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abberior instruments stedycon  (abberior instruments)

 
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    abberior instruments abberior instruments stedycon
    Abberior Instruments Stedycon, supplied by abberior instruments, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/instruments+stedycon/instrument+stedycon/pmc11222159-292-6-6
    Average 90 stars, based on 1 article reviews
    abberior instruments stedycon - by Bioz Stars, 2026-10
    90/100 stars

    Images

    Related Articles

    Labeling:

    Article Title: Click Chemistry with Cell-Permeable Fluorophores Expands the Choice of Bioorthogonal Markers for Two-Color Live-Cell STED Nanoscopy.
    Article Snippet: .. After subsequent labeling with the tetrazine dye, cells were imaged using an abberior Instruments STEDYCON equipped with a top-stage incubation system to maintain the cells at 37 ◦C and 5% CO2. ..

    Incubation:

    Article Title: Click Chemistry with Cell-Permeable Fluorophores Expands the Choice of Bioorthogonal Markers for Two-Color Live-Cell STED Nanoscopy.
    Article Snippet: .. After subsequent labeling with the tetrazine dye, cells were imaged using an abberior Instruments STEDYCON equipped with a top-stage incubation system to maintain the cells at 37 ◦C and 5% CO2. ..

    Article Title: Multiple sclerosis severity variant in DYSF-ZNF638 locus associates with neuronal loss and inflammation
    Article Snippet: .. REAGENT or RESOURCE SOURCE IDENTIFIER Other Axioscan Z1 Zeiss N/A Ensembl (v112) EMBL-EBI https://www.ensembl.org/index.html FACSAria II cell sorter BD Bioscience N/A Fragment Analyzer Advanced Analytical Technologies at GenomeScan B.V. N/A KASP genotyping platform LGC Genomics N/A Molecular Signatures Database (MSigDB, version 2023.2) Subramanian et al.63 https://www.gsea-msigdb.org/gsea/ msigdb/index.jsp NovaSeq6000 Illumina at GenomeScan B.V. N/A STEDYCON microscope Abberior Instruments N/A TCS SP8 confocal microscope Leica N/A iScience 28, 112430, May 16, 2025 e3 were incubated with appropriate biotinylated secondary antibody, followed by avidin-biotin-horseradish peroxidase (HRP) complex (Vector Elite ABC kit; Vector Laboratories), before visualization with 3,3′-diaminobenzidine (DAB) and hematoxylin counterstaining. ..

    Imaging:

    Article Title: ASYNAPSIS3 has diverse dosage-dependent effects on meiotic crossover formation in Brassica napus
    Article Snippet: Images were captured using the SOPTOP RX50 fluorescent microscope (Sunny Optical Technology, China) equipped with a monochrome camera. .. For the super-resolution imaging of ZYP1 with REC8/ASY3 shown in using STED, Abberior STAR Red (goat anti-Rabbit) and STAR Orange (goat anti-Rat) were used as the secondary antibodies, and images were captured with an Olympus IX83 fluorescent microscope equipped with an Abberior instrument STEDYCON using the 561-nm (for STAR Orange) and 640-nm (for STAR Orange) excitation lasers and a 775-nm STED depletion laser. ..

    Article Title: ASYNAPSIS3 has diverse dosage-dependent effects on meiotic crossover formation in Brassica napus.
    Article Snippet: Crossovers create genetic diversity and are required for equal chromosome segregation during meiosis.. Crossover number and distribution are highly regulated by different mechanisms that are not yet fully understood, including crossover interference.. The chromosome axis is crucial for crossover formation.

    Microscopy:

    Article Title: ASYNAPSIS3 has diverse dosage-dependent effects on meiotic crossover formation in Brassica napus
    Article Snippet: Images were captured using the SOPTOP RX50 fluorescent microscope (Sunny Optical Technology, China) equipped with a monochrome camera. .. For the super-resolution imaging of ZYP1 with REC8/ASY3 shown in using STED, Abberior STAR Red (goat anti-Rabbit) and STAR Orange (goat anti-Rat) were used as the secondary antibodies, and images were captured with an Olympus IX83 fluorescent microscope equipped with an Abberior instrument STEDYCON using the 561-nm (for STAR Orange) and 640-nm (for STAR Orange) excitation lasers and a 775-nm STED depletion laser. ..

    Article Title: Multiple sclerosis severity variant in DYSF-ZNF638 locus associates with neuronal loss and inflammation
    Article Snippet: .. REAGENT or RESOURCE SOURCE IDENTIFIER Other Axioscan Z1 Zeiss N/A Ensembl (v112) EMBL-EBI https://www.ensembl.org/index.html FACSAria II cell sorter BD Bioscience N/A Fragment Analyzer Advanced Analytical Technologies at GenomeScan B.V. N/A KASP genotyping platform LGC Genomics N/A Molecular Signatures Database (MSigDB, version 2023.2) Subramanian et al.63 https://www.gsea-msigdb.org/gsea/ msigdb/index.jsp NovaSeq6000 Illumina at GenomeScan B.V. N/A STEDYCON microscope Abberior Instruments N/A TCS SP8 confocal microscope Leica N/A iScience 28, 112430, May 16, 2025 e3 were incubated with appropriate biotinylated secondary antibody, followed by avidin-biotin-horseradish peroxidase (HRP) complex (Vector Elite ABC kit; Vector Laboratories), before visualization with 3,3′-diaminobenzidine (DAB) and hematoxylin counterstaining. ..

    Article Title: ASYNAPSIS3 has diverse dosage-dependent effects on meiotic crossover formation in Brassica napus.
    Article Snippet: Crossovers create genetic diversity and are required for equal chromosome segregation during meiosis.. Crossover number and distribution are highly regulated by different mechanisms that are not yet fully understood, including crossover interference.. The chromosome axis is crucial for crossover formation.

    Article Title: Influenza virus uses mGluR2 as an endocytic receptor to enter cells
    Article Snippet: .. STED images were taken using an Abberior Instruments Stedycon equipped with an inverted IX83 microscope and a ×100/1.45 oil objective (Olympus). .. All acquisition operations were controlled using the Stedycon software (Abberior Instruments).

    Avidin-Biotin Assay:

    Article Title: Multiple sclerosis severity variant in DYSF-ZNF638 locus associates with neuronal loss and inflammation
    Article Snippet: .. REAGENT or RESOURCE SOURCE IDENTIFIER Other Axioscan Z1 Zeiss N/A Ensembl (v112) EMBL-EBI https://www.ensembl.org/index.html FACSAria II cell sorter BD Bioscience N/A Fragment Analyzer Advanced Analytical Technologies at GenomeScan B.V. N/A KASP genotyping platform LGC Genomics N/A Molecular Signatures Database (MSigDB, version 2023.2) Subramanian et al.63 https://www.gsea-msigdb.org/gsea/ msigdb/index.jsp NovaSeq6000 Illumina at GenomeScan B.V. N/A STEDYCON microscope Abberior Instruments N/A TCS SP8 confocal microscope Leica N/A iScience 28, 112430, May 16, 2025 e3 were incubated with appropriate biotinylated secondary antibody, followed by avidin-biotin-horseradish peroxidase (HRP) complex (Vector Elite ABC kit; Vector Laboratories), before visualization with 3,3′-diaminobenzidine (DAB) and hematoxylin counterstaining. ..

    other:

    Article Title: ADP-heptose attenuates Helicobacter pylori -induced dendritic cell activation
    Article Snippet: After washing the samples three times with PBS, glass cover slips were semi-dry mounted in ProLong Gold Antifade Mountant (Invitrogen #P36934) on a microscope slide.

    Article Title: An aldehyde-crosslinking mitochondrial probe for STED imaging in fixed cells
    Article Snippet: Sharing similar chromophore structure, absorption, and emission spectra (Ex = 584 nm, Em = 604 nm) with the nonfixable PKMO ( Fig. 1 C ), Cy3.5-NH 2 is also well-tailored for STED nanoscopy using a 775 nm depletion laser and showed excellent performance in live cell imaging when recorded with commercial STED nanoscopes (Abberior Instruments STEDYCON, Leica TCS SP8 gSTED, SI Appendix , Fig S7 ).

    Article Title: Somatostatin triggers local cAMP and Ca 2+ signaling in primary cilia to modulate pancreatic β-cell function.
    Article Snippet: The emission was detected at 483/32 and 542/27 nm using interference filters from Semrock.



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    NPM1 is necessary for pY397 FAK localization to the nucleolus in adherent cells (A) BCPAP cells were probed with antibodies against NPM1, FBL, and UBTF and imaged using <t>STED</t> microscopy. At least 50 cells were visualized in three independent experiments. Scale bar represent 1μm. (B) Percent of co-localization between pY397 FAK and NPM1, UBTF, and FBL respectively using Integrated Density Analysis by Image J. (C) 8505C cells were knocked down with either a non-targeting control or three shRNAs targeting NPM1 prior to immunoblotting with antibodies against NPM1, pY397 FAK, total FAK, or α-tubulin. Quantification of NPM1 expression is normalized to α-tubulin and sh-COO2 control and is listed under the NPM1 blot. MW marker is shown on the left of each blot in kDa. Two independent experiments were performed. (D) Immunofluorescence was performed in 8505C shCOO2 or shNPM1 cells probed with antibodies against pY397 FAK, FBL, and DAPI. Cells were imaged at 60X confocal imaging in three independent experiments with visualization of at least 50 cells. Scale bar represent 5 μm. (E) Percent of co-localization between pY397 FAK and FBL in our non-targeting controls and shNPM1 knockdown cells using Integrated Density Analysis by Image J. Results displayed as mean +/- SEM. *, p<0.05; **p < 0.01; ***p < 0.001.
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    NPM1 is necessary for pY397 FAK localization to the nucleolus in adherent cells (A) BCPAP cells were probed with antibodies against NPM1, FBL, and UBTF and imaged using <t>STED</t> microscopy. At least 50 cells were visualized in three independent experiments. Scale bar represent 1μm. (B) Percent of co-localization between pY397 FAK and NPM1, UBTF, and FBL respectively using Integrated Density Analysis by Image J. (C) 8505C cells were knocked down with either a non-targeting control or three shRNAs targeting NPM1 prior to immunoblotting with antibodies against NPM1, pY397 FAK, total FAK, or α-tubulin. Quantification of NPM1 expression is normalized to α-tubulin and sh-COO2 control and is listed under the NPM1 blot. MW marker is shown on the left of each blot in kDa. Two independent experiments were performed. (D) Immunofluorescence was performed in 8505C shCOO2 or shNPM1 cells probed with antibodies against pY397 FAK, FBL, and DAPI. Cells were imaged at 60X confocal imaging in three independent experiments with visualization of at least 50 cells. Scale bar represent 5 μm. (E) Percent of co-localization between pY397 FAK and FBL in our non-targeting controls and shNPM1 knockdown cells using Integrated Density Analysis by Image J. Results displayed as mean +/- SEM. *, p<0.05; **p < 0.01; ***p < 0.001.
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    NPM1 is necessary for pY397 FAK localization to the nucleolus in adherent cells (A) BCPAP cells were probed with antibodies against NPM1, FBL, and UBTF and imaged using <t>STED</t> microscopy. At least 50 cells were visualized in three independent experiments. Scale bar represent 1μm. (B) Percent of co-localization between pY397 FAK and NPM1, UBTF, and FBL respectively using Integrated Density Analysis by Image J. (C) 8505C cells were knocked down with either a non-targeting control or three shRNAs targeting NPM1 prior to immunoblotting with antibodies against NPM1, pY397 FAK, total FAK, or α-tubulin. Quantification of NPM1 expression is normalized to α-tubulin and sh-COO2 control and is listed under the NPM1 blot. MW marker is shown on the left of each blot in kDa. Two independent experiments were performed. (D) Immunofluorescence was performed in 8505C shCOO2 or shNPM1 cells probed with antibodies against pY397 FAK, FBL, and DAPI. Cells were imaged at 60X confocal imaging in three independent experiments with visualization of at least 50 cells. Scale bar represent 5 μm. (E) Percent of co-localization between pY397 FAK and FBL in our non-targeting controls and shNPM1 knockdown cells using Integrated Density Analysis by Image J. Results displayed as mean +/- SEM. *, p<0.05; **p < 0.01; ***p < 0.001.
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    NPM1 is necessary for pY397 FAK localization to the nucleolus in adherent cells (A) BCPAP cells were probed with antibodies against NPM1, FBL, and UBTF and imaged using <t>STED</t> microscopy. At least 50 cells were visualized in three independent experiments. Scale bar represent 1μm. (B) Percent of co-localization between pY397 FAK and NPM1, UBTF, and FBL respectively using Integrated Density Analysis by Image J. (C) 8505C cells were knocked down with either a non-targeting control or three shRNAs targeting NPM1 prior to immunoblotting with antibodies against NPM1, pY397 FAK, total FAK, or α-tubulin. Quantification of NPM1 expression is normalized to α-tubulin and sh-COO2 control and is listed under the NPM1 blot. MW marker is shown on the left of each blot in kDa. Two independent experiments were performed. (D) Immunofluorescence was performed in 8505C shCOO2 or shNPM1 cells probed with antibodies against pY397 FAK, FBL, and DAPI. Cells were imaged at 60X confocal imaging in three independent experiments with visualization of at least 50 cells. Scale bar represent 5 μm. (E) Percent of co-localization between pY397 FAK and FBL in our non-targeting controls and shNPM1 knockdown cells using Integrated Density Analysis by Image J. Results displayed as mean +/- SEM. *, p<0.05; **p < 0.01; ***p < 0.001.
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    NPM1 is necessary for pY397 FAK localization to the nucleolus in adherent cells (A) BCPAP cells were probed with antibodies against NPM1, FBL, and UBTF and imaged using <t>STED</t> microscopy. At least 50 cells were visualized in three independent experiments. Scale bar represent 1μm. (B) Percent of co-localization between pY397 FAK and NPM1, UBTF, and FBL respectively using Integrated Density Analysis by Image J. (C) 8505C cells were knocked down with either a non-targeting control or three shRNAs targeting NPM1 prior to immunoblotting with antibodies against NPM1, pY397 FAK, total FAK, or α-tubulin. Quantification of NPM1 expression is normalized to α-tubulin and sh-COO2 control and is listed under the NPM1 blot. MW marker is shown on the left of each blot in kDa. Two independent experiments were performed. (D) Immunofluorescence was performed in 8505C shCOO2 or shNPM1 cells probed with antibodies against pY397 FAK, FBL, and DAPI. Cells were imaged at 60X confocal imaging in three independent experiments with visualization of at least 50 cells. Scale bar represent 5 μm. (E) Percent of co-localization between pY397 FAK and FBL in our non-targeting controls and shNPM1 knockdown cells using Integrated Density Analysis by Image J. Results displayed as mean +/- SEM. *, p<0.05; **p < 0.01; ***p < 0.001.
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    NPM1 is necessary for pY397 FAK localization to the nucleolus in adherent cells (A) BCPAP cells were probed with antibodies against NPM1, FBL, and UBTF and imaged using <t>STED</t> microscopy. At least 50 cells were visualized in three independent experiments. Scale bar represent 1μm. (B) Percent of co-localization between pY397 FAK and NPM1, UBTF, and FBL respectively using Integrated Density Analysis by Image J. (C) 8505C cells were knocked down with either a non-targeting control or three shRNAs targeting NPM1 prior to immunoblotting with antibodies against NPM1, pY397 FAK, total FAK, or α-tubulin. Quantification of NPM1 expression is normalized to α-tubulin and sh-COO2 control and is listed under the NPM1 blot. MW marker is shown on the left of each blot in kDa. Two independent experiments were performed. (D) Immunofluorescence was performed in 8505C shCOO2 or shNPM1 cells probed with antibodies against pY397 FAK, FBL, and DAPI. Cells were imaged at 60X confocal imaging in three independent experiments with visualization of at least 50 cells. Scale bar represent 5 μm. (E) Percent of co-localization between pY397 FAK and FBL in our non-targeting controls and shNPM1 knockdown cells using Integrated Density Analysis by Image J. Results displayed as mean +/- SEM. *, p<0.05; **p < 0.01; ***p < 0.001.
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    Image Search Results


    NPM1 is necessary for pY397 FAK localization to the nucleolus in adherent cells (A) BCPAP cells were probed with antibodies against NPM1, FBL, and UBTF and imaged using STED microscopy. At least 50 cells were visualized in three independent experiments. Scale bar represent 1μm. (B) Percent of co-localization between pY397 FAK and NPM1, UBTF, and FBL respectively using Integrated Density Analysis by Image J. (C) 8505C cells were knocked down with either a non-targeting control or three shRNAs targeting NPM1 prior to immunoblotting with antibodies against NPM1, pY397 FAK, total FAK, or α-tubulin. Quantification of NPM1 expression is normalized to α-tubulin and sh-COO2 control and is listed under the NPM1 blot. MW marker is shown on the left of each blot in kDa. Two independent experiments were performed. (D) Immunofluorescence was performed in 8505C shCOO2 or shNPM1 cells probed with antibodies against pY397 FAK, FBL, and DAPI. Cells were imaged at 60X confocal imaging in three independent experiments with visualization of at least 50 cells. Scale bar represent 5 μm. (E) Percent of co-localization between pY397 FAK and FBL in our non-targeting controls and shNPM1 knockdown cells using Integrated Density Analysis by Image J. Results displayed as mean +/- SEM. *, p<0.05; **p < 0.01; ***p < 0.001.

    Journal: Frontiers in Oncology

    Article Title: Focal adhesion kinase promotes ribosome biogenesis to drive advanced thyroid cancer cell growth and survival

    doi: 10.3389/fonc.2025.1252544

    Figure Lengend Snippet: NPM1 is necessary for pY397 FAK localization to the nucleolus in adherent cells (A) BCPAP cells were probed with antibodies against NPM1, FBL, and UBTF and imaged using STED microscopy. At least 50 cells were visualized in three independent experiments. Scale bar represent 1μm. (B) Percent of co-localization between pY397 FAK and NPM1, UBTF, and FBL respectively using Integrated Density Analysis by Image J. (C) 8505C cells were knocked down with either a non-targeting control or three shRNAs targeting NPM1 prior to immunoblotting with antibodies against NPM1, pY397 FAK, total FAK, or α-tubulin. Quantification of NPM1 expression is normalized to α-tubulin and sh-COO2 control and is listed under the NPM1 blot. MW marker is shown on the left of each blot in kDa. Two independent experiments were performed. (D) Immunofluorescence was performed in 8505C shCOO2 or shNPM1 cells probed with antibodies against pY397 FAK, FBL, and DAPI. Cells were imaged at 60X confocal imaging in three independent experiments with visualization of at least 50 cells. Scale bar represent 5 μm. (E) Percent of co-localization between pY397 FAK and FBL in our non-targeting controls and shNPM1 knockdown cells using Integrated Density Analysis by Image J. Results displayed as mean +/- SEM. *, p<0.05; **p < 0.01; ***p < 0.001.

    Article Snippet: Images were acquired on STED Abberior Stedycon Instrument in the ALMC.

    Techniques: Microscopy, Control, Western Blot, Expressing, Marker, Immunofluorescence, Imaging, Knockdown

    NOP56 co-localizes with pY397 FAK and promotes thyroid cancer growth (A) BioID workflow representing FAK fused to a promiscuous biotin ligase and interacting partners of FAK being biotinylated, pulled down, and identified by mass spectrometry. (B) Immunoblotting of BCPAP cells transduced with EV, WT, and Y397F FAK BioID2 and probed with antibodies against pY397 FAK, total FAK, and α-tubulin. The higher MW band represents the 27kDA BioID2 construct fused to WT or Y397 FAK and lower MW band is the endogenous FAK band. (C) STRING analysis of significantly enriched proteins reveals known interacting partners of FAK. Blue connections signify known interactions from database. Red connections signify experimentally determined known interactions. (D) FAK interacting partners were identified by analyzing proteins that bind to WT FAK in both datasets and enriched at least 2-fold change compared to EV. Gene Ontology Pathway Analysis was conducted for molecular function pathways with a false discovery rate (FDR) <0.05. (E) Gene Ontology Pathway Analysis was conducted for cellular compartment pathways with FDR < 0.05. (F) STRING analysis of nucleolar proteins identified by Gene Ontology Pathway Analysis. Blue connections signify known interactions from database. Red connections signify experimentally determined known interactions. (G) Confocal microscopy of KTC2 cells was performed with antibodies against pY397 FAK and NOP56. At least 50 cells were imaged at 100X with the Abberior Stedycon microscope in two independent experiments. Scale bar represent 2 μm. (H) Immunoblotting of KTC2 cells transduced with a non-targeting control or three NOP56 shRNAs was performed with antibodies against NOP56 and α-tubulin. MW marker is shown on the left of each blot in kDa . (I) Clonogenic assays of KTC2 cells transduced with non-targeting control or NOP56 shRNA were performed. Colonies were stained with crystal violet and imaged after 10 days. Integrated Density was utilized to quantify clonogenic growth using LICOR Odyssey software. Experiments were performed in biological triplicate experiments. Results are displayed as mean +/- SEM. *, p < 0.05.

    Journal: Frontiers in Oncology

    Article Title: Focal adhesion kinase promotes ribosome biogenesis to drive advanced thyroid cancer cell growth and survival

    doi: 10.3389/fonc.2025.1252544

    Figure Lengend Snippet: NOP56 co-localizes with pY397 FAK and promotes thyroid cancer growth (A) BioID workflow representing FAK fused to a promiscuous biotin ligase and interacting partners of FAK being biotinylated, pulled down, and identified by mass spectrometry. (B) Immunoblotting of BCPAP cells transduced with EV, WT, and Y397F FAK BioID2 and probed with antibodies against pY397 FAK, total FAK, and α-tubulin. The higher MW band represents the 27kDA BioID2 construct fused to WT or Y397 FAK and lower MW band is the endogenous FAK band. (C) STRING analysis of significantly enriched proteins reveals known interacting partners of FAK. Blue connections signify known interactions from database. Red connections signify experimentally determined known interactions. (D) FAK interacting partners were identified by analyzing proteins that bind to WT FAK in both datasets and enriched at least 2-fold change compared to EV. Gene Ontology Pathway Analysis was conducted for molecular function pathways with a false discovery rate (FDR) <0.05. (E) Gene Ontology Pathway Analysis was conducted for cellular compartment pathways with FDR < 0.05. (F) STRING analysis of nucleolar proteins identified by Gene Ontology Pathway Analysis. Blue connections signify known interactions from database. Red connections signify experimentally determined known interactions. (G) Confocal microscopy of KTC2 cells was performed with antibodies against pY397 FAK and NOP56. At least 50 cells were imaged at 100X with the Abberior Stedycon microscope in two independent experiments. Scale bar represent 2 μm. (H) Immunoblotting of KTC2 cells transduced with a non-targeting control or three NOP56 shRNAs was performed with antibodies against NOP56 and α-tubulin. MW marker is shown on the left of each blot in kDa . (I) Clonogenic assays of KTC2 cells transduced with non-targeting control or NOP56 shRNA were performed. Colonies were stained with crystal violet and imaged after 10 days. Integrated Density was utilized to quantify clonogenic growth using LICOR Odyssey software. Experiments were performed in biological triplicate experiments. Results are displayed as mean +/- SEM. *, p < 0.05.

    Article Snippet: Images were acquired on STED Abberior Stedycon Instrument in the ALMC.

    Techniques: Mass Spectrometry, Western Blot, Transduction, Construct, Confocal Microscopy, Microscopy, Control, Marker, shRNA, Staining, Software