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stedycon  (abberior instruments)

 
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    Structured Review

    abberior instruments stedycon
    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/stedycon/pm37914933-548-9-10
    Average 90 stars, based on 1 article reviews
    stedycon - by Bioz Stars, 2026-11
    90/100 stars

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    Related Articles

    other:

    Article Title: Control of epithelial tissue organization by mRNA localization.
    Article Snippet: The gross tissue morphology of each tissue was visualized by H&E staining (abcam; ab245880).

    Article Title: Neural and behavioral binaural hearing impairment and its recovery following moderate noise exposure.
    Article Snippet: Noise-induced cochlear synaptopathy has been studied for over 25 years with no known diagnosis for this disorder in humans.. This type of “hidden hearing loss” induces a loss of synapses in the inner ear but no change in audiometric thresholds.. Recent studies have shown that by two months post synaptopathy-inducing noise exposure, synapses in some animal species can regenerate.

    Staining:

    Article Title: Investigation of neuromodulation of the endbulb of Held synapse in the cochlear nucleus by serotonin and norepinephrine
    Article Snippet: Next, the slides were washed in 5 mM phosphate buffer for 5 min and mounted with 50 μl of fluorescence mounting medium based on Mowiol 4–88 (Carl Roth, Karlsruhe, Germany) and covered with a thin glass coverslip. .. Two-color STED images of cryosections stained for monoamine transporters were acquired using a STEDYCON (Abberior Instruments GmbH, Göttingen, Germany) with a 100× oil immersion objective. .. Images of the monoamine receptor preparations were taken with Zeiss confocal laser scanning microscopes 780 and 880 with 40× or 100× oil immersion objectives.

    Imaging:

    Article Title: Endogenous SNAP-Tagging of Munc13‑1 for Monitoring Synapse Nanoarchitecture
    Article Snippet: .. Live confocal and STED imaging was done on a STEDYCON system (Abberior Instruments GmbH, Göttingen), mounted on a Nikon Eclipse TI research microscope, equipped with a Plan APO Lambda D100X/1.45 NA oil objective (Nikon) and controlled by NIS Elements (Nikon). ..

    Article Title: Lamin A/C safeguards replication initiation by orchestrating chromatin accessibility and PCNA recruitment
    Article Snippet: .. Confocal and STED imaging was performed using the Stedycon system (Abberior) equipped with a 100× oil-immersion objective (UPlanSApo 100×, 1.40 NA, Olympus) for high-resolution imaging. ..

    Microscopy:

    Article Title: Endogenous SNAP-Tagging of Munc13‑1 for Monitoring Synapse Nanoarchitecture
    Article Snippet: .. Live confocal and STED imaging was done on a STEDYCON system (Abberior Instruments GmbH, Göttingen), mounted on a Nikon Eclipse TI research microscope, equipped with a Plan APO Lambda D100X/1.45 NA oil objective (Nikon) and controlled by NIS Elements (Nikon). ..



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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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    Average 90 stars, based on 1 article reviews
    instruments stedycon - by Bioz Stars, 2026-11
    90/100 stars
    		  Buy from Supplier
    stedycon instrument  (abberior instruments)
    90
    abberior instruments stedycon instrument
    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.
    Stedycon Instrument, 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
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    		  Buy from Supplier

    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