Apotome 2 fluorescence microscope

Manufactured by Zeiss

Sourced in Germany

The ApoTome.2 is a fluorescence microscope designed for optical sectioning and high-contrast imaging of fluorescently labeled samples. It utilizes a structured illumination technique to provide optical sectioning, enabling the capture of sharp, in-focus images from thicker specimens.

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Lab products found in correlation

Lsm800 confocal microscope, by Zeiss (2 mentions) Hoechst 33342, by Thermo Fisher Scientific (1 mentions) Hoechst 33342, by Dojindo Laboratories (1 mentions) Propidium iodide, by Merck Group (1 mentions) Anti flag antibody, by Merck Group (1 mentions) Goat anti mouse dylight 488, by Thermo Fisher Scientific (1 mentions) Mouse anti zo 1, by BD (1 mentions) Rabbit anti ibai, by Fujifilm (1 mentions) Mouse anti gfap, by Abcam (1 mentions) Mouse anti neun, by Merck Group (1 mentions) Axio observer, by Zeiss (1 mentions) Zen 2012, by Zeiss (1 mentions) Alexa fluor conjugated secondary antibody, by Thermo Fisher Scientific (1 mentions) 4 6 diamidino 2 phenylindole dihydrochloride dapi, by Thermo Fisher Scientific (1 mentions) Alizarin red staining, by Merck Group (1 mentions) Paraformaldehyde (pfa), by Thermo Fisher Scientific (1 mentions) Bovine serum albumin (bsa), by Thermo Fisher Scientific (1 mentions) Alexa fluor 594 conjugated anti rabbit secondary antibody, by Cell Signaling Technology (1 mentions) Triton x, by Merck Group (1 mentions) Vectashield antifade mounting medium with dapi, by Vector Laboratories (1 mentions)

Close spelling variants of this product

ApoTome fluorescence microscope ApoTome.2 microscope Apotome microscope ApoTome.2 Fluorescence microscope Apotome

11 protocols using apotome 2 fluorescence microscope

Imaging LRRF1 recruitment in Chlamydia

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HeLa cells seeded on glass coverslips were infected with the C. trachomatis L2 CT226_FLAG transformants and either not induced or induced for expression at 7 hpi using 5 nM or 20 nM aTc. At 24 hpi, coverslips were fixed with 3% formaldehyde and 0.022% glutaraldehyde in dPBS, permeabilized with methanol, and stained for immunofluorescence to visualize construct expression (FLAG; red), chlamydiae (MOMP; gray), DNA (DAPI; blue), and either LRRF1 (green) or FLII (green). Coverslips were imaged using a Zeiss LSM 800 confocal microscope at a ×63 magnification with a ×2 zoom. Images were captured using the same exposure time (set to that for the samples induced with 20 nM aTc) for uninduced and 5 nM aTc-induced samples.
To examine LRRF1 recruitment using a normal exposure time, HeLa cells seeded on glass coverslips were infected with C. trachomatis L2 CT226_FLAG transformants and either not induced or induced for expression at 7 hpi using 5 nM aTc. At 24 hpi, coverslips were fixed with 4% paraformaldehyde, permeabilized with 0.5% Triton X-100, and stained for immunofluorescence to visualize construct expression (FLAG; red), LRRF1 (green), GFP-expressing chlamydiae (pseudoblue), and DNA (DAPI; blue). Coverslips were imaged using a Zeiss ApoTome.2 fluorescence microscope at a ×100 magnification.

Olson M.G., Widner R.E., Jorgenson L.M., Lawrence A., Lagundzin D., Woods N.T., Ouellette S.P, & Rucks E.A. (2019). Proximity Labeling To Map Host-Pathogen Interactions at the Membrane of a Bacterium-Containing Vacuole in Chlamydia trachomatis-Infected Human Cells. Infection and Immunity, 87(11), e00537-19.

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Unveiling A549 Cell Death Mechanism via Dual Staining

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To know the mechanism of A549 cell death upon the CA extract treatment, the A549 cells were observed every 6 h. After finding A549 cell blebs 12 h after being treated with CA extract, a staining experiment was carried out in order to see the phenomenon more clearly. A staining experiment was performed through dual staining of Hoechst 33342 (Dojindo) and propidium iodide (PI) (Sigma-Aldrich). The A549 cells were seeded on a cover glass and incubated for 24 h. The cells were then treated with 10 µg/mL CA extract and incubated for 12 and 24 h before being transferred to a preparatory glass. The cells were washed with non-phenol red RPMI medium (Gibco) and stained with 100 μL PI and 100 μL Hoechst 33342. A549 cells were then incubated for 20 min at room temperature and in a dark room. A549 cells were then viewed under Apotome.2 fluorescence microscope (Zeiss, Oberkochen, Germany) with FIT-C (red) and DAPI (blue) filter. This experiment was performed in triplicate.

Hadisaputri Y.E., Andika R., Sopyan I., Zuhrotun A., Maharani R., Rachmat R, & Abdulah R. (2021). Caspase Cascade Activation During Apoptotic Cell Death of Human Lung Carcinoma Cells A549 Induced by Marine Sponge Callyspongia aerizusa. Drug Design, Development and Therapy, 15, 1357-1368.

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Subcellular Localization of NFATC1 Proteins

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To determine the subcellular localizations of wild-type and mutant NFATC1 proteins, PC-3 cells plated on coverslips were transiently transfected with Flag-tagged expression vectors. After 48 h, cells were fixed, permeabilized and stained with anti-Flag antibody (Sigma-Aldrich) and Alexa Fluor™ 488 labelled anti-mouse secondary antibody (Thermo Fisher Scientific). Samples were imaged and analysed with the Zeiss ApoTome.2 fluorescence microscope and Zen lite 2012 software. Approximately 15 images were taken from each sample.

Eerola S.K., Santio N.M., Rinne S., Kouvonen P., Corthals G.L., Scaravilli M., Scala G., Serra A., Greco D., Ruusuvuori P., Latonen L., Rainio E.M., Visakorpi T, & Koskinen P.J. (2019). Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Cell Communication and Signaling : CCS, 17, 148.

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Immunofluorescence Staining of ARPE-19 Cells

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After treatments, ARPE19 cells were washed 3× 5min with PBS, fixed with 4% Paraformaldehyde for 20 min, washed 3× 5min with PBS, incubated with PBS containing Glycin 200 mM and Triton X100 (0.3%) for 20 min, and incubated in blocking solution (0.5% BSA and 0.3% Triton X100 in PBS) for 1 h. For ZO1 detection, cells were incubated with primary antibody (mouse anti-ZO1, 1:200, BD Bioscience, San Jose, CA, USA) in blocking solution for 12 h in dark at 4 °C, washed 3× 5min with PBS, followed by incubation with anti-mouse secondary antibody (goat anti-mouse DyLight488, 1:1000, Invitrogen, Karlsruhe, Germany). For visualization of F-actin, cells were incubated in AlexafluorTM 633 Phalloidin (1:100; Invitrogen, Karlsruhe, Germany). After staining, cells were incubated with DAPI for 2 h, washed with PBS containing 0.3% Triton X100 three times for 15 min, embedded in a humidified dark chamber, and imaged using a fluorescent microscope (ApoTome2 fluorescence microscope, Carl Zeiss Microscopy, Jena, Germany).

Karimi P., Gheisari A., Gasparini S.J., Baharvand H., Shekari F., Satarian L, & Ader M. (2020). Crocetin Prevents RPE Cells from Oxidative Stress through Protection of Cellular Metabolic Function and Activation of ERK1/2. International Journal of Molecular Sciences, 21(8), 2949.

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Multimodal Immunostaining of Mouse Brain

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Mice were deeply anesthetized with a mixture ketamine/xylazine and transcardially perfused with cold PBS, followed by cold 4%PFA. Brains were post-fixed overnight in 4% PFA at 4 °C. 30 μm serial coronal floating sections were obtained using a vibratome. For single immunofluorescence, sections were blocked with 10% donkey serum for 30 min at room temperature and then incubated with either mouse anti-NeuN (1:500, Millipore), mouse anti-GFAP (1:400, Abcam), rabbit anti-IbaI (1:500, WAKO), rabbit anti-Synaptotagmin 2 (Syt2) (1:400, Novusbio), rabbit anti-Otoferlin (Otof) (1:400, Arigo Laboratories), mouse anti-EAA1 (1:200, BD Transduction laboratories), rabbit anti-GABAR (1:400, Arigo Laboratories), overnight at 4 °C. The sections were washed with PBS before and after being incubated with Cy3-, Cy5- or Alexa-conjugated secondary antibodies (1/200, Jackson Immunoresearch) for 2 h at room temperature in blocking buffer. All sections were mounted onto gelatin-subbed slides and cover-slipped using Mowiol with DAPI. Images were obtained using a Zeiss Apotome2 fluorescence microscope and analyzed with ImageJ software.

Ramos-Brossier M., Romeo-Guitart D., Lanté F., Boitez V., Mailliet F., Saha S., Rivagorda M., Siopi E., Nemazanyy I., Leroy C., Moriceau S., Beck-Cormier S., Codogno P., Buisson A., Beck L., Friedlander G, & Oury F. (2024). Slc20a1 and Slc20a2 regulate neuronal plasticity and cognition independently of their phosphate transport ability. Cell Death & Disease, 15(1), 20.

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Fluorescence Microscopy Image Analysis

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Images were obtained with an Apotome.2 fluorescence microscope (Carl Zeiss Microscopy GmbH, Jena, Germany). Mean fluorescence intensity (MFI) in the striatum was measured using Fiji-ImageJ, a free-software for image analysis (ImageJ v1.52p, National Institutes of Health (NIH), Bethesda, MD, USA). MFI values were normalized to background signal.

Schröder S., Lai T.H., Toussaint M., Kranz M., Chovsepian A., Shang Q., Dukić-Stefanović S., Deuther-Conrad W., Teodoro R., Wenzel B., Moldovan R.P., Pan-Montojo F, & Brust P. (2020). PET Imaging of the Adenosine A2A Receptor in the Rotenone-Based Mouse Model of Parkinson’s Disease with [18F]FESCH Synthesized by a Simplified Two-Step One-Pot Radiolabeling Strategy. Molecules, 25(7), 1633.

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Tau Phosphorylation and Aggregation in AD

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Misfolded Tau becomes hyperphosphorylated in case of AD due to over-activation of various protein kinases. Phosphorylated Tau tends to aggregate inside the cells and subsequently secreted outside which lead to improper functioning. To study the over-activation of one of the cellular kinases-CDK5 and intracellular Tau phosphorylation, we treated the neuro2A cells with okadaic acid (25 nM) and melatonin (50 µM) separately and together for 24 hours. The cells were washed with PBS thrice and fixed with 4% paraformaldehyde for 15 minutes and permeabilized with 0.2% TritonX-100. The cells were stained with AT8 (1:100), K9JA (1:500), CDK5 (1:50) and mouse anti-tubulin antibody (1:100) for overnight in 2% horse serum-PBS. Then, Alexa flour conjugated secondary antibody was allowed to bind p-Tau, CDK5 specific primary antibody (anti-mouse Alexa flour 555, 1:500) and K9JA (antirabbit Alexa flour 488, 1:1000) for 1 hour along with nuclear staining DAPI (300 nM) for 5 minutes.
The images and 3D localization (orthogonal view) were observed in Zeiss Axio observer with Apotome2 fluorescence microscope at 63X oil immersion and analyzed by ZEN2 software.

Das R., Balmik A.A, & Chinnathambi S. (2020). Effect of Melatonin on Tau aggregation and Tau-mediated cell surface morphology. International journal of biological macromolecules, 152.

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Copper-induced Fluorescence Microscopy

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Gas1-GFP transformed GSHY583 yeast cells grown overnight in Sc-Leu medium were diluted to an absorbance of 0.2 at 600 nm and allowed to reach the exponential phase of absorbance of ∼1 at 600 nm. At this phase, the cells were treated with Cu at 1 mM or UT and grown for 90 min. Postincubation, the cells were harvested and washed twice with 1× PBS. Images were acquired using ZEISS-Apotome.2 fluorescence microscope (ZEISS). The λ excitation/λ emission used for GFP is 450 to 490 nm/500 to 550 nm and for dsRed is 538 to 562 nm/570 to 640 nm. Processing of the image was done using ZEN 2012 software (ZEISS).

Saha N, & Tomar R.S. (2022). Copper inhibits protein maturation in the secretory pathway by targeting the Sec61 translocon in Saccharomyces cerevisiae. The Journal of Biological Chemistry, 298(8), 102170.

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Immunofluorescence Analysis of Telomerase in MSCs and iMSCs

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Both MSCs and iMSCs at their third passage were seeded in 24-well culture plates (1×10⁴ cells/well) on coverslips and cultured in GM. After 24 h, both cells were fixed for 20 min, permeabilized for 5 min, and blocked for 1 h at room temperature using 10% buffered neutral formalin, 0.5% Triton X-100/PBS, and 1% bovine serum albumin. Both cells were incubated with primary monoclonal antibody IgM anti-TERT (1:200; Thermo Fisher Scientific, MA5-16034, Waltham, MA, USA) and Alexa-Fluor conjugated secondary antibody (1:2000; A-11094, Invitrogen) for 1 h and 30 min. Nuclei were stained with 4′, 6-diamidino-2-phenylindole dihydrochloride (DAPI, Thermo Fisher Scientific). The coverslips were assembled on glass slides and images of the cells were acquired with a Zeiss Apotome 2 fluorescence microscope (Carl Zeiss Inc., Oberkochen, Germany).

Freitas G.P., Lopes H.B., Souza A.T., Gomes M.P., Quiles G.K., Gordon J., Tye C., Stein J.L., Stein G.S., Lian J.B., Beloti M.M, & Rosa A.L. (2021). Mesenchymal stem cells overexpressing BMP-9 by CRISPR-Cas9 present high in vitro osteogenic potential and enhance in vivo bone formation. Gene therapy, 28(12), 748-759.

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Osteogenic Differentiation of iMSCs

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The iMSCs-VPR and iMSCs-VPR^BMP-9+ at passage 10 were seeded in 6-well culture plates (1×10⁵ cells/well) and cultured in GM. RNA extraction was performed on days 3, 7, and 14 and RT-PCR was performed as described above (item 2.3.1) to evaluate the relative gene expression of Runx2, Sp7, Alp, and Oc (Table 1). In situ ALP activity was evaluated on days 3, 7, 10, and 14 and extracellular matrix mineralization was evaluated on day 21. In brief, both iMSCs-VPR and iMSCs-VPR^BMP-9+ at passage 10 were seeded in 24-well culture plates (1×10⁵ cells/well), cultured in GM for ALP activity assay, as described above (item 2.3.5) or cultured in OM for extracellular matrix mineralization assay. For this, samples (n = 4) were fixed with 10% buffered neutral formalin for 24 h at 4 °C and stained with Alizarin red staining (Sigma-Aldrich). Afterward, the wells were photographed using a Zeiss Apotome 2 fluorescence microscope (Carl Zeiss Inc.). ImageJ software version 1.5i (National Institutes of Health, Bethesda, MD, USA) was used to quantify the ALP activity and extracellular matrix mineralization by counting the pixels of each group.

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