Fv1000 laser scanning confocal microscope

Manufactured by Leica

Sourced in Germany

The FV1000 is a laser scanning confocal microscope designed for high-resolution imaging. It utilizes advanced laser technology to provide detailed, three-dimensional images of biological samples. The FV1000 offers efficient optical sectioning and reduced background noise, enabling users to capture clear, high-quality data.

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Lab products found in correlation

Fetal calf serum (fcs), by Merck Group (2 mentions) Dulbecco s modified eagle s medium, by Merck Group (2 mentions) Lipofectamine 2000 transfection reagent, by Thermo Fisher Scientific (2 mentions) Anti c myc antibody, by Abcam (2 mentions) Bovine serum albumin (bsa), by Abcam (2 mentions) Microwave antigen retrieval, by Thermo Fisher Scientific (2 mentions) Anti tdo2 antibody, by Abcam (2 mentions) Anti kyn antibody, by Abcam (2 mentions) Abc hrp kit, by Thermo Fisher Scientific (2 mentions) Anti ahr antibody, by Abcam (2 mentions) Anti pcna antibody, by Santa Cruz Biotechnology (1 mentions) Confocal laser scanning microscope, by Leica (1 mentions) Alexa fluor 488, by Thermo Fisher Scientific (1 mentions) G418 sulphate, by Thermo Fisher Scientific (1 mentions) Anti flag antibody, by Merck Group (1 mentions) Cy3 conjugated anti mouse antibody, by Merck Group (1 mentions) Anti sox2 antibody, by Abcam (1 mentions) Citrate edta antigen retrieval solution, by Beyotime (1 mentions) Ab181496, by Abcam (1 mentions) Ab38449, by Abcam (1 mentions)

Close spelling variants of this product

Confocal microscope (1146 citations) Confocal laser scanning microscope (971 citations) Laser confocal microscope (209 citations) FV1000 (35 citations) Laser scanning microscope (22 citations) FV1000 confocal microscope (7 citations)

10 protocols using fv1000 laser scanning confocal microscope

PARI-PCNA Colocalization Assay

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HEK293FT cells were grown in Dulbecco's modified Eagle's medium (Sigma) supplemented with 10% Fetal Calf Serum (FCS) (Sigma) at 37°C. Transfections were carried out using Lipofectamine 2000 transfection reagent (Invitrogen) according to the instruction of the manufacturer. After treatment with UV (as indicated), cells were incubated for 6 h and immunostained where indicated. For cellular localizations of Flag-PARI and PCNA, cells were treated with a detergent solution (10 mM TRIS–HCl, 2.5 mM MgCl₂, 1% NP-40, 1 mM PMSF) and immunostained using anti-Flag antibody (Sigma M2 A8592) diluted 1:300 and Alexa Fluor 488 (Invitrogen, A11011) diluted 1:500, anti-PCNA antibody (Santa Cruz, sc-56) diluted 1:200. Samples were mounted in 25% glycerol in PBS containing 1 mg/ml DAPI followed by microscopy using an Olympus FV1000 confocal Laser Scanning Microscope and a Leica confocal Laser Scanning Microscope.
PARI PCNA co-localization was quantified by counting all PCNA PARI co-localizations in 50 randomly selected cells. All countings were repeated in at least three independent experiments.

Burkovics P., Dome L., Juhasz S., Altmannova V., Sebesta M., Pacesa M., Fugger K., Sorensen C.S., Lee M.Y., Haracska L, & Krejci L. (2016). The PCNA-associated protein PARI negatively regulates homologous recombination via the inhibition of DNA repair synthesis. Nucleic Acids Research, 44(7), 3176-3189.

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Efficient Delivery of miR-99a by PEAL-LA Nanoparticles

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Confocal laser scanning microscopy (CLSM) was employed to evaluate the delivery efficiency of miR-99a. Lipofectamine^TM2000 (Lip2000) transfection reagent was used as a positive control. In brief, HepG2 cells (2 × 10⁵ cells/well) were seeded into a CLSM dish and incubated overnight. Then, Cy5-miR-99a-Lip2000, Cy5-miR-99a-PEAL-LA NPs or Cy5-miR-99a-PEAL-LA/VEGFab NPs, each containing equivalent amounts of Cy5-miR-99a, was added to the culture dish and incubated in the dark for 4 h. Then, the cells were fixed with 4% paraformaldehyde for 15 min and stained with DAPI for another 10 min. The cellular uptake of the Cy5-labeled miR-99a was determined using an FV1000 confocal laser scanning microscope (Leica, Germany).

Cai C., Xie Y., Wu L., Chen X., Liu H., Zhou Y., Zou H., Liu D., Zhao Y., Kong X, & Liu P. (2017). PLGA-based dual targeted nanoparticles enhance miRNA transfection efficiency in hepatic carcinoma. Scientific Reports, 7, 46250.

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Generation of HLTF-Silenced HCT116 Cell Lines

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HCT116 human cells were grown in Dulbecco's modified Eagle's medium (Sigma) supplemented with 10% FCS (Sigma) at 37°C. Transfections were carried out using Lipofectamine 2000 transfection reagent (Invitrogen) according to the instructions of the manufacturer. To generate HLTF-specific shRNA-silenced stable cell lines, we cloned the HLTF-specific DNA sequences O2611 (GAT CCC CGG TGC TTT GGC CTA TAT CAt tca aga gaT GAT ATA GGC CAA AGC ACC TTT TTG GAA A) and O2612 (AGC TTT TCC AAA AAG GTG CTT TGG CCT ATA TCA tct ctt gaa TGA TAT AGG CCA AAG CAC CGG G) into the HindIII site of the shRNA-Neo plasmid, resulting in pIL2394. Next, the silencing plasmid was transfected into HCT116 cells, followed by selection using G-418 SULPHATE (Gibco, cat. no.: 11811064) to obtain stable cell lines.
The cellular localization of expressed FLAG-HLTF WT and HIRAN domain mutant proteins was analyzed by immunostaining using anti-Flag antibody (Sigma) diluted 1:300 and Cy3-conjugated anti-mouse antibody (Sigma, cat. no.: C2181) diluted 1:1000. Samples were mounted in phosphate-buffered saline (PBS) containing 25% glycerol and 1 mg/ml DAPI, followed by microscopy using an Olympus FV1000 confocal laser scanning microscope and a Leica confocal LSM.

Achar Y.J., Balogh D., Neculai D., Juhasz S., Morocz M., Gali H., Dhe-Paganon S., Venclovas Č, & Haracska L. (2015). Human HLTF mediates postreplication repair by its HIRAN domain-dependent replication fork remodelling. Nucleic Acids Research, 43(21), 10277-10291.

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Immunofluorescence Analysis of NSCLC Tumor Markers

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The pathological sections of NSCLC patients’ tumor tissues were retrieved by microwave antigen retrieval (Citrate-EDTA Antigen Retrieval Solution, Beyotime). The sections were then blocked with 5% BSA and incubated with mouse monoclonal anti-integrin αvβ3 (1:100, ab7166, Abcam, UK), rabbit monoclonal SOX2 (1:200, ab92494, Abcam, Cambridge, UK), rabbit polyclonal p-AKT (1:200, ab38449, Abcam, Cambridge, UK), rabbit monoclonal KLF (1:200, ab215036, Abcam, Cambridge, UK), rabbit monoclonal total-PI3K (1:500, ab302958, Abcam, Cambridge, UK), mouse monoclonal CD90 (1:100, ab181496, Abcam, Cambridge, UK) for 4 °C overnight, and followed by horse radish peroxidase (HRP) conjugated secondary antibodies (1:600; Abcam, Cambridge, UK), and the nucleus was stained with DAPI. In addition, the A594 and Lewis cells were fixed in 4% paraformaldehyde, permeabilized with 0.2% triton-X100, and blocked by 5%BSA, followed by incubating with anti-SOX2 antibody (1:200, Abcam, Cambridge, UK) for 4 °C overnight, and followed by HRP conjugated secondary antibodies (1:600; Abcam, Cambridge, UK), and the nucleus was stained with DAPI. All immunofluorescence images were captured from FV1000 laser scanning confocal microscope (Leica, Barnack, Germany) and analyzed by IPP software.

Wu J.L., Xu C.F., Yang X.H, & Wang M.S. (2023). Fibronectin promotes tumor progression through integrin αvβ3/PI3K/AKT/SOX2 signaling in non-small cell lung cancer. Heliyon, 9(9), e20185.

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Immunostaining of Prostate Cancer Markers

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Pathological sections of prostatic tissues were retrieved using microwave antigen retrieval (Thermo, USA). Then samples were blocked by 5% Bovine Serum Albumin, followed by incubating with anti-TDO2 antibody (1:200, abcam, UK), anti-Kyn antibody (1:300, abcam, UK), anti-AhR antibody (1:200, abcam, UK), anti- NF-κB (1:200, abcam, UK) and anti-c-Myc antibody (1:500, abcam, UK) for 4 °C overnight. For immunofluorescence staining, the sections were then incubated with secondary antibodies (1:1000; abcam, UK), and the nucleus was stained with DAPI. Images were captured using a FV1000 laser scanning confocal microscope (Leica, Germany). For immunohistochemical staining, the sections were then stained using the ABC HRP Kit (Thermo, USA) and counterstaining with hematoxylin. Immunohistochemical images were captured using microscope (Leica, Germany). The intensity of proteins in sections were analyzed by Image-Pro Plus 2.0 software.

Li F., Zhao Z., Zhang Z., Zhang Y, & Guan W. (2021). Tryptophan metabolism induced by TDO2 promotes prostatic cancer chemotherapy resistance in a AhR/c-Myc dependent manner. BMC Cancer, 21, 1112.

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Quantifying Receptor Expression in Bipolar Cells

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Images were acquired with an Olympus FV 1000 laser scanning confocal microscope and a 1.35 NA 60X oil immersion objective or a Leica SP8 confocal microscope and a 1.4 NA 63X oil immersion objective at a voxel size around 0.05–0.05–0.3 μm (x-y-z). Further processing of image stacks was performed using MetaMorph (Molecular Devices) and Amira (Thermo Fisher Scientific) software. Because neighboring synaptic puncta could not always be resolved by confocal microscopy for quantification, we determined the volume occupied by the receptor signal within the BC terminal and divided this value by the volume of the BC terminal to obtain a ‘percent volume occupancy’ of receptor expression (see Hoon et al., 2017b (link)). To quantify % occupancy of receptor immunoreactivity within bipolar cells, bipolar cell processes were first masked in 3D using the LabelField function of Amira. Receptor signal within the bipolar process was next isolated with the Amira Arithmetic tool. A threshold was thereafter applied to eliminate background pixels and the total volume of ‘receptor pixels’ above background was then expressed as a percent (%) occupancy relative to the volume of the bipolar cell process (for more details on threshold selection and volume occupancy, see Hoon et al., 2017b (link); Hoon et al., 2015 (link)).

Sinha R., Siddiqui T.J., Padmanabhan N., Wallin J., Zhang C., Karimi B., Rieke F., Craig A.M., Wong R.O, & Hoon M. (2020). LRRTM4: A novel regulator of presynaptic inhibition and ribbon synapse arrangements of retinal bipolar cells. Neuron, 105(6), 1007-1017.e5.

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Immunofluorescence Analysis of c-Myc in Tumor Tissues

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The pathological sections of tumor tissues were retrieved by EDTA antigen retrieval (Solarbio). The tumor cells were fixed with 4% paraformaldehyde and permeated by 0.5% Triton‐X100. The tissues or cell samples were then blocked by 5% BSA, followed by incubating with anti‐c‐Myc primary Ab (1:400, Abcam) for 4°C overnight, and followed by secondary Abs (1:600; Abcam). The nucleus was stained with DAPI. The immunofluorescence images were captured from FV1000 laser scanning confocal microscope (Leica, Barnack).

Liu S., Chen L., Zhao H., Li Q., Hu R, & Wang H. (2020). Integrin β8 facilitates tumor growth and drug resistance through a Y‐box binding protein 1‐dependent signaling pathway in bladder cancer. Cancer Science, 111(7), 2423-2430.

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Probing PI3K/AKT Signaling in Bladder Cancer

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We fixed and permeabilized MB49 cells treated with collagen or E7820 to examine the PI3K/AKT signaling pathway in bladder cancer cells. Then the cells were labeled with anti‐integrin β1 (1:200; Abcam), anti‐p‐PI3K (1:200; Abcam), or p‐AKT (1:200; Abcam) followed by Alexa 594 secondary Abs (1:800; Abcam). In addition, nuclei were labeled with DAPI. All immunofluorescence images were captured from FV1000 laser scanning confocal microscope (Leica, Wetzlar, Germany).

Qiu S., Deng L., Liao X., Nie L., Qi F., Jin K., Tu X., Zheng X., Li J., Liu L., Liu Z., Bao Y., Ai J., Lin T., Yang L, & Wei Q. (2019). Tumor‐associated macrophages promote bladder tumor growth through PI3K/AKT signal induced by collagen. Cancer Science, 110(7), 2110-2118.

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Quantifying PKM2 Expression in Cells

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Cells were seeded in glass coverslips for 24 h, and treated with 8mg/mL mJPYZ for 48 h. The treated cell slices were fixed with 4% paraformaldehyde, washed with PBS, and incubated with primary antibodies against PKM2 at 4°C overnight. The next day, after incubation with fluorescence secondary antibody and 4′,6-diamidine-2-phenylindole, the slices were mounted and observed with an FV1000 laser scanning confocal microscope (Leica, Wetzlar, Germany). All double immunofluorescence images were captured under the same conditions. The co-localization analysis was performed using Image J software (NIH Image, Bethesda, MD, USA).

Sun Q., Yuan M., Wang H., Zhang X., Zhang R., Wang H., Chen X., Zhu M., Liu S, & Wu J. (2021). PKM2 Is the Target of a Multi-Herb-Combined Decoction During the Inhibition of Gastric Cancer Progression. Frontiers in Oncology, 11, 767116.

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Immunohistochemical Profiling of Prostate Tissue

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Pathological sections of prostatic tissues were retrieved using microwave antigen retrieval (Thermo, USA). Then samples were blocked by 5% Bovine Serum Albumin, followed by incubating with anti-TDO2 antibody (1:200, abcam, UK), anti-Kyn antibody (1:300, abcam, UK), anti-AhR antibody (1:200, abcam, UK) and anti-c-Myc antibody (1:500, abcam, UK) for 4ºC overnight. For immuno uorescence staining, the sections were then incubated with secondary antibodies (1:1000; abcam, UK), and the nucleus was stained with DAPI. Images were captured using a FV1000 laser scanning confocal microscope (Leica, Germany). For immunohistochemical staining, the sections were then stained using the ABC HRP Kit (Thermo, USA) and counterstaining with hematoxylin. Immunohistochemical images were captured using microscope (Leica, Germany). The intensity of proteins in sections were analyzed by Image-Pro Plus 2.0 software.

Li F., Zhao Z., Zhang Z., ZHANG Y., & Guan W. (2021). Tryptophan Metabolism Induced by TDO2 Promotes Prostatic Cancer Chemotherapy Resistance in a Ahr/C-Myc Dependent Manner.

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