP or RFP fusions) were analysed with a × 100 objective (NA  =  1.4) using either a Carl Zeiss AG Axioscope (Oberkochen, Germany) or a Nikon (Tokyo, Japan) Eclipse Ni‐U equipped with a DS‐Fi2 digital camera. The grade of co‐localization was quantified as described in Rinnerthaler et al. (Rinnerthaler et al., 2013) using the Co‐localization Finder plugin as part of NIH ImageJ software.
Streubel M.K., Bischof J., Weiss R., Duschl J., Liedl W., Wimmer H., Breitenbach M., Weber M., Geltinger F., Richter K, & Rinnerthaler M. (2017). Behead and live long or the tale of cathepsin L. Yeast (Chichester, England), 35(2), 237-249.
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