Image gauge software

Manufactured by Fujifilm

Sourced in Japan, United States

Image Gauge software is a measurement and analysis tool designed for digital microscopy and imaging applications. It provides users with the ability to perform accurate measurements and annotations on digital images.

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Lab products found in correlation

Las 1000, by Fujifilm (5 mentions) Las 1000 pro, by Fujifilm (4 mentions) Fla3000 phosphorimager, by Fujifilm (4 mentions) Immobilon p membrane, by Merck Group (4 mentions) β actin, by Fujifilm (3 mentions) Gapdh, by Merck Group (3 mentions) Las 4000 mini, by Fujifilm (3 mentions) Fla 5100, by Fujifilm (3 mentions) Ecl prime, by GE Healthcare (3 mentions) Immobilon western chemiluminescent hrp substrate, by Merck Group (3 mentions) Hrp conjugated secondary antibody, by Santa Cruz Biotechnology (3 mentions) Steponeplus qpcr system, by Thermo Fisher Scientific (2 mentions) Turbo dna free rnase free dnase, by Thermo Fisher Scientific (2 mentions) Improm 2, by Promega (2 mentions) Las 3000, by Fujifilm (2 mentions) β actin, by Abcam (2 mentions) Ecl prime reagent, by GE Healthcare (2 mentions) Precision plus protein all blue standard, by Bio-Rad (2 mentions) Fuji las 4000 image analyzer, by Fujifilm (2 mentions) Hybond lfp pvdf membrane, by GE Healthcare (2 mentions)

Close spelling variants of this product

Image Gauge densitometric software Multi Gauge image analysis software Image Gauge software version 4.0 Image Gauge analysis software Film Multi Gauge image analyzer software Image Multi-Gauge Software Multi Gauge Version 3.2 Image software Fuji Image Gauge software Image Gauge

101 protocols using image gauge software

Cell Viability and Proliferation Assay

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HCECs were seeded at a density of 5000 cells/well in a 96-well plate, cultured for 24 hours, and then cultured for a further 24 hours in the presence or absence of inhibitors.
The number of viable cells was evaluated based on the amount of ATP by using a CellTiter-Glo Luminescent Cell Viability Assay using a Veritas Microplate Luminometer (Promega, Fitchburg, WI, USA) according to manufacturer's protocol. Six samples were prepared for each group.
DNA synthesis was detected as incorporation of 5-bromo-2deoxyuridine (BrdU) using the Cell Proliferation Biotrak ELISA system, version 2 (GE Healthcare Life Sciences, Buckinghamshire, UK) according to the manufacturer's instructions. Briefly, HCECs were incubated with 10 lmol/L BrdU for 24 hours, further incubated with fixation solution (Amersham Biosciences, Freiburg, Germany) for 2 hours, and incubated with 100 ll of monoclonal antibody against BrdU for 30 minutes. The BrdU After washing with TBS-T buffer, the blots were incubated with horseradish peroxidase-conjugated secondary antibodies (1:5000: anti-rabbit, anti-mouse IgG; Cell Signaling Technology). The blots were developed with luminal for enhanced chemiluminescence (ECL) using the Chemi-Lumi One Ultra (Nacalai Tesque), documented by LAS4000S (Fuji Film, Tokyo, Japan), and analyzed with Image Gauge software (Fuji Film).

Nakahara M., Okumura N., Nakano S, & Koizumi N. (2018). Effect of a p38 Mitogen-Activated Protein Kinase Inhibitor on Corneal Endothelial Cell Proliferation. Investigative ophthalmology & visual science, 59(10).

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Transfection and qPCR Analysis in HEK293 Cells

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Human embryonic kidney (HEK293 and HEK293T) cells were cultured in DMEM (Invitrogen) supplemented with 10% FCS, l-glutamine (2 mM), penicillin, and streptomycin and grown in 5% CO₂ at 37°C. For reporter assays, cells were cotransfected using Fugene 6 reagent (Roche) with expression vectors encoding the splice reporter and RNA-binding proteins. RNA was harvested 24–36 h after transfection using Trizol reagent (Invitrogen), followed by removal of contaminating DNA using Turbo DNA-free (RNase-free DNase; Ambion). 1 µg of total RNA was reverse transcribed using random hexamers and ImProm-II (Promega).
For semi-quantitative PCR, DNA fragment intensities were quantified by image analyzer (FAS-III; Toyobo) and ImageGauge software (Fujifilm). Oligonucleotide primers used for semi-quantitative PCR were described previously (Iijima et al., 2011 (link)).
Quantitative PCR was performed on a StepOnePlus qPCR system (Applied Biosystems). Custom and commercial gene expression assays (see Table 1) were used with TaqMan Master Mix (Applied Biosystems) and comparative C_T method. The mRNA levels were normalized to that of Gapdh mRNA.

Iijima T., Iijima Y., Witte H, & Scheiffele P. (2014). Neuronal cell type–specific alternative splicing is regulated by the KH domain protein SLM1. The Journal of Cell Biology, 204(3), 331-342.

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Autophagy Analysis in S. aureus-Infected Macrophages

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RAW264.7 (2.5 × 10⁶ cells/well) were infected with S. aureus at a MOI of 50 in 6-well plates for 3 h and then collected and washed twice with ice-cold PBS. The total protein from the cells was extracted using a RIPA lysis buffer solution (Wuhan Boster), with the total protein concentration determined using a bicinchoninic acid protein assay kit (Thermo Fisher Scientific). Cell lysis solutions were separated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to poly-vinylidene difluoride membranes (Millipore). The membranes were blocked in 5% skim milk in tris-buffered saline Tween 20 buffer for 2 h at room temperature and then incubated overnight at 4°C with primary antibodies against LC3-I/II and p62/SQSTM1 (1:1000, Cell Signaling Technology). The membranes were then incubated with a 1:5000 dilution of horseradish peroxidase-conjugated secondary antibody for 1 h at room temperature. Densitometric analysis of the western blot was performed using Image Gauge software (Fujifilm). β-actin was used as an internal control, and the ratio of the intensity of the protein of interest to β-actin was calculated.

Dai Y., Gao C., Chen L., Chang W., Yu W., Ma X, & Li J. (2019). Heterogeneous Vancomycin-Intermediate Staphylococcus aureus Uses the VraSR Regulatory System to Modulate Autophagy for Increased Intracellular Survival in Macrophage-Like Cell Line RAW264.7. Frontiers in Microbiology, 10, 1222.

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Immunostaining and Reactivation of p38 in C2C12 Cells

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Immunostaining for MHC expression was performed as described previously [1 (link)]. Briefly, C2C12 cells were transfected with Cdo plus GFP vector or Stx4 and GFP vector, fixed with 4 % paraformaldehyde for 20 min, permeabilized with 1 % Triton X-100 in PBS for 10 min, blocked, and stained with anti-MHC, followed by an FITC-conjugated and Alexa Fluor 568-conjugated secondary antibody (Invitrogen). Images were captured and processed with a Nikon ECLIPSE TE-2000U microscope and NIS-Elements F software (Nikon). Quantitative differentiation assay was performed for at least three independent experiments.
For reactivation of p38 in Cdo-depleted cells by Stx4 overexpression experiment, C2C12 cells in 12-well plates were cotransfected with 100 ng of a GFP expression vector and 900 ng of the indicated DNA construct for 2 days and then fixed with 4 % paraformaldehyde for 20 min. Cultures were then permeabilized with 1 % Triton X-100 in PBS, blocked, and incubated with anti-p-p38 followed by incubation with an Alexa Fluor 568-conjugated secondary antibody. Nuclei were counterstained with 4',6-diamidino-2-phenylindole (DAPI). An image was obtained on a Zeiss LSM-510 Meta Confocal Microscope. Quantification of the fluorescent signal for p-p38 was performed with Image Gauge software (Fujifilm).

Yoo M., Kim B.G., Lee S.J., Jeong H.J., Park J.W., Seo D.W., Kim Y.K., Lee H.Y., Han J.W., Kang J.S, & Bae G.U. (2015). Syntaxin 4 regulates the surface localization of a promyogenic receptor Cdo thereby promoting myogenic differentiation. Skeletal Muscle, 5, 28.

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Immunoblot Analysis of Mitochondrial Proteins

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The immunoblot procedure was performed as described previously. Antibodies specific for HK2 (Cell Signaling Technology, Boston, MA, USA), ATP6 and CTYB (Abcam, Cambridge, MA, USA), COXIV-1 (Thermo Fisher Scientific Inc., Kalamazoo, MI, USA), and ß-actin (Sigma-Aldrich, St Louis, MO, USA) were used. The signals of the target genes were analyzed using the Image Gauge software (Fujifilm, Tokyo, Japan) and further normalized to those of β-actin.

Lin Y.H., Chu Y.D., Lim S.N., Chen C.W., Yeh C.T, & Lin W.R. (2021). Impact of an MT-RNR1 Gene Polymorphism on Hepatocellular Carcinoma Progression and Clinical Characteristics. International Journal of Molecular Sciences, 22(3), 1119.

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Hepatic Spheroid Protein Extraction and Analysis

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Hepatic spheroids were lysed with RIPA buffer (Thermo Fisher Scientific) containing a protease inhibitor cocktail (Merck Millipore, Frankfurter, Germany) on ice for 20 min and centrifuged at 20,000 x g for 30 min at 4 °C. Protein concentrations were determined using a Bradford protein assay kit (Bio-Rad, Hercules, CA, USA). Total protein (10 μg) was separated via Mini-PROTEAN TGX Gels (Bio-Rad) and electrotransferred to PVDF membranes (Bio-Rad) using a Trans-Blot Turbo Transfer System (Bio-Rad). The membranes were blocked in 5% skim milk (BD Biosciences) at RT for 2 h and then incubated with a specific primary antibody overnight at 4 °C. The membranes were washed with PBS containing 0.1% Tween-20 and then probed with HRP-conjugated secondary antibodies (Santa Cruz Biotechnology). The bands were detected using SuperSignal West Femto Chemiluminescent Substrate (Thermo Fisher Scientific) and LAS-3000 (Fujifilm, Minato, Tokyo, Japan). The bands were analysed using Image Gauge software (Fujifilm). The antibodies used in these experiments are listed in Additional file 2: Table S1.

Ryu J.S., Lee M., Mun S.J., Hong S.H., Lee H.J., Ahn H.S., Chung K.S., Kim G.H, & Son M.J. (2019). Targeting CYP4A attenuates hepatic steatosis in a novel multicellular organotypic liver model. Journal of Biological Engineering, 13, 69.

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HeLa Cell Lysis and Protein Analysis

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HeLa cells from 60-mm plates were harvested in Tris-SDS lysis buffer (25 mM Tris-Cl, pH 6.7, 1.5% SDS, 0.1% β-mercaptoethanol, and 1 mM phenylmethanesulfonylfluoride), passed through a 25-gauge needle ∼10 times, and clarified by centrifugation at 15,000 rpm in a microfuge for 15 min at 4°C. Protein levels were determined using the Pierce BCA Protein Assay (Thermo Scientific, Waltham, MA), and equal protein amounts of lysate were analyzed by SDS–PAGE and immunoblotting. Immunoblots were quantified using ImageGauge software (Fujifilm, Valhalla, NY). For the GPP130-FM, Man1-FM, and GT-FM blots, the transfected cells were subjected to AP washout for the indicated times before lysis. To inhibit lysosomal hydrolases, GPP130-FM– transfected cells were preincubated with leupeptin (100 μg/ml) and pepstatin (50 μg/ml) for 24 h before AP washout for 5 h in the continued presence of the inhibitors. For Bip assays, cells were treated for 6 h with 3 μM tunicamycin, 500 μM Mn, or a washout of AP from GPP130-FM–transfected cells.

Tewari R., Bachert C, & Linstedt A.D. (2015). Induced oligomerization targets Golgi proteins for degradation in lysosomes. Molecular Biology of the Cell, 26(24), 4427-4437.

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Western Blot Analysis of Cellular Signaling

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Total cell lysates, nuclear extracts, and conditioned medium (CM) were isolated and fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) on 8-12% gels. Separated proteins were transferred to a PVDF (polyvinylidene difluoride) membrane and blocked by incubating in 5% (w/v) nonfat milk. PVDF membranes were incubated with appropriate primary and horseradish peroxidase (HRP)-conjugated secondary antibodies, and immunoreactive proteins were subsequently detected by chemiluminescence using an ECL detection kit (Amersham Inc., RPN2232) and visualized with X-ray film. The intensities of immunoreactive bands were quantified using Image Gauge software (Fuji Film, Tokyo, Japan). The indicated antibodies against the following proteins were used: NUPR1 (made in-house), lamin A/C (Santa Cruz, sc-20681), GAPDH (Millipore, MAB374), β-actin (Chemicon, MAB1501R), PDGFA (Abcam, ab135881), fascin (Santa Cruz, sc-21743), phospho-PDGFRα (Santa Cruz, sc-12911), PDGFRα (R&D Systems, AF-307-NA), phospho-MEK1/2 (Cell Signaling, #9154), MEK1/2 (Cell Signaling, #4694), phospho-ERK1/2 (Cell Signaling, #4370), ERK1/2 (Cell Signaling, #9211), and TR (Santa Cruz, sc-739).

Chen C.Y., Wu S.M., Lin Y.H., Chi H.C., Lin S.L., Yeh C.T., Chuang W.Y, & Lin K.H. (2019). Induction of nuclear protein-1 by thyroid hormone enhances platelet-derived growth factor A mediated angiogenesis in liver cancer. Theranostics, 9(8), 2361-2379.

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Protein Expression Analysis in Neuron Cultures

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DNs were lysed with sample buffer (62.5 mM Tris–HCl buffer [pH 6.8] containing 2% sodium dodecyl sulfate [SDS], 5% β‐mercaptoethanol, and 10% glycerol) and incubated at 95°C for 5 min. The proteins in the cell lysates were electrophoresed using SDS‐polyacrylamide gel electrophoresis, and immunoblotting was performed using rabbit anti‐nuclear receptor‐related 1 (NURR1; #10975‐2‐AP; Proteintech), mouse anti‐TH (#66334‐1‐Ig; Proteintech), rabbit anti‐forkhead box protein A2 (FOXA2; #22474‐1‐AP; Proteintech), rabbit anti‐peroxisome proliferator‐activated receptor gamma coactivator 1 alpha (PGC‐1α; #NBP1‐04676; Novus Biologicals), mouse anti‐postsynaptic density protein 95 (PSD‐95; #MAB1598; Millipore), rabbit anti‐paired‐like homeodomain 3 (PITX3; #CSB‐PA010844LA01HU; CUSABIO), mouse anti‐microtubule‐associated protein 2 (MAP2; #M9942; Sigma–Aldrich), rabbit anti‐delta like non‐canonical Notch ligand 1 (DLK1; #10636‐1‐AP; Proteintech), rabbit anti‐DAT1; #22524‐1‐AP; Proteintech) and mouse anti‐α‐tubulin (#sc‐32,293; Santa Cruz Biotechnology) antibodies. The immunoreactive bands were detected using ECL Prime (Cytiva) and analyzed using LAS‐1000 pro (Fuji Film) and Image Gauge software (Fuji Film). α‐tubulin was used as an internal control. To normalize the protein expression, the chemiluminescent signal was divided by the chemiluminescent signal of α‐tubulin.

Sun X., Kato H., Sato H., Han X., Hirofuji Y., Kato T.A., Sakai Y., Ohga S., Fukumoto S, & Masuda K. (2022). Dopamine‐related oxidative stress and mitochondrial dysfunction in dopaminergic neurons differentiated from deciduous teeth‐derived stem cells of children with Down syndrome. FASEB BioAdvances, 4(7), 454-467.

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Arabidopsis Pi Uptake Experiments

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The Arabidopsis Pi‐content and Pi‐uptake experiments were assayed as previously (Misson et al., 2004).
Detection of ³³Pi accumulation was performed with imaging plates as described (Kanno et al., 2012). The data were analysed using the Image Gauge software (Fujifilm, Tokyo, Japan). Preliminary experiments have shown that Pi‐uptake was linear at least from 30 min to 2 h (data not shown).

Bonnot C., Pinson B., Clément M., Bernillon S., Chiarenza S., Kanno S., Kobayashi N., Delannoy E., Nakanishi T.M., Nussaume L, & Desnos T. (2015). A chemical genetic strategy identify the PHOSTIN, a synthetic molecule that triggers phosphate starvation responses in Arabidopsis thaliana. The New Phytologist, 209(1), 161-176.

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