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  • 95
    Millipore discovery hs f5 column
    Discovery Hs F5 Column, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/discovery hs f5 column/product/Millipore
    Average 95 stars, based on 34 article reviews
    Price from $9.99 to $1999.99
    discovery hs f5 column - by Bioz Stars, 2020-09
    95/100 stars
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    91
    Polyplus Transfection f5 peptide
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    F5 Peptide, supplied by Polyplus Transfection, used in various techniques. Bioz Stars score: 91/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/f5 peptide/product/Polyplus Transfection
    Average 91 stars, based on 68 article reviews
    Price from $9.99 to $1999.99
    f5 peptide - by Bioz Stars, 2020-09
    91/100 stars
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    90
    Phenomenex kinetex f5 column
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Kinetex F5 Column, supplied by Phenomenex, used in various techniques. Bioz Stars score: 90/100, based on 76 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kinetex f5 column/product/Phenomenex
    Average 90 stars, based on 76 article reviews
    Price from $9.99 to $1999.99
    kinetex f5 column - by Bioz Stars, 2020-09
    90/100 stars
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    91
    Phenomenex kinetex f5
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Kinetex F5, supplied by Phenomenex, used in various techniques. Bioz Stars score: 91/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kinetex f5/product/Phenomenex
    Average 91 stars, based on 55 article reviews
    Price from $9.99 to $1999.99
    kinetex f5 - by Bioz Stars, 2020-09
    91/100 stars
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    90
    Supelco ascentis express f5 column
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Ascentis Express F5 Column, supplied by Supelco, used in various techniques. Bioz Stars score: 90/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ascentis express f5 column/product/Supelco
    Average 90 stars, based on 35 article reviews
    Price from $9.99 to $1999.99
    ascentis express f5 column - by Bioz Stars, 2020-09
    90/100 stars
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    94
    Arbor Assays glutathione fluorescent detection kit
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Glutathione Fluorescent Detection Kit, supplied by Arbor Assays, used in various techniques. Bioz Stars score: 94/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/glutathione fluorescent detection kit/product/Arbor Assays
    Average 94 stars, based on 39 article reviews
    Price from $9.99 to $1999.99
    glutathione fluorescent detection kit - by Bioz Stars, 2020-09
    94/100 stars
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    88
    Supelco discovery hs f5 column
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Discovery Hs F5 Column, supplied by Supelco, used in various techniques. Bioz Stars score: 88/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/discovery hs f5 column/product/Supelco
    Average 88 stars, based on 43 article reviews
    Price from $9.99 to $1999.99
    discovery hs f5 column - by Bioz Stars, 2020-09
    88/100 stars
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    91
    Santa Cruz Biotechnology p21 f 5
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    P21 F 5, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 150 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p21 f 5/product/Santa Cruz Biotechnology
    Average 91 stars, based on 150 article reviews
    Price from $9.99 to $1999.99
    p21 f 5 - by Bioz Stars, 2020-09
    91/100 stars
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    88
    Santa Cruz Biotechnology anti p21 f 5
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Anti P21 F 5, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p21 f 5/product/Santa Cruz Biotechnology
    Average 88 stars, based on 40 article reviews
    Price from $9.99 to $1999.99
    anti p21 f 5 - by Bioz Stars, 2020-09
    88/100 stars
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    88
    Supelco discovery hs f5 3 hplc column
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Discovery Hs F5 3 Hplc Column, supplied by Supelco, used in various techniques. Bioz Stars score: 88/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/discovery hs f5 3 hplc column/product/Supelco
    Average 88 stars, based on 27 article reviews
    Price from $9.99 to $1999.99
    discovery hs f5 3 hplc column - by Bioz Stars, 2020-09
    88/100 stars
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    93
    Thermo Fisher microplate reader filtermax f5
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Microplate Reader Filtermax F5, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/microplate reader filtermax f5/product/Thermo Fisher
    Average 93 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    microplate reader filtermax f5 - by Bioz Stars, 2020-09
    93/100 stars
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    93
    Millipore ascentis express f5
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Ascentis Express F5, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ascentis express f5/product/Millipore
    Average 93 stars, based on 20 article reviews
    Price from $9.99 to $1999.99
    ascentis express f5 - by Bioz Stars, 2020-09
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    94
    R&D Systems recombinant human fgf
    Overexpression of <t>F5-peptide</t> in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P
    Recombinant Human Fgf, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 57 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human fgf/product/R&D Systems
    Average 94 stars, based on 57 article reviews
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    recombinant human fgf - by Bioz Stars, 2020-09
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    89
    Supelco discovery hs f5
    Chromatograms of 3-ADON/15-ADON, FB 2 /FB 3 , and FA 2 /FA 3  using each PFP column. ( a ) Mastro PFP; ( b ) ACQUITY UPLC CSH Fluoro-Phenyl; ( c ) Discovery HS F5. The analytical sample was 200 μg/L standards in neat solvent. Extraction mass window was ±5 ppm. Abbreviations; 3-ADON, 3-acetyl deoxynivalenol; 15-ADON, 15-acetyl deoxynivalenol; FB 2 , fumonisin B 2 ; FB 3 , fumonisin B 3 ; FA 2 , fumonisin A 2 ; FA 3 , fumonisin A 3 .
    Discovery Hs F5, supplied by Supelco, used in various techniques. Bioz Stars score: 89/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/discovery hs f5/product/Supelco
    Average 89 stars, based on 53 article reviews
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    discovery hs f5 - by Bioz Stars, 2020-09
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    86
    Supelco discovery hs f5 3
    Chromatograms of 3-ADON/15-ADON, FB 2 /FB 3 , and FA 2 /FA 3  using each PFP column. ( a ) Mastro PFP; ( b ) ACQUITY UPLC CSH Fluoro-Phenyl; ( c ) Discovery HS F5. The analytical sample was 200 μg/L standards in neat solvent. Extraction mass window was ±5 ppm. Abbreviations; 3-ADON, 3-acetyl deoxynivalenol; 15-ADON, 15-acetyl deoxynivalenol; FB 2 , fumonisin B 2 ; FB 3 , fumonisin B 3 ; FA 2 , fumonisin A 2 ; FA 3 , fumonisin A 3 .
    Discovery Hs F5 3, supplied by Supelco, used in various techniques. Bioz Stars score: 86/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/discovery hs f5 3/product/Supelco
    Average 86 stars, based on 22 article reviews
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    discovery hs f5 3 - by Bioz Stars, 2020-09
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    92
    NETZSCH sta 449 f5 jupiter
    Chromatograms of 3-ADON/15-ADON, FB 2 /FB 3 , and FA 2 /FA 3  using each PFP column. ( a ) Mastro PFP; ( b ) ACQUITY UPLC CSH Fluoro-Phenyl; ( c ) Discovery HS F5. The analytical sample was 200 μg/L standards in neat solvent. Extraction mass window was ±5 ppm. Abbreviations; 3-ADON, 3-acetyl deoxynivalenol; 15-ADON, 15-acetyl deoxynivalenol; FB 2 , fumonisin B 2 ; FB 3 , fumonisin B 3 ; FA 2 , fumonisin A 2 ; FA 3 , fumonisin A 3 .
    Sta 449 F5 Jupiter, supplied by NETZSCH, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sta 449 f5 jupiter/product/NETZSCH
    Average 92 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    sta 449 f5 jupiter - by Bioz Stars, 2020-09
    92/100 stars
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    92
    R&D Systems recombinant human fgf 5 protein
    Chromatograms of 3-ADON/15-ADON, FB 2 /FB 3 , and FA 2 /FA 3  using each PFP column. ( a ) Mastro PFP; ( b ) ACQUITY UPLC CSH Fluoro-Phenyl; ( c ) Discovery HS F5. The analytical sample was 200 μg/L standards in neat solvent. Extraction mass window was ±5 ppm. Abbreviations; 3-ADON, 3-acetyl deoxynivalenol; 15-ADON, 15-acetyl deoxynivalenol; FB 2 , fumonisin B 2 ; FB 3 , fumonisin B 3 ; FA 2 , fumonisin A 2 ; FA 3 , fumonisin A 3 .
    Recombinant Human Fgf 5 Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human fgf 5 protein/product/R&D Systems
    Average 92 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    recombinant human fgf 5 protein - by Bioz Stars, 2020-09
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    91
    Olympus cell f 5 1
    Chromatograms of 3-ADON/15-ADON, FB 2 /FB 3 , and FA 2 /FA 3  using each PFP column. ( a ) Mastro PFP; ( b ) ACQUITY UPLC CSH Fluoro-Phenyl; ( c ) Discovery HS F5. The analytical sample was 200 μg/L standards in neat solvent. Extraction mass window was ±5 ppm. Abbreviations; 3-ADON, 3-acetyl deoxynivalenol; 15-ADON, 15-acetyl deoxynivalenol; FB 2 , fumonisin B 2 ; FB 3 , fumonisin B 3 ; FA 2 , fumonisin A 2 ; FA 3 , fumonisin A 3 .
    Cell F 5 1, supplied by Olympus, used in various techniques. Bioz Stars score: 91/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cell f 5 1/product/Olympus
    Average 91 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
    cell f 5 1 - by Bioz Stars, 2020-09
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    Image Search Results


    Overexpression of F5-peptide in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P

    Journal: Oncotarget

    Article Title: F5-peptide induces aspermatogenesis by disrupting organization of actin- and microtubule-based cytoskeletons in the testis

    doi: 10.18632/oncotarget.11887

    Figure Lengend Snippet: Overexpression of F5-peptide in the test is perturbs BTB function in vivo BTB integrity assay was performed to assess the ability of an intact BTB to block the diffusion of a small molecule biotin (EZ-Link Sulfo-NHS-LC-Biotin, Mr 556.59) across the BTB which biotinylated proteins in the adluminal compartment. In normal rat testes and testes transfected with pCI-neo alone (control), the functional BTB blocked biotin reagent from entering the adluminal compartment so that only proteins at the BTB and the interstitial space were labeled. Biotinylated proteins were subsequently visualized using frozen sections of the testis and stained with Alexa Fluor 488-streptavidin (green fluorescence). Distance traveled by biotin beyond the basement membrane/tunica propria was annotated by a yellow bracket. In control testes, biotin failed to travel beyond the basement membrane/tunica propria which was annotated by a dashed white line. In testes from rats treated with CdCl 2 (positive control) or transfected with pCI-neo/F5, biotin penetrated well into the adluminal compartment, illustrating that F5-peptide perturbed the BTB integrity. Lower magnified images of ~3–4 tubules were shown in insets and the enlarged image of a typical tubule was shown in the micrograph. Scale bars, 50 μm, and 200 μm in insets, which applies to corresponding micrographs and/or insets. Histograms show the semi-quantitative data by comparing the distance of biotin traveled into the epithelium (D Biotin ) vs. the radius of seminiferous tubule (D Radius ). For oblique sections, the radius of the tubule was obtained by averaging the longest and shortest distance from the basement membrane. Each bar is a mean ± SD of ~50 tubules that were randomly selected and scored from testes of 6 rats with a total of 300 randomly selected tubules. ** P

    Article Snippet: It was noted that overexpression of F5-peptide reduced the expression of F-actin at the BTB (Figure ).

    Techniques: Over Expression, In Vivo, Integrity Assay, Blocking Assay, Diffusion-based Assay, Transfection, Functional Assay, Labeling, Staining, Fluorescence, Positive Control

    Overexpression of F5-peptide perturbs MT organization in the seminiferous epithelium of adult rat testes in vivo Rat testes were transfected with pCI-neo/F5 vs. pCI-neo empty vector (control) using regimens ( n = 9 rats) shown in Figure 3A . Testes were used for immunohistochemistry to visualize the distribution of α-tubulin, the building block of microtubules (MTs) in the seminiferous epithelium. ( A ) In normal testes, MTs appeared as track-like structures were found longitudinally across the epithelium to provide the tracks to support the transport of organelles (e.g., phagosomes, endocytic vesicles) and also spermatids in virtually all stages of the epithelial cycle. Following overexpression of F5-peptide, on day 2 or day 5 after completion of transfection, tracks were grossly affected. They no longer distinctively found across the epithelium, but truncated and some laid across the epithelium in parallel to the tunica propria. Moreover, MTs were also found to engulf round spermatids, becoming the precursors of giant multinucleated round spermatids, destined to be degenerated. The last micrograph on the right of the top panel is the negative control (a stage VIII tubule) in which the primary antibody was substituted with the mouse IgG. Scale bar, 30 μm, which applies to other micrographs. ( B ) Changes in the organization of EB1, a +TIP protein known to bind to MTs, helping to stabilize MTs, were also noted in testes following overexpression of F5-peptide. Similar to α-tubulin, EB1 appeared as track-like structures across the epithelium, but overexpression of F5-peptide led to either considerably loss of EB1 in the epithelium, and it no longer laid across the epithelium longitudinally, but truncated and also wrapped around groups of round spermatids destined to become giant multinucleated round spermatids for eventual degeneration. The last micrograph on the right of the top panel is the negative control (a stage V tubule) in which the primary antibody was substituted with the mouse IgG. Scale bar, 30 μm, which applies to other micrographs.

    Journal: Oncotarget

    Article Title: F5-peptide induces aspermatogenesis by disrupting organization of actin- and microtubule-based cytoskeletons in the testis

    doi: 10.18632/oncotarget.11887

    Figure Lengend Snippet: Overexpression of F5-peptide perturbs MT organization in the seminiferous epithelium of adult rat testes in vivo Rat testes were transfected with pCI-neo/F5 vs. pCI-neo empty vector (control) using regimens ( n = 9 rats) shown in Figure 3A . Testes were used for immunohistochemistry to visualize the distribution of α-tubulin, the building block of microtubules (MTs) in the seminiferous epithelium. ( A ) In normal testes, MTs appeared as track-like structures were found longitudinally across the epithelium to provide the tracks to support the transport of organelles (e.g., phagosomes, endocytic vesicles) and also spermatids in virtually all stages of the epithelial cycle. Following overexpression of F5-peptide, on day 2 or day 5 after completion of transfection, tracks were grossly affected. They no longer distinctively found across the epithelium, but truncated and some laid across the epithelium in parallel to the tunica propria. Moreover, MTs were also found to engulf round spermatids, becoming the precursors of giant multinucleated round spermatids, destined to be degenerated. The last micrograph on the right of the top panel is the negative control (a stage VIII tubule) in which the primary antibody was substituted with the mouse IgG. Scale bar, 30 μm, which applies to other micrographs. ( B ) Changes in the organization of EB1, a +TIP protein known to bind to MTs, helping to stabilize MTs, were also noted in testes following overexpression of F5-peptide. Similar to α-tubulin, EB1 appeared as track-like structures across the epithelium, but overexpression of F5-peptide led to either considerably loss of EB1 in the epithelium, and it no longer laid across the epithelium longitudinally, but truncated and also wrapped around groups of round spermatids destined to become giant multinucleated round spermatids for eventual degeneration. The last micrograph on the right of the top panel is the negative control (a stage V tubule) in which the primary antibody was substituted with the mouse IgG. Scale bar, 30 μm, which applies to other micrographs.

    Article Snippet: It was noted that overexpression of F5-peptide reduced the expression of F-actin at the BTB (Figure ).

    Techniques: Over Expression, In Vivo, Transfection, Plasmid Preparation, Immunohistochemistry, Blocking Assay, Negative Control

    Overexpression of F5-peptide perturbs F-actin organization in the seminiferous epithelium of adult rat testes in vivo Rat testes were transfected with pCI-neo/F5 vs. pCI-neo (control) using Regimens ( n = 9 rats) shown in Figure 3A . Frozen sections of testes were used to visualize the distribution of F-actin by FITC-phalloidin. Cell nuclei were visualized by DAPI. ( A ) Overexpression of F5-peptide led to extensive germ cell loss in tubules wherein F-actin distribution was grossly disrupted. The typical “stalk-like” structures of F-actin was not found in tubules following overexpression with F5-peptide. Scale bar in the left column, 100 μm; Scale bar in yellow box, 50 μm; red or blue box, 15 μm. ( B ) Representative micrographs of frozen sections of normal testes in selected stages were stained for F-actin. As noted herein, F-actin appeared as “stalk-like” structures, tightly associated with elongating spermatids in transport across the epithelium in stage V tubules, also associated with apical ES surrounding the head of elongated spermatids in late stage VII, but considerably diminished in late stage VIII tubules to facilitate the release of sperms at spermiation. Moreover, some stalk-like structure reappeared across the epithelium in late stage VIII, perhaps being used to support the transport of residual bodies/phagosome to the basal compartment for their eventual lysosomal degradation. However, following F5-peptide overexpression, the typical F-actin organization in the epithelium was considerably disrupted, For instance, elongating spermatids in stage V tubules no longer associated with the F-actin-based stalk-like structures and F-actin was considerably diminished in stage VII-VIII tubules. Elongated spermatids, however, remained entrapped inside the epithelium even though the apical ES had been disrupted. Scale bar, 25 μm, which applies to other micrographs.

    Journal: Oncotarget

    Article Title: F5-peptide induces aspermatogenesis by disrupting organization of actin- and microtubule-based cytoskeletons in the testis

    doi: 10.18632/oncotarget.11887

    Figure Lengend Snippet: Overexpression of F5-peptide perturbs F-actin organization in the seminiferous epithelium of adult rat testes in vivo Rat testes were transfected with pCI-neo/F5 vs. pCI-neo (control) using Regimens ( n = 9 rats) shown in Figure 3A . Frozen sections of testes were used to visualize the distribution of F-actin by FITC-phalloidin. Cell nuclei were visualized by DAPI. ( A ) Overexpression of F5-peptide led to extensive germ cell loss in tubules wherein F-actin distribution was grossly disrupted. The typical “stalk-like” structures of F-actin was not found in tubules following overexpression with F5-peptide. Scale bar in the left column, 100 μm; Scale bar in yellow box, 50 μm; red or blue box, 15 μm. ( B ) Representative micrographs of frozen sections of normal testes in selected stages were stained for F-actin. As noted herein, F-actin appeared as “stalk-like” structures, tightly associated with elongating spermatids in transport across the epithelium in stage V tubules, also associated with apical ES surrounding the head of elongated spermatids in late stage VII, but considerably diminished in late stage VIII tubules to facilitate the release of sperms at spermiation. Moreover, some stalk-like structure reappeared across the epithelium in late stage VIII, perhaps being used to support the transport of residual bodies/phagosome to the basal compartment for their eventual lysosomal degradation. However, following F5-peptide overexpression, the typical F-actin organization in the epithelium was considerably disrupted, For instance, elongating spermatids in stage V tubules no longer associated with the F-actin-based stalk-like structures and F-actin was considerably diminished in stage VII-VIII tubules. Elongated spermatids, however, remained entrapped inside the epithelium even though the apical ES had been disrupted. Scale bar, 25 μm, which applies to other micrographs.

    Article Snippet: It was noted that overexpression of F5-peptide reduced the expression of F-actin at the BTB (Figure ).

    Techniques: Over Expression, In Vivo, Transfection, Staining

    Overexpression of F5-peptide induces re-organization of actin- and microtubule (MT)-based cytoskeletons in Sertoli cells ( A ) Overexpression of F5-peptide induced disorganization of actin microfilaments in which truncation of F-actin network (green or gray) in Sertoli cells was noted. Scale bar, 30 μm, which applies to other micrographs. ( B ) Actin bundling assay was performed to illustrate overexpression of F5-peptide led to a considerable loss of actin bundling capability. In this biochemical assay, pellet contained bundled actin microfilaments, whereas supernatant contained unbundled, linear and/or truncated actin microfilaments. Histograms summarize the findings on the upper panel, and each bar is a mean ± SD of n = 4 experiments. ** P

    Journal: Oncotarget

    Article Title: F5-peptide induces aspermatogenesis by disrupting organization of actin- and microtubule-based cytoskeletons in the testis

    doi: 10.18632/oncotarget.11887

    Figure Lengend Snippet: Overexpression of F5-peptide induces re-organization of actin- and microtubule (MT)-based cytoskeletons in Sertoli cells ( A ) Overexpression of F5-peptide induced disorganization of actin microfilaments in which truncation of F-actin network (green or gray) in Sertoli cells was noted. Scale bar, 30 μm, which applies to other micrographs. ( B ) Actin bundling assay was performed to illustrate overexpression of F5-peptide led to a considerable loss of actin bundling capability. In this biochemical assay, pellet contained bundled actin microfilaments, whereas supernatant contained unbundled, linear and/or truncated actin microfilaments. Histograms summarize the findings on the upper panel, and each bar is a mean ± SD of n = 4 experiments. ** P

    Article Snippet: It was noted that overexpression of F5-peptide reduced the expression of F-actin at the BTB (Figure ).

    Techniques: Over Expression

    Overexpression of F5 peptide impairs spermatogenesis in vivo ( A ) Two regimens were used since phenotypes on day 5 (Regimen 1) vs. day 8 and 11 (Regimen 2) were similar, data were pooled for analysis. ( B ) Testis weight in control (pCI-neo) vs . pCI-neo/F5 in both regimens of n = 18 rats. ( C ) F5-peptide mRNA level was analyzed by q-PCR. GAPDH served as an internal control. Each bar is a mean ± SD of n = 9 rats. ** P

    Journal: Oncotarget

    Article Title: F5-peptide induces aspermatogenesis by disrupting organization of actin- and microtubule-based cytoskeletons in the testis

    doi: 10.18632/oncotarget.11887

    Figure Lengend Snippet: Overexpression of F5 peptide impairs spermatogenesis in vivo ( A ) Two regimens were used since phenotypes on day 5 (Regimen 1) vs. day 8 and 11 (Regimen 2) were similar, data were pooled for analysis. ( B ) Testis weight in control (pCI-neo) vs . pCI-neo/F5 in both regimens of n = 18 rats. ( C ) F5-peptide mRNA level was analyzed by q-PCR. GAPDH served as an internal control. Each bar is a mean ± SD of n = 9 rats. ** P

    Article Snippet: It was noted that overexpression of F5-peptide reduced the expression of F-actin at the BTB (Figure ).

    Techniques: Over Expression, In Vivo, Polymerase Chain Reaction

    Overexpression of F5-peptide perturbs distribution TJ and basal ES proteins at the BTB through changes in the organization of F-actin in adult rat testes in vivo ( A ) Frozen sections obtained from testes transfected with pCI-neo/F5 vs. pCI-neo alone (control) were stained for F-actin, TJ proteins claudin-11 and ZO-1, as well as basal ES proteins N-cadherin and β-catenin. Cell nuclei were visualized by DAPI (blue). The fluorescence intensity of F-actin at the BTB was considerably diminished after F5-peptide overexpression, consistent with in vitro observation due to truncation and dis-organization of actin microfilaments at the site. TJ proteins claudin-11 and ZO-1, as well as basal ES proteins N-cadherin and β-catenin were found to be diffusely localized at the Sertoli cell BTB in the testis transfected with pCI-neo/F5, supporting findings in vitro that illustrate an increase in protein internalization at the site. Basement membrane was annotated by a dashed white line illustrating the relative location of the basement membrane/tunica propria. Scale bar, 30 μm, which applies to all other micrographs. ( B ) Semi-quantitative analysis of fluorescence data shown in (A) including fluorescence intensity (left panel) vs. mis-localization of TJ and basal ES proteins by diffusing away from the BTB (right panel). Data in the control group were arbitrarily set at 1 against which statistical comparison was performed. Each bar is a mean ± SD of n = 4 rats. ** P

    Journal: Oncotarget

    Article Title: F5-peptide induces aspermatogenesis by disrupting organization of actin- and microtubule-based cytoskeletons in the testis

    doi: 10.18632/oncotarget.11887

    Figure Lengend Snippet: Overexpression of F5-peptide perturbs distribution TJ and basal ES proteins at the BTB through changes in the organization of F-actin in adult rat testes in vivo ( A ) Frozen sections obtained from testes transfected with pCI-neo/F5 vs. pCI-neo alone (control) were stained for F-actin, TJ proteins claudin-11 and ZO-1, as well as basal ES proteins N-cadherin and β-catenin. Cell nuclei were visualized by DAPI (blue). The fluorescence intensity of F-actin at the BTB was considerably diminished after F5-peptide overexpression, consistent with in vitro observation due to truncation and dis-organization of actin microfilaments at the site. TJ proteins claudin-11 and ZO-1, as well as basal ES proteins N-cadherin and β-catenin were found to be diffusely localized at the Sertoli cell BTB in the testis transfected with pCI-neo/F5, supporting findings in vitro that illustrate an increase in protein internalization at the site. Basement membrane was annotated by a dashed white line illustrating the relative location of the basement membrane/tunica propria. Scale bar, 30 μm, which applies to all other micrographs. ( B ) Semi-quantitative analysis of fluorescence data shown in (A) including fluorescence intensity (left panel) vs. mis-localization of TJ and basal ES proteins by diffusing away from the BTB (right panel). Data in the control group were arbitrarily set at 1 against which statistical comparison was performed. Each bar is a mean ± SD of n = 4 rats. ** P

    Article Snippet: It was noted that overexpression of F5-peptide reduced the expression of F-actin at the BTB (Figure ).

    Techniques: Over Expression, In Vivo, Transfection, Staining, Fluorescence, In Vitro

    Overexpression of F5-peptide perturbs F-actin organization through changes in the spatial expression of actin regulatory proteins, which in turn disrupts apical ES protein distribution in adult rat testes in vivo Frozen sections of testes following transfection of pCI-neo/F5 vs. pCI-neo (vector alone, control) were stained for F-actin, Arp3, and Eps8; as well as integral membrane proteins at the apical ES: β1-integrin (Sertoli cell-specific) vs. spermatid-specific laminin-γ3 chain and nectin-3. Spermatids that were entrapped inside the seminiferous epithelium were shown in the two rectangular columns on the right. Cell nuclei were visualized by DAPI. ( A ) At stage VII, F-actin, actin regulatory proteins Arp3 and Eps8 were prominently localized to the concave side of spermatid heads in control testes. Overexpression of F5-peptide, however, induced mis-organization of F-actin which was considerably diminished at the apical ES found in elongated spermatids located near the tubule lumen or embedded inside the epithelium. These changes in F-actin organization were the result of changes in spatial expression of Arp3 and Eps8 since these proteins no longer restricted to the concave side of spermatids, and their expression was considerably diminished. Furthermore, many spermatids had lost their polarity since they no longer pointed toward the basement membrane as found in control tubules. For spermatids entrapped inside the epithelium in these tubules, the fluorescence signals of Arp3 and Eps8 were also considerably diminished after F5-peptide overexpression, illustrating apical ES in these spermatids was also disrupted. Scale bar, 10 μm, which applies to other micrographs. ( B ) Apical ES adhesion proteins β1-integrin and nectin-3 were localized at the convex side of spermatid heads whereas laminin-γ3 chain was at the tip of spermatid heads in normal testes. Following F5-peptide overexpression, β1-integrin was grossly mis-localized since some fluorescence signal was found on the concave side of spermatid heads; whereas laminin-γ3 chain and nectin-3 were also considerably down-regulated and mis-localized, thereby impeding spermatid adhesion, leading to germ cell exfoliation as noted in Figure 3 . Scale bar, 10 μm, which applies to other micrographs in the same panel.

    Journal: Oncotarget

    Article Title: F5-peptide induces aspermatogenesis by disrupting organization of actin- and microtubule-based cytoskeletons in the testis

    doi: 10.18632/oncotarget.11887

    Figure Lengend Snippet: Overexpression of F5-peptide perturbs F-actin organization through changes in the spatial expression of actin regulatory proteins, which in turn disrupts apical ES protein distribution in adult rat testes in vivo Frozen sections of testes following transfection of pCI-neo/F5 vs. pCI-neo (vector alone, control) were stained for F-actin, Arp3, and Eps8; as well as integral membrane proteins at the apical ES: β1-integrin (Sertoli cell-specific) vs. spermatid-specific laminin-γ3 chain and nectin-3. Spermatids that were entrapped inside the seminiferous epithelium were shown in the two rectangular columns on the right. Cell nuclei were visualized by DAPI. ( A ) At stage VII, F-actin, actin regulatory proteins Arp3 and Eps8 were prominently localized to the concave side of spermatid heads in control testes. Overexpression of F5-peptide, however, induced mis-organization of F-actin which was considerably diminished at the apical ES found in elongated spermatids located near the tubule lumen or embedded inside the epithelium. These changes in F-actin organization were the result of changes in spatial expression of Arp3 and Eps8 since these proteins no longer restricted to the concave side of spermatids, and their expression was considerably diminished. Furthermore, many spermatids had lost their polarity since they no longer pointed toward the basement membrane as found in control tubules. For spermatids entrapped inside the epithelium in these tubules, the fluorescence signals of Arp3 and Eps8 were also considerably diminished after F5-peptide overexpression, illustrating apical ES in these spermatids was also disrupted. Scale bar, 10 μm, which applies to other micrographs. ( B ) Apical ES adhesion proteins β1-integrin and nectin-3 were localized at the convex side of spermatid heads whereas laminin-γ3 chain was at the tip of spermatid heads in normal testes. Following F5-peptide overexpression, β1-integrin was grossly mis-localized since some fluorescence signal was found on the concave side of spermatid heads; whereas laminin-γ3 chain and nectin-3 were also considerably down-regulated and mis-localized, thereby impeding spermatid adhesion, leading to germ cell exfoliation as noted in Figure 3 . Scale bar, 10 μm, which applies to other micrographs in the same panel.

    Article Snippet: It was noted that overexpression of F5-peptide reduced the expression of F-actin at the BTB (Figure ).

    Techniques: Over Expression, Expressing, In Vivo, Transfection, Plasmid Preparation, Staining, Fluorescence

    F5-peptide perturbs distribution of BTB-associated proteins at the Sertoli cell-cell interface Sertoli cells were cultured alone for 3 day, and transfected with pCI-neo/F5 vs. pCI-neo vector alone (control) for 24 hr. Thereafter, cells were rinsed with F12/DMEM and terminated 24 hr later for RT-PCR and IF on day 5 vs. 48 hr later for IB on day 6. ( A ) Successful overexpression of F5-peptide was confirmed by RT-PCR and q-PCR by using a specific primer pair ( Table S2 ) specific to F5-peptide. S16 served as a loading control for RT-PCR. GAPDH served as an internal control for q-PCR. ( B ) The steady-state levels of TJ proteins, basal ES proteins, actin regulatory proteins, MT regulatory protein, and signaling proteins found at the BTB were analyzed by IB. Overexpression of F5-peptide caused down-regulation of actin bundling proteins palladin and plastin 3 and also TJ proteins occludin and JAM-A. Actin served as a loading control. Histograms on the lower panel illustrate the down-regulation of occludin, JAM-A, palladin and plastin 3 following overexpression of F5-peptide. Each bar is a mean ± SD of n = 5 experiments, and data were normalized against actin. ** P

    Journal: Oncotarget

    Article Title: F5-peptide induces aspermatogenesis by disrupting organization of actin- and microtubule-based cytoskeletons in the testis

    doi: 10.18632/oncotarget.11887

    Figure Lengend Snippet: F5-peptide perturbs distribution of BTB-associated proteins at the Sertoli cell-cell interface Sertoli cells were cultured alone for 3 day, and transfected with pCI-neo/F5 vs. pCI-neo vector alone (control) for 24 hr. Thereafter, cells were rinsed with F12/DMEM and terminated 24 hr later for RT-PCR and IF on day 5 vs. 48 hr later for IB on day 6. ( A ) Successful overexpression of F5-peptide was confirmed by RT-PCR and q-PCR by using a specific primer pair ( Table S2 ) specific to F5-peptide. S16 served as a loading control for RT-PCR. GAPDH served as an internal control for q-PCR. ( B ) The steady-state levels of TJ proteins, basal ES proteins, actin regulatory proteins, MT regulatory protein, and signaling proteins found at the BTB were analyzed by IB. Overexpression of F5-peptide caused down-regulation of actin bundling proteins palladin and plastin 3 and also TJ proteins occludin and JAM-A. Actin served as a loading control. Histograms on the lower panel illustrate the down-regulation of occludin, JAM-A, palladin and plastin 3 following overexpression of F5-peptide. Each bar is a mean ± SD of n = 5 experiments, and data were normalized against actin. ** P

    Article Snippet: It was noted that overexpression of F5-peptide reduced the expression of F-actin at the BTB (Figure ).

    Techniques: Cell Culture, Transfection, Plasmid Preparation, Reverse Transcription Polymerase Chain Reaction, Over Expression, Polymerase Chain Reaction

    Chromatograms of 3-ADON/15-ADON, FB 2 /FB 3 , and FA 2 /FA 3  using each PFP column. ( a ) Mastro PFP; ( b ) ACQUITY UPLC CSH Fluoro-Phenyl; ( c ) Discovery HS F5. The analytical sample was 200 μg/L standards in neat solvent. Extraction mass window was ±5 ppm. Abbreviations; 3-ADON, 3-acetyl deoxynivalenol; 15-ADON, 15-acetyl deoxynivalenol; FB 2 , fumonisin B 2 ; FB 3 , fumonisin B 3 ; FA 2 , fumonisin A 2 ; FA 3 , fumonisin A 3 .

    Journal: Toxins

    Article Title: A Method for Simultaneous Determination of 20 Fusarium Toxins in Cereals by High-Resolution Liquid Chromatography-Orbitrap Mass Spectrometry with a Pentafluorophenyl Column

    doi: 10.3390/toxins7051664

    Figure Lengend Snippet: Chromatograms of 3-ADON/15-ADON, FB 2 /FB 3 , and FA 2 /FA 3 using each PFP column. ( a ) Mastro PFP; ( b ) ACQUITY UPLC CSH Fluoro-Phenyl; ( c ) Discovery HS F5. The analytical sample was 200 μg/L standards in neat solvent. Extraction mass window was ±5 ppm. Abbreviations; 3-ADON, 3-acetyl deoxynivalenol; 15-ADON, 15-acetyl deoxynivalenol; FB 2 , fumonisin B 2 ; FB 3 , fumonisin B 3 ; FA 2 , fumonisin A 2 ; FA 3 , fumonisin A 3 .

    Article Snippet: The separation of 20 Fusarium toxins was compared using the following analytical columns: Mastro C18 (2.1 mm × 150 mm, 3 μm; Shimadzu GLC, Ltd., Tokyo, Japan), Mastro PFP (2.1 mm × 150 mm, 3 μm; Shimadzu GLC, Ltd. Tokyo, Japan), ACQUITY UPLC CSH Fluoro-Phenyl (2.1 mm × 150 mm, 1.7 μm; Waters, Milford, MA, USA), and Discovery HS F5 (2.1 mm × 150 mm, 3 μm; Supelco, Bellefonte, PA, USA).

    Techniques: Cell Surface Hydrophobicity, Analytical Sample Preparation