Ti e microscope

Manufactured by Nikon

Sourced in Japan, United States, United Kingdom, Germany

The Ti-E microscope is a high-performance inverted microscope system designed for advanced imaging and research applications. It features a robust and stable frame, precision optics, and a modular design that allows for customization to meet specific experimental requirements.

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Lab products found in correlation

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Spelling variants of this product

Ti microscope (160 citations) Ti-E fluorescence microscope (54 citations) Eclipse Ti-E epifluorescence microscope (8 citations) Eclipse Ti-E epifluorescence inverted microscope (7 citations) Ti-E spinning disk microscope (5 citations) Eclipse Ti-E N-STORM microscope (3 citations) Inverted Ti-E A1 confocal microscope (2 citations) Ti-E wide-field fluorescence microscope (2 citations) Ti-E inverted light microscope (2 citations) Ti-E SpectraX widefield microscope (2 citations)

435 protocols using ti e microscope

High-Content Microscopy Analysis of Host-Pathogen Interactions

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Specimens were prepared as described above. Images were acquired using a Ti-E Nikon microscope equipped with LED-illumination and an Orca-Flash4 camera using a 60x magnification. All intracellular parasites/bacteria of 100 fields of view were automatically counted based on whether they showed recruitment of the protein of interest using HRMAn high-content image analysis (Fisch et al., 2019b (link)). Further, the analysis pipeline was used to measure the fluorescence intensity of GBP1 on STm vacuoles using the radial intensity measurement implemented in HRMAn. The coat thickness of decorated vacuoles was determined by calculating the full width half maximum (FWHM) of the radial intensity measurement following a Gaussian curve fit of the raw fluorescence intensity data distribution measured starting from the centroid of the respective pathogen vacuole.
For quantification of ASC speck formation, 100 Tg-infected cells were manually counted per condition using a Ti-E Nikon microscope equipped with LED-illumination using 60x magnification based on whether they contain an ASC speck and whether STm was decorated with GBP1/CASP4. The experiment was repeated independently three times.

Fisch D., Clough B., Domart M.C., Encheva V., Bando H., Snijders A.P., Collinson L.M., Yamamoto M., Shenoy A.R, & Frickel E.M. (2020). Human GBP1 Differentially Targets Salmonella and Toxoplasma to License Recognition of Microbial Ligands and Caspase-Mediated Death. Cell Reports, 32(6), 108008.

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Intracellular Pathogen Vacuole Dynamics

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Cells seeded as above were infected with Tg MOI = 1 and fixed 6 h p.i. or STm‐GFP MOI = 30 and fixed 2 h p.i. Nuclei were stained with Hoechst 33342 and coverslips mounted as described above. Images were acquired using a Ti‐E Nikon microscope equipped with LED‐illumination and an Orca‐Flash4 camera using a 60× magnification. All intracellular vacuoles of 100 fields of view were automatically counted based on whether they show recruitment of GBP1, caspase‐4, both, or no recruitment using HRMAn high‐content image analysis (Fisch et al, 2019). Further, the analysis pipeline was used to measure the fluorescence intensity of GBP1 on STm vacuoles using the radial intensity measurement implemented in HRMAn. The Pearson's correlation coefficient for colocalization analysis was also computed on cropped STm vacuoles, that have been classified as decorated with both proteins by HRMAn, using Fiji. The experiment was repeated independently three times.
For quantification of ASC speck formation and caspase‐8 recruitment, 100 Tg‐infected cells were manually counted per condition using a Ti‐E Nikon microscope equipped with LED‐illumination using a 100× magnification based on whether they contain an ASC speck and whether caspase‐8 was recruited to this speck. The experiment was repeated independently three times.

Fisch D., Bando H., Clough B., Hornung V., Yamamoto M., Shenoy A.R, & Frickel E. (2019). Human GBP1 is a microbe‐specific gatekeeper of macrophage apoptosis and pyroptosis. The EMBO Journal, 38(13), e100926.

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Quantitative Analysis of Murine Wound Healing

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Murine wounds were photographed with an in-frame ruler at indicated times. Wound area was calculated using ImageJ software (NIH, Bethesda, MD) and plotted as a function of time (Volk et al., 2011 (link)). Gross wound closure data represent averages based on independent evaluations by two investigators (G.R. and S.W.V.). At the time of wound harvest, wounds and surrounding tissue were fixed with splints intact in Prefer fixative (Anatech Ltd., Battle Creek, MI) and processed as described previously (Volk et al., 2007 ). Briefly, splints were removed and the bisected wounds embedded in paraffin. Sequential 5 μm sections were stained with hematoxylin and eosin and imaged on a Nikon Ti-E microscope (Melville, NY) and total wound length was measured for each section using Nikon Elements software. The section with the greatest length, representing the center, was further analyzed. Healing parameters were measured as described previously (Volk et al., 2011 (link)).
Normal human skin and wounds were obtained via punch biopsy from volunteers as described (Sebastian et al., 2015 (link)). Samples were processed and stained for ST2L (MD Bioproducts, biotin-conjugated mouse IgG1) as described previously (Kim et al., 2014 ). Images were obtained using a Nikon Ti-E microscope (Melville, NY).

Rak G.D., Osborne L.C., Siracusa M.C., Kim B.S., Wang K., Bayat A., Artis D, & Volk S.W. (2016). IL-33-dependent group 2 innate lymphoid cells promote cutaneous wound healing. The Journal of investigative dermatology, 136(2), 487-496.

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Quantitative Analysis of Murine Wound Healing

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Monitoring DNA Damage Response Dynamics

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Two days prior imaging cells were transiently transfected with plasmid encoding eGFP-53BP1 which was a gift from Daniel Durocher (Addgene plasmid #60813; http://n2t.net/addgene:60813; RRID:Addgene_60813, Watertown, MA, USA). Live cell imaging was performed at 37 °C and 5% CO₂ in a humidified stage top incubator (Tokai Hit, Shizuoka, Japan). Nikon Ti-E microscope with 60× Plan Apo oil objective (NA 1.4) and Nikon C2plus camera was used to collect multipoint time-lapse live cell images for 1 h with a temporal resolution of 5 min/frame. Imaging conditions were adjusted to minimize phototoxicity.
FRAP experiments were performed on the Nikon Ti-E microscope with 60× Plan Apo oil objective (NA 1.4) and Nikon C2plus camera at 37 °C in a humidified incubator. For bleaching and imaging of eGFP-53PB1, a 488-nm laser was used. After bleaching cells were imaged every 5 s for 5 min. Resulted images were analyzed using ImageJ software (version 1.44).

Luzhin A.V., Avanesyan B., Velichko A.K., Shender V.O., Ovsyannikova N., Arapidi G.P., Shnaider P.V., Petrova N.V., Kireev I.I., Razin S.V, & Kantidze O.L. (2020). Chromatin Trapping of Factors Involved in DNA Replication and Repair Underlies Heat-Induced Radio- and Chemosensitization. Cells, 9(6), 1423.

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Optogenetic Cre-loxP Recombination in Cells

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HEK 293T cells were plated at 2 × 10⁵ cells/dish in 3.5 cm glass bottom dish (MatTek) coated with poly-ornithine. The following day, the cells were transfected with cDNAs encoding PA-Cre along with Floxed-mCherry reporter using X-treameGENE9 reagent. The standard transfection ratio is PA-Cre and Floxed-mCherry at 1:9 ratio. The cells were then exposed to blue light (total 12 h, 20 s light/60 s dark cycle, homemade device) 36 h after transfection at 37 °C in a CO₂ incubator. The cells were imaged with TxRed filters and Nikon NIS using the custom Nikon microscope Ti-E immediately after illumination was completed. The Cre-loxP recombination efficiency were analyzed by ImageJ software (NIH) upon the red fluorescent signals. MEF cells, NPCs, and cortical neurons were also imaged with TxRed filters and Nikon NIS using the custom Nikon microscope Ti-E.

Morikawa K., Furuhashi K., de Sena-Tomas C., Garcia-Garcia A.L., Bekdash R., Klein A.D., Gallerani N., Yamamoto H.E., Park S.H., Collins G.S., Kawano F., Sato M., Lin C.S., Targoff K.L., Au E., Salling M.C, & Yazawa M. (2020). Photoactivatable Cre recombinase 3.0 for in vivo mouse applications. Nature Communications, 11, 2141.

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Time-lapse Imaging of Cell Dynamics

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Phase contrast time-lapse imaging was conducted using a Ti-E Nikon microscope. The objective lens was 10x, NA = 0.3. Time-lapse imaging was performed using NIS-Elements Advanced Research (Nikon) software. A single frame was captured every 5 min during the first 10 h, followed by a frame rate of one frame per 15 min during the rest of the experiment.

Belansky J, & Yelin D. (2022). Optimization study of plasmonic cell fusion. Scientific Reports, 12, 7159.

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Thioflavin T Labeling for Amyloid Imaging

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Following the 2x wash in MB, we washed the cells again in an MB solution containing the Thioflavin T (ThT) dye (10 μM). We resuspended the cell pellet in the same MB-ThT solution. All the reservoirs (MB-only and MB-indole solutions) contained 10 μM ThT. Once the cells were adhered to the coverslip and loaded into the perfusion chamber, we continuously perfused the MB-ThT solution into the chamber. During the experiment, we excited the cells with an LED light (SOLA SE Light Engine, Lumencor, Inc.) filtered with a 435/20 nm excitation filter (Nikon Inc.) on Ti-E Nikon microscope. The emissions were collected with a water immersion objective (60X, NA 1.2, Nikon Inc.) and passed through a 525/50 nm emission filter (AVR optics). The signal was relayed to a sensitive photomultiplier (H7421-40 SEL Hamamatsu Corp.) and sampled at 10 Hz (25 (link)). Since the wash in MB-ThT solution, the cells had ~30 min to equilibrate with the dye prior to imaging. The excitation intensity, focus, and cell coverage were maintained the same between all biological replicates.

Gupta R., Rhee K.Y., Beagle S.D., Chawla R., Perdomo N., Lockless S.W, & Lele P.P. (2022). Indole modulates cooperative protein–protein interactions in the flagellar motor. PNAS Nexus, 1(2), pgac035.

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Thioflavin T-based Live-Cell Imaging

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Following the 2x wash in MB, we washed the cells again in an MB solution containing the Thioflavin T (ThT) dye (10 μM). We resuspended the cell pellet in the same MB-ThT solution. All the reservoirs (MB-only and MB-indole solutions) contained 10 μM ThT. Once the cells were adhered to the coverslip and loaded into the perfusion chamber, we continuously perfused the MB-ThT solution into the chamber. During the experiment, we excited the cells with an LED light (SOLA SE Light Engine, Lumencor, Inc.) filtered with a 435/20 nm excitation filter (Nikon Inc.) on Ti-E Nikon microscope. The emissions were collected with a water immersion objective (60X, NA 1.2, Nikon Inc.) and passed through a 525/50 nm emission filter (AVR optics). The signal was relayed to a sensitive photomultiplier (H7421-40 SEL Hamamatsu Corp.) and sampled at 10 Hz (25 (link)). Since the wash in MB-ThT solution, the cells had ∼30 min to equilibrate with the dye prior to imaging. The excitation intensity, focus, and cell coverage were maintained the same between all biological replicates.

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Immunofluorescent Labeling of Toxoplasma Parasites

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Parasites were seeded onto HFFs grown on coverslips. 16–24 hr after seeding, the coverslips were fixed in 3% formaldehyde for 15 min at room temperature then permeabilised in 0.2% Triton X-100/PBS for 3–10 min and blocked in 3% BSA/PBS for 1 hr. Staining was performed using appropriate primary antibodies and goat Alexa Fluor 488-, Alexa Fluor 594- and Alexa Fluor 647-conjugated secondary antibodies (1:2000) alongside DAPI (5 µg/ml). Coverslips were mounted on glass slides with SlowFade gold antifade mountant (Life Technologies). Antibody concentrations used were: rat anti-HA high affinity (Roche, Basel, Switzerland) (1:1000), rabbit anti-T. gondii CAP (1:2000), mouse anti-Toxoplasma antigen B1247M (Abcam) (1:1000) and rabbit anti-T. gondii RON4 (Leriche and Dubremetz, 1991 (link)) (1:2000).
Widefield images were generated with a Ti-E Nikon microscope using a 63x or 100x objective (Tokyo, Japan). Images were processed with Nikon Elements software. Confocal images were taken using a Zeiss LSM-780 inverted confocal laser scanning microscope with a 63x objective. Images were processed with Zeiss Zen Black software (Oberkochen, Germany).

Hunt A., Russell M.R., Wagener J., Kent R., Carmeille R., Peddie C.J., Collinson L., Heaslip A., Ward G.E, & Treeck M. (2019). Differential requirements for cyclase-associated protein (CAP) in actin-dependent processes of Toxoplasma gondii. eLife, 8, e50598.

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