Lumplanfl n

Manufactured by Olympus

Sourced in Japan

The LUMPlanFL N is a fluorescence microscope objective lens designed for Olympus' line of biological microscopes. It features a high numerical aperture and long working distance, allowing for high-resolution imaging of samples while maintaining adequate space for sample manipulation.

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Lab products found in correlation

Bx51wi, by Olympus (4 mentions) Orca flash4.0 v2, by Hamamatsu Photonics (2 mentions) Lumen 200 metal arc lamp, by Prior Scientific (2 mentions) Fura 2 am, by Thermo Fisher Scientific (2 mentions) Cellmask orange, by Thermo Fisher Scientific (1 mentions) Ba575if, by Olympus (1 mentions) P 721 pifoc, by Physik Instrumente (1 mentions) Alexa fluor 594, by Thermo Fisher Scientific (1 mentions) Pc 10 pipette puller, by Narishige (1 mentions) Multiclamp 700a amplifier, by Molecular Devices (1 mentions) Incubation chamber, by Tokai Hit (1 mentions) Leibovitz s l 15 medium, by Thermo Fisher Scientific (1 mentions) Mai tai deepsee hp ti sapphire laser, by Spectra-Physics (1 mentions) Imaris software, by Oxford Instruments (1 mentions) Metamorph, by Universal Imaging (1 mentions) Dcu224m, by Thorlabs (1 mentions) Vt1200, by Leica (1 mentions) Umplanfl, by Olympus (1 mentions) Bx50wi, by Olympus (1 mentions) Lex2 b, by BrainVision (1 mentions)

Close spelling variants of this product

LUMPlanFl (7 citations) LUMPlanFL lens 40x/0.80 N.A (2 citations) LUMPlanFl N 60x / 1.00 w (2 citations)

15 protocols using lumplanfl n

Fluorescence Imaging of pH-Sensitive FITC

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Detailed experimental conditions are provided in supplementary information (SI-1).
Briefly (Fig. 1), fluorescence imaging was carried out on an inverted epifluorescence microscope (Olympus IC71) equipped with a ×40 0.6-NA air objective (Olympus LUMPlanFL N). The sample was illuminated with a white light source (Hg lamp) coupled through Olympus U-MSWB2 cube (with excitation filter within 450-480 nm and emission at 500 nm) to excite and reveal fluorescence emitted from the deprotonated FITC probe (ca. 0.2 mM), occurring for pH higher than ca. 6 (Fig. S1). 40 (link) A digital USB color camera (UI-3080CP Rev. 2, IDS with CMOS 2456×2054-pixel detector) collected the fluorescence emitted from the solution. FL images covering a wide field of 288 × 288 µm 2 were recorded at a speed of 2 frames per second (fps) with 500 ms accumulation time.
RM imaging was carried out an Olympus microscope, equipped with a water immersion objective (magnification ×60 1.00-NA (Olympus LUMPlanFL N)) with a focus distance of ca.

Godeffroy L., Makogon A., Gam Derouich S., Kanoufi F, & Shkirskiy V. (2023). Imaging and Quantifying the Chemical Communication between Single Particles in Metal Alloys. Analytical chemistry, 95(26).

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Micromanipulation of C. elegans for Force-Displacement Experiments

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For larger amplitude force-displacement experiments we used an in-house customized micromanipulation setup to allow uniaxial indentation of C. elegans with a microforce sensing probe (Elmi et al., 2017 (link)). Treated animals were mounted on a 2% agarose pad on top of a microscope slide (Figure 3B). To prevent motion during indentation, animals were glued (Dermabond glue, Suturonline.com) on the side to the edge of a coverslip fixed on top of the agarose pad before immersion in M9 buffer. The sample imaged using an upright widefield fluorescence microscope (BX51WI, Olympus) with 20x/1.0 water immersion objective lens (LUMPlanFL N, Olympus) fluorescence filter cube (Semrock) and a sCMOS camera (Orca-Flash4.0 v2, Hamamatsu Photonics). The body of each animal was indented using a microforce sensing probe (FT-S100, FemtoTools) fitted with a tungsten tip. The position of the probe was controlled using a motorized 4-axis stage system (ECS series, Attocube), which allowed precise positioning of the tip within (x, z) and perpendicular (y) to the focal plane of the microscope, as well as adjustment of the in-plane tilt. Animals were mounted on a separate kinematic stage system decoupled from the microscope body and the probe.

Essmann C.L., Elmi M., Rekatsinas C., Chrysochoidis N., Shaw M., Pawar V., Srinivasan M.A, & Vavourakis V. (2024). The influence of internal pressure and neuromuscular agents on C. elegans biomechanics: an empirical and multi-compartmental in silico modelling study. Frontiers in Bioengineering and Biotechnology, 12, 1335788.

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Imaging Cardiac Z-disks and T-tubules

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Experiments were performed as described in our previous study (Inoue et al., 2013 (link)). In brief, the heart was isolated from the mouse anesthetized with pentobarbital sodium (100 mg/kg, intraperitoneally), and perfused via the aorta with 5 ml of Ca²⁺-free HEPES-Tyrode’s solution containing 80 mM 2,3-butane-dione monoxime (BDM) at a speed of ∼1 drop/s. Then, the heart was mounted on the custom-made microscope stage, and AcGFP-expressing Z-disks were imaged. In some experiments, CellMask Orange (5 µg/ml in the above solution, 2 ml at a speed of ∼0.5 drop/s; Life Technologies) was used to stain the T-tubules in ventricular myocytes in the isolated heart. After the treatment with CellMask Orange, the heart was perfused with 5 mL of Ca²⁺-free HEPES-Tyrode’s solution containing 80 mM BDM at a speed of ∼1 drop/s. In this case, the heart was illuminated with a 532-nm laser light (PID-1500; Snake Creek Lasers), and the resultant fluorescence signals (emission filter, BA575IF; Olympus) were detected by the EMCCD camera. A 60× lens (60×W; numerical aperture [N/A] 1.00; LUMPlanFL N; Olympus) was used. Experiments were performed at 25°C.

Kobirumaki-Shimozawa F., Oyama K., Shimozawa T., Mizuno A., Ohki T., Terui T., Minamisawa S., Ishiwata S, & Fukuda N. (2016). Nano-imaging of the beating mouse heart in vivo: Importance of sarcomere dynamics, as opposed to sarcomere length per se, in the regulation of cardiac function. The Journal of General Physiology, 147(1), 53-62.

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Cardiac Sarcomere Length Imaging

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The objective lens (60×W; N/A 1.00; LUMPlanFL N; Olympus) was moved in the Z-direction by using a piezo-driven nano-positioning device consisting of a piezo flexure objective scanner (P-721 PIFOC; Physik Instrumente GmbH & Co. KG) and a piezo amplifier/servo controller (E-665; Physik Instrumente GmbH & Co. KG) at increments of 1 µm. The EMCCD camera shutter signal was synchronized with ECG, LVP, and the objective lens position (i.e., the Z-direction) by using a four-channel recorder (FA-404; Transonic Scisense Inc., NY). In this experiment, a LVP record was divided into 17 discrete periods (phases), and fluorescence images of a myocyte were obtained in each phase (period, 10.2 ms). The images were then analyzed by a custom-made macro software based on Excel (2010; Microsoft) and ImageJ software, and the best-focused images from phases −8 to 8 were combined to construct an image sequence. SL was measured as stated above by using the multi-peak Gaussian fitting (see Materials and methods in the supplemental text). Because tracking of individual sarcomeres during the course of the cardiac cycle was difficult as a result of a myocyte’s XY movements upon heartbeat, the average SL values (17–92 sarcomeres; i.e., 3–11 consecutive sarcomeres in 3–11 different regions within a myocyte) were obtained and used for the analyses.

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Whole-cell voltage-clamp recordings of retinal ganglion cells

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Whole-cell voltage clamp recordings were made from whole-mount retinas continuously superfused in oxygenated ACSF (32–34°C) at a rate of 2–4 ml/min. Retinas were visualized under infrared illumination (870 nm). Voltage-clamp recordings from somas of ganglion cells (holding potential of −60/−65 mV) were obtained using glass microelectrodes of 4–5 MΩ (PC-10 pipette puller; Narishige, East Meadow, NY) filled with an internal solution containing (in mM): 110 CsMeSO₄, 2.8 NaCl, 4 EGTA, 5 TEA-Cl, 4 adenosine 5′-triphosphate (magnesium salt), 0.3 guanosine 5′-triphosphate (trisodium salt), 20 HEPES and 10 phosphocreatine (disodium salt), pH 7.2 and 290 mOsm. The liquid junction potential correction for this solution was −13 mV. Signals were acquired using pCLAMP 9 recording software and a Multiclamp 700 A amplifier (Molecular Devices, Sunnyvale, CA), sampled at 20 kHz and low-pass filtered at 2 kHz.
RGC dendritic stratification was visualized by including 20 μM Alexa Fluor 594 (Invitrogen, Grand Island, NY) in the intracellular solution. The dendritic morphology of dye-injected RGCs was reconstructed by two-photon imaging with the laser tuned to 780 nm. Images (RGCs and whole retina) were acquired at z intervals of 0.5 μm using a 60× objective (Olympus 60×, 1 NA, LUMPlanFLN). Images were later reconstructed from image stacks with ImageJ.

Rosa J.M., Bos R., Sack G.S., Fortuny C., Agarwal A., Bergles D.E., Flannery J.G, & Feller M.B. (2015). Neuron-glia signaling in developing retina mediated by neurotransmitter spillover. eLife, 4, e09590.

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Two-Photon Calcium Imaging of Mice

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Five mice were imaged on all days, in 5-min sessions, during exposure, training, and retrieval. We used a resonant galvanometer two-photon microscope (Prairie Technologies). We used the genetically encoded calcium indicator GCaMP6m in all experiments (GCaMP6m was amplified from Addgene plasmid #40754 by PCR and subcloned into an AAV backbone under the control of the CaMKIIa promoter.) All experiments were performed using a Coherent Ultra II Ti-Sapphire pulsed laser tuned to 920 nm to excite GCaMP6m through a ×20 0.5 LUMPlanFL/N (Olympus) water-immersion objective interfacing with the implanted cannula through a few drops of distilled water. Fluorescence was detected through gallium arsenide phosphide (GaAsP) photomultiplier tubes (PMTs) using the PrairieView acquisition software. High speed z stacks were collected in the green channel (using a 520/44 bandpass filter, Semrock) at 512 × 512 pixels covering each x–y plane of 500 μm × 500 μm over a depth of ~100 μm (3–7 z slices ~10–20 μm apart) by coupling the 30 Hz rapid resonant scanning (x–y) to a Z-piezo to achieve ~6 Hz per volume.

Rajasethupathy P., Sankaran S., Marshel J.H., Kim C.K., Ferenczi E., Lee S.Y., Berndt A., Ramakrishnan C., Jaffe A., Lo M., Liston C, & Deisseroth K. (2015). Projections from neocortex mediate top-down control of memory retrieval. Nature, 526(7575), 653-659.

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Indentation-based Fluorescence Microscopy Imaging

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Images were acquired using an upright widefield fluorescence microscope (BX51WI, Olympus) with a 60x/1.0 water immersion objective lens (LUMPlanFL N, Olympus), dual band GFP/RFP fluorescence filter cube (Semrock) and a scientific CMOS camera (Orca-Flash4.0 v2, Hamamatsu Photonics). Focal series of image were obtained by translating the objective lens using a piezoelectric translation stage (PIFOC, PI) synchronized to the global exposure period of the camera’s rolling shutter. The cuticle of each animal was indented using either a pulled glass capillary with a tip diameter of between 2–4 µm or a microforce sensing probe (FT-S100, FemtoTools) fitted with tungsten tip with a nominal diameter of less than 2 µm. The position of the probe was controlled using a motorized 4-axis stage system (ECS series, Attocube), which allowed precise positioning of the tip within (x, z) and perpendicular (y) to the focal plane of the microscope, as well as adjustment of the in-plane tilt. Animals were mounted on a separate kinematic stage system decoupled from the microscope body and the capillary.

Elmi M., Pawar V.M., Shaw M., Wong D., Zhan H, & Srinivasan M.A. (2017). Determining the biomechanics of touch sensation in C. elegans. Scientific Reports, 7, 12329.

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Fura-2-based Ca2+ Influx Imaging

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For Ca²⁺ measurements, cells were washed with HBSS+/+ (GIBCO #14025-050) and stained with 1 µM Fura-2-AM (Thermo Fisher Scientific #F1201) at 37 °C for 30 min. Afterward, cells were washed with HBSS+/+ and left for another 30 min at RT in HBSS+/+. Cover slips were taken out from 12-well plates and placed into an imaging chamber made of plexi glass. Cells were covered with HBSS+/+, and fixed to a platform adjusted at an Olympus BX51W1 immersion microscope (Olympus; Shinjuku, Tokyo, Japan) (light source: Tilluxe PX45 Xenon-light). To induce TRPC6-mediated Ca²⁺ influx into the cell soma, hyperforin 10 µM was applied. Ca²⁺ influx was recorded and visualized in TillVision Live Acquisition and Offline Analysis software [formerly FEI Munich GmbH (Till Photonics), now Thermo Fisher Scientific] as a ratio of 340/380 nm with a 40 X objective [40x/0.80 W ∞/0/FN26.5 objective (LUMPlan FL N), Olympus]. Ca²⁺-bound Fura-2 is excitable at 340 nm and the unbound state of Fura-2 at 380 nm. The ratio was calculated by analyses of emission, which was detectable at 510 nm after excitation with each wavelength. The amplitude between baseline and first plateau (ca. after 40 s past hyperforin application) was calculated and interpreted as maximum Ca²⁺ influx inducible with hyperforin 10 µM.

Zeitler S., Schumacher F., Monti J., Anni D., Guhathakurta D., Kleuser B., Friedland K., Fejtová A., Kornhuber J, & Rhein C. (2020). Acid Sphingomyelinase Impacts Canonical Transient Receptor Potential Channels 6 (TRPC6) Activity in Primary Neuronal Systems. Cells, 9(11), 2502.

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Patch-clamp recordings of calyces

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During all experiments, slices were continuously perfused with standard aCSF at RT (~25°C) and visualized by an upright microscope (BX51WI, Olympus) through a 60x water-immersion objective (LUMPlanFL N, Olympus) and either CCD (QI-Click, QImaging) or EMCCD camera (Luca^EM S, Andor^™ Technology, Belfast, UK). Patch-clamp recordings were performed by using an EPC 10/2 patch-clamp amplifier, controlled by Patchmaster Software (HEKA, RRID:SCR 000034). Data were acquired at a sampling rate of 50 kHz and low-pass filtered at 6 kHz. To allow identification of calyces transduced with HdAd expressing Ca_V2.1 α₁ OE or Ca_V2.2 α₁ OE, we co-expressed mEGFP as a marker. To visualize mEGFP, slices were illuminated at 470 nm wavelength using a Lumen 200 metal arc lamp (Prior Scientific) or a Polychrome V xenon bulb monochromator (ThermoFisher).

Lübbert M., Goral R.O., Keine C., Thomas C., Guerrero-Given D., Putzke T., Satterfield R., Kamasawa N, & Young SM J.r. (2018). CaV2.1 α1 Subunit Expression Regulates Presynaptic CaV2.1 Abundance and Synaptic Strength at a Central Synapse. Neuron, 101(2), 260-273.e6.

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Rac1-FRET Biosensor Imaging in Mice

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OCs from P2 Rac1-fluorescence resonance energy transfer (FRET) biosensor TG mice [30 (link)] were dissected in Leibovitz’s L-15 medium (Invitrogen), attached to 3.5-mm Cell-Tak coated dishes (150 µg/µL; BD Biosciences) and maintained in Dulbecco’s modified Eagle medium/F-12 supplemented with 10% fetal bovine serum. FRET imaging under a two-photon excitation microscope was performed as previously described [28 (link)]. Samples were maintained in an incubation chamber (Tokai Hit, Nagoya, Japan) and imaged using a BX61WI/FV1000 upright microscope equipped with a × 60 water-immersion objective (LUMPlanFLN; Olympus, Tokyo, Japan) connected to a Mai Tai DeepSee HP Ti:sapphire laser (Spectra Physics, Mountain View, CA, USA). FRET/CFP images were acquired and analyzed using MetaMorph (Universal Imaging, West Chester, PA, USA) and Imaris software (Bitplane AG, Zürich, Switzerland) and represented using the intensity-modulated display mode, in which eight colors from red to blue are used to represent the FRET/CFP ratio.

Nakamura T., Sakaguchi H., Mohri H., Ninoyu Y., Goto A., Yamaguchi T., Hishikawa Y., Matsuda M., Saito N, & Ueyama T. (2023). Dispensable role of Rac1 and Rac3 after cochlear hair cell specification. Journal of Molecular Medicine (Berlin, Germany), 101(7), 843-854.

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