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Metamorph

Manufactured by Olympus
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Sourced in Japan

MetaMorph is a versatile imaging and analysis software platform that enables users to acquire, visualize, and analyze a wide range of microscopy data. It provides a comprehensive set of tools for image processing, measurement, and automation, supporting multiple imaging modalities and file formats.

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Lab products found in correlation

Ax70 microscope, by Olympus (2 mentions) Metamorph, by Molecular Devices (2 mentions) Pen strep, by Thermo Fisher Scientific (1 mentions) Roswell park memorial institute (rpmi), by Corning (1 mentions) Fetal bovine serum (fbs), by Merck Group (1 mentions) Tamoxifen, by Merck Group (1 mentions) Bx61 microscope, by Olympus (1 mentions) Metamorph, by Adobe (1 mentions) Lsm 700 780, by Zeiss (1 mentions) Ccd camera, by Hamamatsu Photonics (1 mentions) Fluorescence microscope, by Olympus (1 mentions) Intercept blocking buffer, by LI COR (1 mentions) Ab11826, by Abcam (1 mentions) Alexa fluor 488 anti mouse secondary antibody, by Thermo Fisher Scientific (1 mentions) Prolong gold antifade mountant with dapi, by Thermo Fisher Scientific (1 mentions) Ix81 inverted fluorescence microscope, by Olympus (1 mentions) Celltirf 4line excitation system, by Olympus (1 mentions) Orca flash 4.0 cmos camera, by Hamamatsu Photonics (1 mentions) Ix83 inverted microscope, by Olympus (1 mentions) Inverted microscope, by Olympus (1 mentions)

16 protocols using metamorph

1

Tamoxifen-induced E47 activity assay

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T6PNE cells were maintained in RPMI (5.5 mM glucose, Cellgro) supplemented with 10% fetal bovine serum (FBS, Sigma-Aldrich) and 1% penicillin/streptomycin (pen-strep, Gibco, Waltham, MA, USA) and grown in 5% CO2 at 37 °C. To induce E47 activity, 0.5 μM tamoxifen (Sigma-Aldrich) was added to the culture media. PBS or 10 μM 2fL1 (Santa Cruz) was added once per day for 4 days (n=4). Media was changed after 2 days with the addition of fresh tamoxifen. Photomicrographs of wells were captured by MetaMorph for Olympus (Olympus America, Center Valley, PA, USA) and analyzed with ImageJ (NIH) for intensity and localization.
Piran R., Lee S.H., Kuss P., Hao E., Newlin R., Millán J.L, & Levine F. (2016). PAR2 regulates regeneration, transdifferentiation, and death. Cell Death & Disease, 7(11), e2452-.
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2

In Situ Expression of DPP4 and PLAU in Human Skin

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FFPE-sections of human skin and scar tissue were prepared according to RNAScope (ACDBio, Bio-Techne, Bristol, UK) pre-treatment protocol, hybridized with probes targeting human DPP4 (RNAScope® Probe-Hs-DPP4) and PLAU (RNAScope® Probe-Hs-PLAU), and visualized with RNAScope 2.5 HD Assay—RED as suggested by the manufacturer. Images were acquired by AX70 microscope (Olympus, Tokyo, Japan) using the imaging software MetaMorph (Olympus).
Vorstandlechner V., Laggner M., Copic D., Klas K., Direder M., Chen Y., Golabi B., Haslik W., Radtke C., Tschachler E., Hötzenecker K., Ankersmit H.J, & Mildner M. (2021). The serine proteases dipeptidyl-peptidase 4 and urokinase are key molecules in human and mouse scar formation. Nature Communications, 12, 6242.
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3

Automated Imaging and Analysis of Rabies-Mediated Neural Connections

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Brain section images were acquired by using automated slide scanning and analysis software (MetaMorph) in a high-capacity computer coupled with a fluorescent BX61 Olympus microscope and a high-sensitive Hamamatsu CCD camera. Under a 10× objective, we were able to obtain images of sufficient resolution for all subsequent computer-based analyses. Image stitching, overlaying, cell counting, and further imaging analysis were completed by using MetaMorph imaging and analysis tools. In addition, we imaged labeled cells in selected sections with a confocal microscope (LSM 700/780, Carl Zeiss Microscopy) coupled with z-stack and tile scanning features under a 20× objective lens. Image stitching, overlaying, maximum projections, and export were performed by using the ZEN software analysis tools.
Quantitative examinations across the series of sections were conducted for complete and unbiased analyses of rabies-mediated, direct synaptic connections to targeted Cre-defined cell types by using either MetaMorph or Adobe Photoshop software (CS4 extended version, Adobe Systems). For mapping rabies-labeled presynaptic neurons (expressing mCherry only), digital images of brain sections were examined to identify and mark the locations of mCherry-expressing cell bodies. These labeled cells were assigned to specific anatomic structures for regional input quantification.
Sun Y., Nitz D.A., Holmes T.C, & Xu X. (2018). Opposing and Complementary Topographic Connectivity Gradients Revealed by Quantitative Analysis of Canonical and Noncanonical Hippocampal CA1 Inputs. eNeuro, 5(1), ENEURO.0322-17.2018.
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4

Monitoring ROS Production in Cells

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To monitor the ROS production, T24 cells were treated with 0.5 mg/mL of NP-AAG for 24 hr followed by 30 min loading with 2′, 7′- dichlorofluorescin-diacetate (DCF) (Sigma) as an indicator in 6-well plate. Cells were washed three times with PBS and replaced with fresh medium. A portion of the well was illuminated with NIR light, ROS production were analyzed by flow cytometry. For in vivo ROS production, tumor samples were incubated with DCF for 30 min, then after 2 minute NIR light exposure, ROS production was acquired under fluorescence microscope (Olympus) using the Metamorph program.
Long Q., Lin T.Y., Huang Y., Li X., Ma A.H., Zhang H., Carney R., Airhart S., Lam K.S., Pan C.X, & Li Y. (2018). Imaging-guided photo-therapeutic nanoporphyrin synergized HSP90 inhibitor in patient-derived xenograft bladder cancer model. Nanomedicine : nanotechnology, biology, and medicine, 14(3), 789-799.
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5

Cyclic Immunohistochemistry Imaging

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Frozen tissue sections were cut to 5 μm and then processed for immunohistochemistry or FAST cycling. Frozen tissue sections were thawed, rehydrated, and blocked with Intercept Blocking buffer (LI-COR) for 30 min before antibody staining. For FAST imaging, tissue sections were incubated with antibodies for 1–2 h and washed with PBS for 10 min three times. After imaging, the fluorescence signal was quenched by incubating tissue sections in 10 Mμ Tz-BHQ3 for 30 min. The quenched signal was imaged. Then tissue sections were incubated with 50 μM of free TCO solution to react with the residual quencher. Antibodies for the subsequent cycle were then added, and the cycles were repeated until all proteins of interest were imaged. Olympus BX-63 system and Metamorph were used for image acquisition. CellProfiler version 4.1.8 was used for the analysis of tissue section images.
Kumagai Y., Konishi K., Gomi T., Yagishita H., Yajima A, & Yoshikawa M. (2000). Enzymatic Properties of Dipeptidyl Aminopeptidase IV Produced by the Periodontal Pathogen Porphyromonas gingivalis and Its Participation in Virulence. Infection and Immunity, 68(2), 716-724.
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6

Histological Analysis of Bone Tissue

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After μ-CT scanning, the specimens from the respective groups were fixed and decalcified. The specimens were then bisected and embedded in paraffin, sectioned at a thickness of 5 μm and placed on the glass slide. The slides were stained with hematoxylin and eosin (H&E) and Goldner’s Trichrome staining, then examined under a light microscope (IX71; Olympus, Tokyo, Japan) using Meta-Morph to visualize the formation of newly formed bone tissue.
Fang C.H., Lin Y.W., Lin F.H., Sun J.S., Chao Y.H., Lin H.Y, & Chang Z.C. (2019). Biomimetic Synthesis of Nanocrystalline Hydroxyapatite Composites: Therapeutic Potential and Effects on Bone Regeneration. International Journal of Molecular Sciences, 20(23), 6002.
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7

Cell Migration on Patterned Surfaces

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Bright-field and interference reflection microscopy (IRM) images of cells and fluorescent images of patterns (in blue) were obtained using 60× objective in time-lapsed manner for 30 min with 20 s intervals immediately after seeding. Movie S1 (ESI†) was obtained in the same manner. Mean velocity (μm min–1) of cells walking or stopping on patterns was analyzed from IRM images using Track Object App in Metamorph software (Olympus).
Lee J.H., Dustin M.L, & Kam L.C. (2015). A microfluidic platform reveals differential response of regulatory T cells to micropatterned costimulation arrays †Electronic supplementary information (ESI) available. See DOI: 10.1039/c5ib00215j. Integrative Biology, 7(11), 1442-1453.
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8

Immunofluorescence Analysis of SF3B1 and SC35

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One million cells of indicated genotypes were seeded onto Corning BioCoat Fibronectin 22 mm cover-slips (Fisher Scientific 08-774-386) in six-well plates. After 2 days, cells were fixed with 4% paraformaldehyde/phosphate-buffered saline (PBS) for 20 min at room temperature (RT). After 3 × PBS wash, cells were permeabilized with 0.1% Triton X-100/PBS for 20 min at RT. After 3 × PBS wash, cells were blocked with 5% FBS/PBS for 1 h at RT and incubated with α-SF3B1 mouse monoclonal antibody (MBL, D221-3) or α-SC35 mouse monoclonal antibody (Abcam, ab11826) at 1:50 dilution in 5% FBS/PBS in cold room overnight. On the second day, coverslips were washed with PBS three times and incubated with Alexa Fluor 488 anti-mouse secondary antibody (Thermo Fisher Cat #: A-11029) at 1:500 dilution in 5% FBS/PBS at RT in dark for 1 h. Coverslips were then washed with PBS three times and mounted using ProLong Gold Antifade Mountant with DAPI (Thermo Fisher, P36935). Slides were imaged with a × 40 objective on an Olympus IX-81 inverted fluorescence microscope and imaged, captured and processed with Metamorph for Olympus.
Teng T., Tsai J.H., Puyang X., Seiler M., Peng S., Prajapati S., Aird D., Buonamici S., Caleb B., Chan B., Corson L., Feala J., Fekkes P., Gerard B., Karr C., Korpal M., Liu X., T. Lowe J., Mizui Y., Palacino J., Park E., Smith P.G., Subramanian V., Wu Z.J., Zou J., Yu L., Chicas A., Warmuth M., Larsen N, & Zhu P. (2017). Splicing modulators act at the branch point adenosine binding pocket defined by the PHF5A–SF3b complex. Nature Communications, 8, 15522.
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9

Single-Molecule SNARE Complex Visualization

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Preparation of flow cells for single-molecule experiments was performed as described previously69 (link). Purified trans-SNARE NDs (syntaxin1a labeled with cy3, 0.5 µM) were incubated with C2AB (labeled with cy5, 1 µM) and complexin I (labeled with Alexa Fluor 488, 1 µM) at RT for 10 min, and diluted to 10 pM before injection into flow cells. Unbound protein was washed out and samples were imaged in a buffer consisting of (in mM): 1 Trolox, 0.5 CaCl2, 100 KCl, and 25 HEPES pH 7.4, and an oxygen scavenging system (1% glucose, 1 mg/ml glucose oxidase, and 0.02 mg/ml catalase). Single-molecule imaging was performed using an Olympus IX83 inverted microscope equipped with a cellTIRF-4Line excitation system, a 60 × /1.49 Apo N objective (Olympus), and an Orca Flash4.0 CMOS camera (Hamamatsu Photonics, Skokie, IL). The following excitation filter sets: 488 nm, 590 nm, and 640 nm, were used to collect signals from Alexa Fluor 488, cy3, and cy5, respectively. Images were acquired using Metamorph and Olympus 7.8.6.0 (Molecular devices; Sunnyvale, CA), and adjusted for presentation in ImageJ.
Courtney N.A., Bao H., Briguglio J.S, & Chapman E.R. (2019). Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin. Nature Communications, 10, 4076.
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10

Immunofluorescence Staining of Formalin-Fixed Paraffin-Embedded Samples

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Five μm thin-sections of formalin-fixed, paraffin-embedded SE were staining by immunofluorescence labeling as described previously (Mildner et al., 2010a (link)). Briefly, fixed sections were deparaffinized, rehydrated and washed in PBS (2×5 min), incubated with 10% goat serum at RT for 30 minutes and then with primary antibodies overnight at 4°C (the same antibodies as described for Western Blot were used). Sections were then washed in PBS (2×5 min) and incubated with goat anti–rabbit Alexa Fluor 488 (Alexa, Eugene, OR, USA). Slides were washed in PBS (2×5 min) and counterstained with Hoechst to visualize nuclei. Images were recorded using the AX70 microscope with the imaging software MetaMorph from Olympus (Hamburg, GER).
Gschwandtner M., Zhong S., Tschachler A., Mlitz V., Karner S., Elbe-Bürger A, & Mildner M. (2014). Fetal human keratinocytes produce large amounts of antimicrobial peptides: Involvement of histone-methylation processes. The Journal of investigative dermatology, 134(8), 2192-2201.
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