Review



mouse α emcv 3d polymerase  (Santa Cruz Biotechnology)


Bioz Verified Symbol Santa Cruz Biotechnology is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 93
      Buy from Supplier

    Structured Review

    Santa Cruz Biotechnology mouse α emcv 3d polymerase
    a , b <t>EMCV-Wt</t> and <t>EMCV-L</t> Zn -infected HeLa cells and corresponding cell culture supernatants were harvested at the indicated timepoints after infection. Line graphs display the increase in intracellular virus titers ( a ) and virus titers in the cell culture supernatant ( b ) over time, as determined by end-point dilution. Depicted are mean values ± SD from n = 3 independent experiments. c 10 K and 100 K EVs were separated from naked virions using density gradient centrifugation and EV-enclosed virus titers were determined by end-point dilution assay. Bars display the mean fold infectivity of EMCV-L Zn EVs relative to EMCV-Wt EVs ± SD from n = 5 independent experiments. **** p < 0.0001, as assessed by a two-tailed one-sample t -test. ND not detected. d 100 K EVs released by cells infected with either EMCV-Wt or EMCV-L Zn were isolated and EV-protein composition was analyzed by LC-MS/MS. The number of unique EMCV peptides identified within and outside of the capsid-coding region are indicated. Source data are provided as a Source Data file.
    Mouse α Emcv 3d Polymerase, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/3d+interactive+microscopy+visualization+software/pmc09232559-312-87-94?v=Santa+Cruz+Biotechnology
    Average 93 stars, based on 6 article reviews
    mouse α emcv 3d polymerase - by Bioz Stars, 2026-08
    93/100 stars

    Images

    1) Product Images from "The encephalomyocarditis virus Leader promotes the release of virions inside extracellular vesicles via the induction of secretory autophagy"

    Article Title: The encephalomyocarditis virus Leader promotes the release of virions inside extracellular vesicles via the induction of secretory autophagy

    Journal: Nature Communications

    doi: 10.1038/s41467-022-31181-y

    a , b EMCV-Wt and EMCV-L Zn -infected HeLa cells and corresponding cell culture supernatants were harvested at the indicated timepoints after infection. Line graphs display the increase in intracellular virus titers ( a ) and virus titers in the cell culture supernatant ( b ) over time, as determined by end-point dilution. Depicted are mean values ± SD from n = 3 independent experiments. c 10 K and 100 K EVs were separated from naked virions using density gradient centrifugation and EV-enclosed virus titers were determined by end-point dilution assay. Bars display the mean fold infectivity of EMCV-L Zn EVs relative to EMCV-Wt EVs ± SD from n = 5 independent experiments. **** p < 0.0001, as assessed by a two-tailed one-sample t -test. ND not detected. d 100 K EVs released by cells infected with either EMCV-Wt or EMCV-L Zn were isolated and EV-protein composition was analyzed by LC-MS/MS. The number of unique EMCV peptides identified within and outside of the capsid-coding region are indicated. Source data are provided as a Source Data file.
    Figure Legend Snippet: a , b EMCV-Wt and EMCV-L Zn -infected HeLa cells and corresponding cell culture supernatants were harvested at the indicated timepoints after infection. Line graphs display the increase in intracellular virus titers ( a ) and virus titers in the cell culture supernatant ( b ) over time, as determined by end-point dilution. Depicted are mean values ± SD from n = 3 independent experiments. c 10 K and 100 K EVs were separated from naked virions using density gradient centrifugation and EV-enclosed virus titers were determined by end-point dilution assay. Bars display the mean fold infectivity of EMCV-L Zn EVs relative to EMCV-Wt EVs ± SD from n = 5 independent experiments. **** p < 0.0001, as assessed by a two-tailed one-sample t -test. ND not detected. d 100 K EVs released by cells infected with either EMCV-Wt or EMCV-L Zn were isolated and EV-protein composition was analyzed by LC-MS/MS. The number of unique EMCV peptides identified within and outside of the capsid-coding region are indicated. Source data are provided as a Source Data file.

    Techniques Used: Infection, Cell Culture, Virus, Gradient Centrifugation, End-point Dilution Assay, Two Tailed Test, Isolation, Liquid Chromatography with Mass Spectroscopy

    a 10,000× g (10 K) and 100,000× g (100 K) ultracentrifugation pellets were collected from an equal number of EV-producing cells 8 h after mock, EMCV-Wt, or EMCV-L Zn infection and analyzed by western blotting for the presence of EV-marker proteins CD9, CD63, and flotillin. Depicted is a representative of n = 3 independent experiments. b – g EVs were isolated from cell culture supernatants of mock, EMCV-Wt, and EMCV-L Zn infected cells by differential ultracentrifugation and density gradient centrifugation at indicated timepoints p.i. EVs were fluorescently labeled with CFSE and analyzed by high-resolution flow cytometry. b The contribution of 10 K vs. 100 K EVs to the overall EV release by mock, EMCV-Wt, and EMCV-L Zn infected cells was quantified. Mean values ± SD are presented for n = 3 independent experiments. **left p = 0.0025, **right p = 0.0015. c , d Depicted is the increase over time of 100 K EV numbers present in 1.06–1.10 g/ml fractions measured in a fixed time window of 30 s ( c ) and the number of EVs present in those density fractions at 8 h p.i. ( d ). ** p = 0.0047, * p = 0.0107. e Representative FSC/SSC dot plots are depicted of the samples in ( d ). Gates delineate FSC-high and FSC-low EVs. f , g Presented are the percentage of FSC-high EVs of the total EVs present in the 1.08 g/ml density fraction at the indicated timepoints ( f ) and the percentage of FSC-high EVs at 8 h p.i. ( g ). ** left p = 0.0061, ** right p = 0.0084. For ( c ) and ( f ) a representative image of n = 2 individual experiments is shown. For ( d ) and ( g ) mean values ± SD are presented for n = 4 independent experiments. p values were assessed by one-way ANOVA with Tukey’s multiple comparisons test. Source data are provided as a Source Data file.
    Figure Legend Snippet: a 10,000× g (10 K) and 100,000× g (100 K) ultracentrifugation pellets were collected from an equal number of EV-producing cells 8 h after mock, EMCV-Wt, or EMCV-L Zn infection and analyzed by western blotting for the presence of EV-marker proteins CD9, CD63, and flotillin. Depicted is a representative of n = 3 independent experiments. b – g EVs were isolated from cell culture supernatants of mock, EMCV-Wt, and EMCV-L Zn infected cells by differential ultracentrifugation and density gradient centrifugation at indicated timepoints p.i. EVs were fluorescently labeled with CFSE and analyzed by high-resolution flow cytometry. b The contribution of 10 K vs. 100 K EVs to the overall EV release by mock, EMCV-Wt, and EMCV-L Zn infected cells was quantified. Mean values ± SD are presented for n = 3 independent experiments. **left p = 0.0025, **right p = 0.0015. c , d Depicted is the increase over time of 100 K EV numbers present in 1.06–1.10 g/ml fractions measured in a fixed time window of 30 s ( c ) and the number of EVs present in those density fractions at 8 h p.i. ( d ). ** p = 0.0047, * p = 0.0107. e Representative FSC/SSC dot plots are depicted of the samples in ( d ). Gates delineate FSC-high and FSC-low EVs. f , g Presented are the percentage of FSC-high EVs of the total EVs present in the 1.08 g/ml density fraction at the indicated timepoints ( f ) and the percentage of FSC-high EVs at 8 h p.i. ( g ). ** left p = 0.0061, ** right p = 0.0084. For ( c ) and ( f ) a representative image of n = 2 individual experiments is shown. For ( d ) and ( g ) mean values ± SD are presented for n = 4 independent experiments. p values were assessed by one-way ANOVA with Tukey’s multiple comparisons test. Source data are provided as a Source Data file.

    Techniques Used: Infection, Western Blot, Marker, Isolation, Cell Culture, Gradient Centrifugation, Labeling, Flow Cytometry

    EVs released by cells infected with either EMCV-Wt or EMCV-L Zn were isolated and EV-protein composition was analyzed by LC-MS/MS. a Venn diagram depicting the number of unique and overlapping host proteins identified in at least 2 out of 3 replicate preparations of EMCV-Wt and EMCV-L Zn EVs. b – e Functional enrichment analysis for the 44 unique proteins in EMCV-Wt EVs was combined with an evaluation of protein–protein interactions using the STRING database. b , d Functional annotations are listed for the GO domains cellular component ( b ) and biological process ( d ). Bars depict the fold enrichment for the indicated GO-terms compared to the genome, with concomitant p values as assessed by one-tailed Fisher’s exact test with Bonferroni correction for multiple testing. c , e Proteins in interactome networks are indicated by their gene name and thickness of the connecting lines correlates with the strength of data support for interaction. Color-coding of individual proteins corresponds to their association with GO-terms that are enriched >10-fold compared to the genome for cellular component ( c ) or biological process ( e ). f Ultracentrifugation pellets (100 K) of cell culture supernatants from an equal number of mock, EMCV-Wt, or EMCV-L Zn infected cells were analyzed by western blotting for the presence of extracellular LC3. g EMCV-Wt samples from ( f ) were treated with proteinase K in the absence or presence of 0.2% triton and analyzed by western blotting for the presence of LC3. LC3I PC and LC3II PC are positive control samples for western blot detection of LC3I and LC3II, respectively. h EMCV-Wt samples from ( f ) were floated into a sucrose density gradient. Individual gradient fractions were analyzed for the presence of LC3 and the EV markers CD9 and flotillin by western blotting. Representative images of n = 3 independent experiments are shown for ( f , g ) and n = 2 independent experiments for ( h ). Source data are provided as a Source Data file.
    Figure Legend Snippet: EVs released by cells infected with either EMCV-Wt or EMCV-L Zn were isolated and EV-protein composition was analyzed by LC-MS/MS. a Venn diagram depicting the number of unique and overlapping host proteins identified in at least 2 out of 3 replicate preparations of EMCV-Wt and EMCV-L Zn EVs. b – e Functional enrichment analysis for the 44 unique proteins in EMCV-Wt EVs was combined with an evaluation of protein–protein interactions using the STRING database. b , d Functional annotations are listed for the GO domains cellular component ( b ) and biological process ( d ). Bars depict the fold enrichment for the indicated GO-terms compared to the genome, with concomitant p values as assessed by one-tailed Fisher’s exact test with Bonferroni correction for multiple testing. c , e Proteins in interactome networks are indicated by their gene name and thickness of the connecting lines correlates with the strength of data support for interaction. Color-coding of individual proteins corresponds to their association with GO-terms that are enriched >10-fold compared to the genome for cellular component ( c ) or biological process ( e ). f Ultracentrifugation pellets (100 K) of cell culture supernatants from an equal number of mock, EMCV-Wt, or EMCV-L Zn infected cells were analyzed by western blotting for the presence of extracellular LC3. g EMCV-Wt samples from ( f ) were treated with proteinase K in the absence or presence of 0.2% triton and analyzed by western blotting for the presence of LC3. LC3I PC and LC3II PC are positive control samples for western blot detection of LC3I and LC3II, respectively. h EMCV-Wt samples from ( f ) were floated into a sucrose density gradient. Individual gradient fractions were analyzed for the presence of LC3 and the EV markers CD9 and flotillin by western blotting. Representative images of n = 3 independent experiments are shown for ( f , g ) and n = 2 independent experiments for ( h ). Source data are provided as a Source Data file.

    Techniques Used: Infection, Isolation, Liquid Chromatography with Mass Spectroscopy, Functional Assay, Protein-Protein interactions, One-tailed Test, Cell Culture, Western Blot, Positive Control

    a Mock-infected cells and cells infected with EMCV-Wt or EMCV-L Zn were harvested 8 h p.i. Whole-cell lysates were analyzed for conversion of LC3I to LC3II by western blotting and the LC3II:LC3I ratios were calculated relative to mock-infected cells. *Indicates a detected LC3 band with intermediate size. Actin was included as a loading control and EMCV-3D to confirm infection. Depicted are representative blots and the mean ± SD of n = 4 independent experiments. * p = 0.0341 (bottom), p = 0.0257 (top) as determined by a two-tailed one-sample t -test. # p = 0.0437 using a two-tailed t -test. b Schematic overview of the mCherry-EGFP-LC3 autophagy reporter system. Using spot detection on LC3 reporter cells imaged by confocal microscopy, the accumulation of LC3 in autophagosomal vs. autolysosomal compartments can be monitored. Whereas autophagosomes appear as mCherry+ EGFP+ LC3+ puncta, autolysosomes are detected as mCherry+ EGFP− LC3+ puncta due to a loss of EGFP fluorescence in the acidic environment of the autolysosome lumen. c LC3 reporter cells were infected with EMCV-Wt or EMCV-L Zn for the indicated time or treated with bafA1 for 6 h and imaged for EGFP and mCherry fluorescence using confocal microscopy. Some EGFP+ compartments seem to lack mCherry signal, but this is likely due to the lower detection efficiency of mCherry versus EGFP. Bar graphs display a quantification of the ratio between the total surface area of EGFP and mCherry positive puncta as a measure for the ratio between the autophagosomes and autolysosomes present in the cells. Indicated are mean values ± SEM of ≥7 separate images with 2–5 cells each from a representative of n = 3 individual experiments. ** p = 0.0083, *** p = 0.0001, **** p < 0.0001 as assessed by one-way ANOVA with Dunnett’s multiple comparison test. Scale bar = 20 µm. ( d ) Infected cells were stained with 50 nM lysotracker and compared to mock-infected cells or bafA1 treated controls 6 h p.i. using live-cell confocal imaging. Depicted are representative images showing lysotracker fluorescence staining. Bar graphs display the average cellular staining intensity relative to uninfected controls. Indicated are mean values ± SD of five independent experiments. Scale bar = 30 µm. ** p = 0.0012, as assessed by a one-sample t -test. ns, p = 0.1400 as assessed by an unpaired, two-tailed t -test. Source data are provided as a Source Data file.
    Figure Legend Snippet: a Mock-infected cells and cells infected with EMCV-Wt or EMCV-L Zn were harvested 8 h p.i. Whole-cell lysates were analyzed for conversion of LC3I to LC3II by western blotting and the LC3II:LC3I ratios were calculated relative to mock-infected cells. *Indicates a detected LC3 band with intermediate size. Actin was included as a loading control and EMCV-3D to confirm infection. Depicted are representative blots and the mean ± SD of n = 4 independent experiments. * p = 0.0341 (bottom), p = 0.0257 (top) as determined by a two-tailed one-sample t -test. # p = 0.0437 using a two-tailed t -test. b Schematic overview of the mCherry-EGFP-LC3 autophagy reporter system. Using spot detection on LC3 reporter cells imaged by confocal microscopy, the accumulation of LC3 in autophagosomal vs. autolysosomal compartments can be monitored. Whereas autophagosomes appear as mCherry+ EGFP+ LC3+ puncta, autolysosomes are detected as mCherry+ EGFP− LC3+ puncta due to a loss of EGFP fluorescence in the acidic environment of the autolysosome lumen. c LC3 reporter cells were infected with EMCV-Wt or EMCV-L Zn for the indicated time or treated with bafA1 for 6 h and imaged for EGFP and mCherry fluorescence using confocal microscopy. Some EGFP+ compartments seem to lack mCherry signal, but this is likely due to the lower detection efficiency of mCherry versus EGFP. Bar graphs display a quantification of the ratio between the total surface area of EGFP and mCherry positive puncta as a measure for the ratio between the autophagosomes and autolysosomes present in the cells. Indicated are mean values ± SEM of ≥7 separate images with 2–5 cells each from a representative of n = 3 individual experiments. ** p = 0.0083, *** p = 0.0001, **** p < 0.0001 as assessed by one-way ANOVA with Dunnett’s multiple comparison test. Scale bar = 20 µm. ( d ) Infected cells were stained with 50 nM lysotracker and compared to mock-infected cells or bafA1 treated controls 6 h p.i. using live-cell confocal imaging. Depicted are representative images showing lysotracker fluorescence staining. Bar graphs display the average cellular staining intensity relative to uninfected controls. Indicated are mean values ± SD of five independent experiments. Scale bar = 30 µm. ** p = 0.0012, as assessed by a one-sample t -test. ns, p = 0.1400 as assessed by an unpaired, two-tailed t -test. Source data are provided as a Source Data file.

    Techniques Used: Infection, Western Blot, Control, Two Tailed Test, Confocal Microscopy, Fluorescence, Comparison, Staining, Imaging

    EMCV-Wt infected cells were treated with 200 nM rapamycin 1 h p.i. onwards to increase autophagic flux and enhance autolysosome formation. a Representative confocal microscopy images of infected mCherry-EGFP-LC3 reporter cells 6 h p.i. Bar graphs display the ratio between the total surface area of EGFP and mCherry positive puncta, that correspond to autophagosomes (EGFP+ mCherry+) and autolysosomes (EGFP−mCherry+). Indicated are mean values ± SEM of ≥7 separate images with 2–5 cells each from a representative of n = 3 individual experiments. *** p = 0.0008, * p = 0.0434 as assessed by one-way ANOVA with Tukey’s multiple comparison test. Scale bar = 10 μm. b Western blot analysis of LC3 release in ultracentrifugation pellets harvested 8 h p.i. from cell supernatants of an equal number of cells. Depicted is a representative image of n = 3 independent experiments. LC3I PC and LC3II PC are positive control samples for western blot detection of LC3I and LC3II, respectively. c , d 10 K and 100 K EVs were isolated and purified using density gradients. Depicted is the total amount of EV-associated infectivity ( c ) and its distribution over 100 K vs. 10 K EVs ( d ) (mean ± SD of n = 3 independent experiments) as determined by end-point dilution assay. *** p = 0.0009, ns p = 0.6599 as assessed by an unpaired, two-tailed t -test. Source data are provided as a Source Data file.
    Figure Legend Snippet: EMCV-Wt infected cells were treated with 200 nM rapamycin 1 h p.i. onwards to increase autophagic flux and enhance autolysosome formation. a Representative confocal microscopy images of infected mCherry-EGFP-LC3 reporter cells 6 h p.i. Bar graphs display the ratio between the total surface area of EGFP and mCherry positive puncta, that correspond to autophagosomes (EGFP+ mCherry+) and autolysosomes (EGFP−mCherry+). Indicated are mean values ± SEM of ≥7 separate images with 2–5 cells each from a representative of n = 3 individual experiments. *** p = 0.0008, * p = 0.0434 as assessed by one-way ANOVA with Tukey’s multiple comparison test. Scale bar = 10 μm. b Western blot analysis of LC3 release in ultracentrifugation pellets harvested 8 h p.i. from cell supernatants of an equal number of cells. Depicted is a representative image of n = 3 independent experiments. LC3I PC and LC3II PC are positive control samples for western blot detection of LC3I and LC3II, respectively. c , d 10 K and 100 K EVs were isolated and purified using density gradients. Depicted is the total amount of EV-associated infectivity ( c ) and its distribution over 100 K vs. 10 K EVs ( d ) (mean ± SD of n = 3 independent experiments) as determined by end-point dilution assay. *** p = 0.0009, ns p = 0.6599 as assessed by an unpaired, two-tailed t -test. Source data are provided as a Source Data file.

    Techniques Used: Infection, Confocal Microscopy, Comparison, Western Blot, Positive Control, Isolation, Purification, End-point Dilution Assay, Two Tailed Test

    a EMCV-L Zn infected cells were treated with 500 nM apilimod for 16 h prior to infection or 200 nM BafA1 1 h p.i. onwards. EV-containing 100,000× g ultracentrifugation pellets were isolated from supernatants of an equal number of cells at 8 h p.i. and analyzed by western blot for the presence of extracellular released LC3. Depicted is a representative image of n = 2 independent experiments. LC3I PC and LC3II PC are positive control samples for western blot detection of LC3I and LC3II, respectively. b 100 K EVs were labeled with CFSE, purified by density gradient centrifugation, and analyzed by high-resolution flow cytometry. Bars indicate the mean fold increase in EV release relative to untreated controls ±SD from n = 3 (BafA1) or n = 4 (apilimod) independent experiments. ** p = 0.0064, ns (left) p = 0.1148 as assessed by a two-tailed one-sample t -test, or two-tailed t -test for ns (right) p = 0.9936. c , d Depicted is the mean fold increase in EV-enclosed infectivity ( c ) and intracellular virus titers ( d ) relative to untreated controls ±SD corresponding to the samples in ( b ) as determined by end-point dilution assay. For c * p = 0.0210, ns p = 0.1464, for d * p = 0.0285, ns p = 0.4226, as assessed by a two-tailed one-sample t -test. Source data are provided as a Source Data file.
    Figure Legend Snippet: a EMCV-L Zn infected cells were treated with 500 nM apilimod for 16 h prior to infection or 200 nM BafA1 1 h p.i. onwards. EV-containing 100,000× g ultracentrifugation pellets were isolated from supernatants of an equal number of cells at 8 h p.i. and analyzed by western blot for the presence of extracellular released LC3. Depicted is a representative image of n = 2 independent experiments. LC3I PC and LC3II PC are positive control samples for western blot detection of LC3I and LC3II, respectively. b 100 K EVs were labeled with CFSE, purified by density gradient centrifugation, and analyzed by high-resolution flow cytometry. Bars indicate the mean fold increase in EV release relative to untreated controls ±SD from n = 3 (BafA1) or n = 4 (apilimod) independent experiments. ** p = 0.0064, ns (left) p = 0.1148 as assessed by a two-tailed one-sample t -test, or two-tailed t -test for ns (right) p = 0.9936. c , d Depicted is the mean fold increase in EV-enclosed infectivity ( c ) and intracellular virus titers ( d ) relative to untreated controls ±SD corresponding to the samples in ( b ) as determined by end-point dilution assay. For c * p = 0.0210, ns p = 0.1464, for d * p = 0.0285, ns p = 0.4226, as assessed by a two-tailed one-sample t -test. Source data are provided as a Source Data file.

    Techniques Used: Infection, Isolation, Western Blot, Positive Control, Labeling, Purification, Gradient Centrifugation, Flow Cytometry, Two Tailed Test, Virus, End-point Dilution Assay



    Similar Products

    10 1 3d interactive microscopy visualization software  (Oxford Instruments)
    99
    Oxford Instruments 10 1 3d interactive microscopy visualization software
    10 1 3d Interactive Microscopy Visualization Software, supplied by Oxford Instruments, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/3d+interactive+microscopy+visualization+software/10__1038_slash_s44321___025___00275___7-246-16-15?v=Oxford+Instruments
    Average 99 stars, based on 1 article reviews
    10 1 3d interactive microscopy visualization software - by Bioz Stars, 2026-08
    99/100 stars
    		  Buy from Supplier
    ma imaris 3d interactive microscopy visualization software oxford instruments  (Oxford Instruments)
    99
    Oxford Instruments ma imaris 3d interactive microscopy visualization software oxford instruments
    Ma Imaris 3d Interactive Microscopy Visualization Software Oxford Instruments, supplied by Oxford Instruments, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/3d+interactive+microscopy+visualization+software/10__1038_slash_s44321___025___00275___7-206-137-138?v=Oxford+Instruments
    Average 99 stars, based on 1 article reviews
    ma imaris 3d interactive microscopy visualization software oxford instruments - by Bioz Stars, 2026-08
    99/100 stars
    		  Buy from Supplier
    3d interactive microscopy visualization software  (Oxford Instruments)
    99
    Oxford Instruments 3d interactive microscopy visualization software
    ( A ) <t>3D</t> surface projection of IHCs and OHCs from the cochlear 32 kHz region of Clic5 +/− , Clic5 −/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with a CLIC5 (red) and actin (gray). ( B ) Representative confocal images of IHCs from the apical turn of Clic5 +/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with a CLIC5 (red), actin (gray), and FLAG tag (green). ( C ) Representative confocal images of IHCs and OHCs from the cochlear 8 kHz region of Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with actin. ( D ) Stereocilia length measurements of IHC at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( E ) Quantification of OHC survival at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( F ) Quantification of IHC survival at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( G ) High-magnification scanning electron <t>microscopy</t> images of outer and inner hair bundles from the cochlea middle-turn of the Clic5 −/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks. ( H ) Representative images of IHCs and OHCs at 12 weeks at different regions of the cochlea of Clic5 −/ − injected with scAAV. Clic5 . ( I ) ABR thresholds at 4 weeks of Clic5 +/− ( n = 11), Clic5 −/− ( n = 10), and Clic5 −/− injected with scAAV. Clic5 ( n = 10). ( J ) ABR thresholds at 8 weeks of Clic5 +/− ( n = 11), Clic5 −/− ( n = 11), and Clic5 −/− injected with scAVV. Clic5 (n = 7). ( K ) ABR thresholds at 12 weeks of Clic5 +/− ( n = 10), Clic5 −/− ( n = 10), and Clic5 −/− injected with scAAV. Clic5 ( n = 7). ( L ) DPOAE thresholds at 4 weeks of Clic5 +/− ( n = 12), Clic5 −/ − ( n = 12), and Clic5 −/− injected with scAAV. Clic5 ( n = 10). ( M ) ABR thresholds at 3-time points of Clic5 −/− injected with scAAV. Clic5: 4 weeks ( n = 10), 8 weeks ( n = 7), and 12 weeks ( n = 7). ( N ) Freezing behavior duration in a fear conditioning assay at 12 weeks of Clic5 +/− ( n = 14), Clic5 − /− ( n = 14), and Clic5 −/− injected with scAAV. Clic5 ( n = 6). ( O ) Expression rates of scAAV. Clic5 across the cochlea as a function of viral titer, n = 3 for each group. ( P ) ABR thresholds at 4 weeks of Clic5 −/ − injected with scAAV .Clic5 at different viral doses: 1.52 × 10¹³ gc/ml ( n = 10), 1.52 × 10 12 gc/ml ( n = 3) and 1.52 × 10 11 gc/ml ( n = 3). Data information: Statistical tests were two-way ANOVA with Holm–Sidak correction for multiple comparisons for ( D – F , I – N , P ), and one-way ANOVA followed by Tukey correction for multiple comparisons for ( O ). Plots show mean ± SD. ns not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 (Exact P values are provided in Appendix Table S ). Scale bars = 10 μm for ( A , C , H ), 2 μm for ( B ), 0.5 μm for OHC ( G ), and 2 μm for IHC ( G ). .
    3d Interactive Microscopy Visualization Software, supplied by Oxford Instruments, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/3d+interactive+microscopy+visualization+software/pmc12423326-40-1-0?v=Oxford+Instruments
    Average 99 stars, based on 1 article reviews
    3d interactive microscopy visualization software - by Bioz Stars, 2026-08
    99/100 stars
    		  Buy from Supplier

    Image Search Results


    ( A ) 3D surface projection of IHCs and OHCs from the cochlear 32 kHz region of Clic5 +/− , Clic5 −/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with a CLIC5 (red) and actin (gray). ( B ) Representative confocal images of IHCs from the apical turn of Clic5 +/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with a CLIC5 (red), actin (gray), and FLAG tag (green). ( C ) Representative confocal images of IHCs and OHCs from the cochlear 8 kHz region of Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with actin. ( D ) Stereocilia length measurements of IHC at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( E ) Quantification of OHC survival at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( F ) Quantification of IHC survival at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( G ) High-magnification scanning electron microscopy images of outer and inner hair bundles from the cochlea middle-turn of the Clic5 −/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks. ( H ) Representative images of IHCs and OHCs at 12 weeks at different regions of the cochlea of Clic5 −/ − injected with scAAV. Clic5 . ( I ) ABR thresholds at 4 weeks of Clic5 +/− ( n = 11), Clic5 −/− ( n = 10), and Clic5 −/− injected with scAAV. Clic5 ( n = 10). ( J ) ABR thresholds at 8 weeks of Clic5 +/− ( n = 11), Clic5 −/− ( n = 11), and Clic5 −/− injected with scAVV. Clic5 (n = 7). ( K ) ABR thresholds at 12 weeks of Clic5 +/− ( n = 10), Clic5 −/− ( n = 10), and Clic5 −/− injected with scAAV. Clic5 ( n = 7). ( L ) DPOAE thresholds at 4 weeks of Clic5 +/− ( n = 12), Clic5 −/ − ( n = 12), and Clic5 −/− injected with scAAV. Clic5 ( n = 10). ( M ) ABR thresholds at 3-time points of Clic5 −/− injected with scAAV. Clic5: 4 weeks ( n = 10), 8 weeks ( n = 7), and 12 weeks ( n = 7). ( N ) Freezing behavior duration in a fear conditioning assay at 12 weeks of Clic5 +/− ( n = 14), Clic5 − /− ( n = 14), and Clic5 −/− injected with scAAV. Clic5 ( n = 6). ( O ) Expression rates of scAAV. Clic5 across the cochlea as a function of viral titer, n = 3 for each group. ( P ) ABR thresholds at 4 weeks of Clic5 −/ − injected with scAAV .Clic5 at different viral doses: 1.52 × 10¹³ gc/ml ( n = 10), 1.52 × 10 12 gc/ml ( n = 3) and 1.52 × 10 11 gc/ml ( n = 3). Data information: Statistical tests were two-way ANOVA with Holm–Sidak correction for multiple comparisons for ( D – F , I – N , P ), and one-way ANOVA followed by Tukey correction for multiple comparisons for ( O ). Plots show mean ± SD. ns not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 (Exact P values are provided in Appendix Table S ). Scale bars = 10 μm for ( A , C , H ), 2 μm for ( B ), 0.5 μm for OHC ( G ), and 2 μm for IHC ( G ). .

    Journal: EMBO Molecular Medicine

    Article Title: AAV gene therapy rescues hearing and balance in a model of CLIC5 deafness

    doi: 10.1038/s44321-025-00275-7

    Figure Lengend Snippet: ( A ) 3D surface projection of IHCs and OHCs from the cochlear 32 kHz region of Clic5 +/− , Clic5 −/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with a CLIC5 (red) and actin (gray). ( B ) Representative confocal images of IHCs from the apical turn of Clic5 +/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with a CLIC5 (red), actin (gray), and FLAG tag (green). ( C ) Representative confocal images of IHCs and OHCs from the cochlear 8 kHz region of Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 at 12 weeks, stained with actin. ( D ) Stereocilia length measurements of IHC at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( E ) Quantification of OHC survival at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( F ) Quantification of IHC survival at different regions of the cochlea, n = 3 for Clic5 +/− , Clic5 −/− , and Clic5 −/− injected with scAAV. Clic5 . ( G ) High-magnification scanning electron microscopy images of outer and inner hair bundles from the cochlea middle-turn of the Clic5 −/− and Clic5 −/− injected with scAAV. Clic5 at 12 weeks. ( H ) Representative images of IHCs and OHCs at 12 weeks at different regions of the cochlea of Clic5 −/ − injected with scAAV. Clic5 . ( I ) ABR thresholds at 4 weeks of Clic5 +/− ( n = 11), Clic5 −/− ( n = 10), and Clic5 −/− injected with scAAV. Clic5 ( n = 10). ( J ) ABR thresholds at 8 weeks of Clic5 +/− ( n = 11), Clic5 −/− ( n = 11), and Clic5 −/− injected with scAVV. Clic5 (n = 7). ( K ) ABR thresholds at 12 weeks of Clic5 +/− ( n = 10), Clic5 −/− ( n = 10), and Clic5 −/− injected with scAAV. Clic5 ( n = 7). ( L ) DPOAE thresholds at 4 weeks of Clic5 +/− ( n = 12), Clic5 −/ − ( n = 12), and Clic5 −/− injected with scAAV. Clic5 ( n = 10). ( M ) ABR thresholds at 3-time points of Clic5 −/− injected with scAAV. Clic5: 4 weeks ( n = 10), 8 weeks ( n = 7), and 12 weeks ( n = 7). ( N ) Freezing behavior duration in a fear conditioning assay at 12 weeks of Clic5 +/− ( n = 14), Clic5 − /− ( n = 14), and Clic5 −/− injected with scAAV. Clic5 ( n = 6). ( O ) Expression rates of scAAV. Clic5 across the cochlea as a function of viral titer, n = 3 for each group. ( P ) ABR thresholds at 4 weeks of Clic5 −/ − injected with scAAV .Clic5 at different viral doses: 1.52 × 10¹³ gc/ml ( n = 10), 1.52 × 10 12 gc/ml ( n = 3) and 1.52 × 10 11 gc/ml ( n = 3). Data information: Statistical tests were two-way ANOVA with Holm–Sidak correction for multiple comparisons for ( D – F , I – N , P ), and one-way ANOVA followed by Tukey correction for multiple comparisons for ( O ). Plots show mean ± SD. ns not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 (Exact P values are provided in Appendix Table S ). Scale bars = 10 μm for ( A , C , H ), 2 μm for ( B ), 0.5 μm for OHC ( G ), and 2 μm for IHC ( G ). .

    Article Snippet: Imaris 3D Interactive Microscopy Visualization software , Oxford Instruments . , version 10.1.

    Techniques: Injection, Staining, FLAG-tag, Electron Microscopy, Expressing