tokuyasu cryosections Search Results


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  • 93
    Millipore anti mouse igg whole molecule gold antibody
    Induction of anti-HA humoral and cellular responses in mice vaccinated with <t>VLP-HA/VSP-G.</t> a – e Mice were orally vaccinated with VLPs and the humoral response against HA in different biological samples was evaluated. Levels of total serum anti-HA <t>IgG</t> ( a ), IgG1 and IgG2a ( b ), n = 8 from two independent experiments. Levels of IgA anti-HA in fecal extracts and BAL, n = 6 from two independent experiments ( c ). Levels of serum IgG anti-HA measured at different times post immunization, n = 6 from two independent experiments ( d ). Levels of serum IgG anti-HA in animals immunized with a mixture of VLP-HA plus VLP-VSP-G, n = 6 from two independent experiments ( e ). f Levels of serum IgG and fecal IgA in mice vaccinated with VLPs via oral or subcutaneous (s.c.) route, n = 8 from two independent experiments. g Mice were orally immunized with four weekly doses of 50 μg of recombinant ΔVSP1267 or vehicle. One week after the last immunization the presence of anti-VSP1267 antibodies in blood and fecal samples was checked, then these animals were orally immunized with VLP-HA/VSP-G, according to the protocol previously used. One week after the last VLP dose, the levels of serum IgG and fecal IgA anti-HA Abs were measured, n = 6 from two independent experiments. h , i Mice were orally vaccinated with VLPs and the cellular response against HA was evaluated. The frequency of HA-specific IFN-γ-secreting T cells (spot-forming colonies, SFC) was determined after antigen-specific re-stimulation of splenocytes, n = 7 from two independent experiments ( h ). Cytokines were measured in splenocyte supernatants and only those cytokines with detectable levels are shown, n = 6 from two independent experiments ( i ). Data were analyzed by one-way ANOVA and Tukey’s multiple comparison test ( a – f , h , i ) or by two-way ANOVA and Bonferroni post-tests ( g ). Values represent mean ± s.e.m. * p
    Anti Mouse Igg Whole Molecule Gold Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 402 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Abcam rabbit anti gfp serum
    Immunogold Localization of <t>VHA-a1–GFP</t> and TGN Morphology.
    Rabbit Anti Gfp Serum, supplied by Abcam, used in various techniques. Bioz Stars score: 98/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Nanoprobes nanogold
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Nanogold, supplied by Nanoprobes, used in various techniques. Bioz Stars score: 91/100, based on 625 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Nanoprobes goat fab anti rabbit igg
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Goat Fab Anti Rabbit Igg, supplied by Nanoprobes, used in various techniques. Bioz Stars score: 89/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bsa  (Abcam)
    99
    Abcam bsa
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Bsa, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 11355 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore anti mouse
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Anti Mouse, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3840 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore anti ha
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Anti Ha, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 6148 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore bovine gelatin
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Bovine Gelatin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 238 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore uranyl acetate methylcellulose
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Uranyl Acetate Methylcellulose, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore hepes
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Hepes, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 50050 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Hamamatsu orca er ii camera
    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced <t>Nanogold.</t> Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Orca Er Ii Camera, supplied by Hamamatsu, used in various techniques. Bioz Stars score: 92/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Abcam immunogold labeling
    <t>Immunogold</t> labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced Nanogold. Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Immunogold Labeling, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 145 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    JEOL jem 1011 electron microscope operating
    <t>Immunogold</t> labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced Nanogold. Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.
    Jem 1011 Electron Microscope Operating, supplied by JEOL, used in various techniques. Bioz Stars score: 88/100, based on 166 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Dianova 10 nm gold particles
    Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A <t>10-nm</t> thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.
    10 Nm Gold Particles, supplied by Dianova, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    JEOL 1200 ex ii electron microscope operating
    Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A <t>10-nm</t> thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.
    1200 Ex Ii Electron Microscope Operating, supplied by JEOL, used in various techniques. Bioz Stars score: 89/100, based on 121 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Aurion 15 nm gold particles
    Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A <t>10-nm</t> thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.
    15 Nm Gold Particles, supplied by Aurion, used in various techniques. Bioz Stars score: 90/100, based on 70 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bsa  (Aurion)
    92
    Aurion bsa
    Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A <t>10-nm</t> thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.
    Bsa, supplied by Aurion, used in various techniques. Bioz Stars score: 92/100, based on 349 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Aurion antibody against mouse igg
    Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A <t>10-nm</t> thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.
    Antibody Against Mouse Igg, supplied by Aurion, used in various techniques. Bioz Stars score: 88/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Rockland Immunochemicals anti biotin rabbit antibody
    Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A <t>10-nm</t> thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.
    Anti Biotin Rabbit Antibody, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore anti myc
    Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A <t>10-nm</t> thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.
    Anti Myc, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4223 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Becton Dickinson monoclonal anti flotillin 2 antibody
    <t>Flotillin-2</t> is found in pre-fusion myoblasts after cholesterol depletion. Immunofluorescence of flotillin-2, desmin and DAPI in cultures treated with methyl-β-cyclodextrin (MbCD) showing flotillin-2 expression in mononucleated cells that are fusing with myotubes. Chick myogenic cells were grown for 24 hours, treated with 2 mM MbCD for 30 min and grown for the next 24 hours ( B and C ). Some cells were not treated and were fixed at 48 hours of culture (control, A ). All cells were fixed with paraformaldehyde and stained with antibodies against desmin ( red ) and flotillin-2 ( green ) and with the nuclear dye DAPI ( blue ). Merged images are shown in A–C . Note an increase in the number of flotillin-2 positive-mononucleated cells in close contact with the membrane of multinucleated myotubes (arrows in B and C ). Scale bar in A represents 20 µm.
    Monoclonal Anti Flotillin 2 Antibody, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Becton Dickinson nh4 cl
    <t>Flotillin-2</t> is found in pre-fusion myoblasts after cholesterol depletion. Immunofluorescence of flotillin-2, desmin and DAPI in cultures treated with methyl-β-cyclodextrin (MbCD) showing flotillin-2 expression in mononucleated cells that are fusing with myotubes. Chick myogenic cells were grown for 24 hours, treated with 2 mM MbCD for 30 min and grown for the next 24 hours ( B and C ). Some cells were not treated and were fixed at 48 hours of culture (control, A ). All cells were fixed with paraformaldehyde and stained with antibodies against desmin ( red ) and flotillin-2 ( green ) and with the nuclear dye DAPI ( blue ). Merged images are shown in A–C . Note an increase in the number of flotillin-2 positive-mononucleated cells in close contact with the membrane of multinucleated myotubes (arrows in B and C ). Scale bar in A represents 20 µm.
    Nh4 Cl, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 93/100, based on 438 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Dianova goat anti rabbit igg
    <t>Flotillin-2</t> is found in pre-fusion myoblasts after cholesterol depletion. Immunofluorescence of flotillin-2, desmin and DAPI in cultures treated with methyl-β-cyclodextrin (MbCD) showing flotillin-2 expression in mononucleated cells that are fusing with myotubes. Chick myogenic cells were grown for 24 hours, treated with 2 mM MbCD for 30 min and grown for the next 24 hours ( B and C ). Some cells were not treated and were fixed at 48 hours of culture (control, A ). All cells were fixed with paraformaldehyde and stained with antibodies against desmin ( red ) and flotillin-2 ( green ) and with the nuclear dye DAPI ( blue ). Merged images are shown in A–C . Note an increase in the number of flotillin-2 positive-mononucleated cells in close contact with the membrane of multinucleated myotubes (arrows in B and C ). Scale bar in A represents 20 µm.
    Goat Anti Rabbit Igg, supplied by Dianova, used in various techniques. Bioz Stars score: 92/100, based on 397 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Induction of anti-HA humoral and cellular responses in mice vaccinated with VLP-HA/VSP-G. a – e Mice were orally vaccinated with VLPs and the humoral response against HA in different biological samples was evaluated. Levels of total serum anti-HA IgG ( a ), IgG1 and IgG2a ( b ), n = 8 from two independent experiments. Levels of IgA anti-HA in fecal extracts and BAL, n = 6 from two independent experiments ( c ). Levels of serum IgG anti-HA measured at different times post immunization, n = 6 from two independent experiments ( d ). Levels of serum IgG anti-HA in animals immunized with a mixture of VLP-HA plus VLP-VSP-G, n = 6 from two independent experiments ( e ). f Levels of serum IgG and fecal IgA in mice vaccinated with VLPs via oral or subcutaneous (s.c.) route, n = 8 from two independent experiments. g Mice were orally immunized with four weekly doses of 50 μg of recombinant ΔVSP1267 or vehicle. One week after the last immunization the presence of anti-VSP1267 antibodies in blood and fecal samples was checked, then these animals were orally immunized with VLP-HA/VSP-G, according to the protocol previously used. One week after the last VLP dose, the levels of serum IgG and fecal IgA anti-HA Abs were measured, n = 6 from two independent experiments. h , i Mice were orally vaccinated with VLPs and the cellular response against HA was evaluated. The frequency of HA-specific IFN-γ-secreting T cells (spot-forming colonies, SFC) was determined after antigen-specific re-stimulation of splenocytes, n = 7 from two independent experiments ( h ). Cytokines were measured in splenocyte supernatants and only those cytokines with detectable levels are shown, n = 6 from two independent experiments ( i ). Data were analyzed by one-way ANOVA and Tukey’s multiple comparison test ( a – f , h , i ) or by two-way ANOVA and Bonferroni post-tests ( g ). Values represent mean ± s.e.m. * p

    Journal: Nature Communications

    Article Title: Efficient oral vaccination by bioengineering virus-like particles with protozoan surface proteins

    doi: 10.1038/s41467-018-08265-9

    Figure Lengend Snippet: Induction of anti-HA humoral and cellular responses in mice vaccinated with VLP-HA/VSP-G. a – e Mice were orally vaccinated with VLPs and the humoral response against HA in different biological samples was evaluated. Levels of total serum anti-HA IgG ( a ), IgG1 and IgG2a ( b ), n = 8 from two independent experiments. Levels of IgA anti-HA in fecal extracts and BAL, n = 6 from two independent experiments ( c ). Levels of serum IgG anti-HA measured at different times post immunization, n = 6 from two independent experiments ( d ). Levels of serum IgG anti-HA in animals immunized with a mixture of VLP-HA plus VLP-VSP-G, n = 6 from two independent experiments ( e ). f Levels of serum IgG and fecal IgA in mice vaccinated with VLPs via oral or subcutaneous (s.c.) route, n = 8 from two independent experiments. g Mice were orally immunized with four weekly doses of 50 μg of recombinant ΔVSP1267 or vehicle. One week after the last immunization the presence of anti-VSP1267 antibodies in blood and fecal samples was checked, then these animals were orally immunized with VLP-HA/VSP-G, according to the protocol previously used. One week after the last VLP dose, the levels of serum IgG and fecal IgA anti-HA Abs were measured, n = 6 from two independent experiments. h , i Mice were orally vaccinated with VLPs and the cellular response against HA was evaluated. The frequency of HA-specific IFN-γ-secreting T cells (spot-forming colonies, SFC) was determined after antigen-specific re-stimulation of splenocytes, n = 7 from two independent experiments ( h ). Cytokines were measured in splenocyte supernatants and only those cytokines with detectable levels are shown, n = 6 from two independent experiments ( i ). Data were analyzed by one-way ANOVA and Tukey’s multiple comparison test ( a – f , h , i ) or by two-way ANOVA and Bonferroni post-tests ( g ). Values represent mean ± s.e.m. * p

    Article Snippet: TEM of cryosections was performed by applying the Tokuyasu technique and incubated with anti-HA or anti-VSP and anti-mouse coupled 5-nm gold particles (Sigma-Aldrich, Cat. # G7527, dilution 1/50).

    Techniques: Mouse Assay, Recombinant

    Immunogold Localization of VHA-a1–GFP and TGN Morphology.

    Journal: The Plant Cell

    Article Title: Vacuolar H+-ATPase Activity Is Required for Endocytic and Secretory Trafficking in Arabidopsis [W]

    doi: 10.1105/tpc.105.037978

    Figure Lengend Snippet: Immunogold Localization of VHA-a1–GFP and TGN Morphology.

    Article Snippet: Immunogold labeling was performed on ultrathin thawed Tokuyasu cryosections of formaldehyde-fixed (8%, 3 h) and sucrose-infiltrated (2.1 M) root tips using rabbit anti-GFP serum (1:25; Abcam) or rabbit anti-VHA-E serum (1:500) ( ) and silver-enhanced (HQ Silver, 6 min; Nanoprobes) goat (Fab′) anti-rabbit IgG coupled to Nanogold (No. 2004; Nanoprobes).

    Techniques:

    Rapid Colocalization of VHA-a1–GFP with FM4-64.

    Journal: The Plant Cell

    Article Title: Vacuolar H+-ATPase Activity Is Required for Endocytic and Secretory Trafficking in Arabidopsis [W]

    doi: 10.1105/tpc.105.037978

    Figure Lengend Snippet: Rapid Colocalization of VHA-a1–GFP with FM4-64.

    Article Snippet: Immunogold labeling was performed on ultrathin thawed Tokuyasu cryosections of formaldehyde-fixed (8%, 3 h) and sucrose-infiltrated (2.1 M) root tips using rabbit anti-GFP serum (1:25; Abcam) or rabbit anti-VHA-E serum (1:500) ( ) and silver-enhanced (HQ Silver, 6 min; Nanoprobes) goat (Fab′) anti-rabbit IgG coupled to Nanogold (No. 2004; Nanoprobes).

    Techniques:

    Subcellular Localization of VHA-a–GFP Fusion Proteins Expressed in Roots of Seedlings.

    Journal: The Plant Cell

    Article Title: Vacuolar H+-ATPase Activity Is Required for Endocytic and Secretory Trafficking in Arabidopsis [W]

    doi: 10.1105/tpc.105.037978

    Figure Lengend Snippet: Subcellular Localization of VHA-a–GFP Fusion Proteins Expressed in Roots of Seedlings.

    Article Snippet: Immunogold labeling was performed on ultrathin thawed Tokuyasu cryosections of formaldehyde-fixed (8%, 3 h) and sucrose-infiltrated (2.1 M) root tips using rabbit anti-GFP serum (1:25; Abcam) or rabbit anti-VHA-E serum (1:500) ( ) and silver-enhanced (HQ Silver, 6 min; Nanoprobes) goat (Fab′) anti-rabbit IgG coupled to Nanogold (No. 2004; Nanoprobes).

    Techniques:

    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced Nanogold. Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.

    Journal: The Plant Journal

    Article Title: Function of the anion transporter AtCLC-d in the trans-Golgi network

    doi: 10.1111/j.1365-313X.2007.03061.x

    Figure Lengend Snippet: Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced Nanogold. Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.

    Article Snippet: Immunogold labeling was performed on ultra-thin (80–100 nm) thawed Tokuyasu cryosections of formaldehyde-fixed (8%, 2 h) and sucrose-infiltrated (2.1 M) root tips using rabbit anti-GFP serum (1:250, 60 min; Abcam, http://www.abcam.com ) and silver-enhanced (HQ Silver, 8 min; Nanoprobes, http://www.nanoprobes.com ) goat (Fab′) anti-rabbit IgG coupled to Nanogold (1:50; no. 2004, Nanoprobes) ( ).

    Techniques: Labeling, Stable Transfection, Expressing

    Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced Nanogold. Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.

    Journal: The Plant Journal

    Article Title: Function of the anion transporter AtCLC-d in the trans-Golgi network

    doi: 10.1111/j.1365-313X.2007.03061.x

    Figure Lengend Snippet: Immunogold labeling of ultra-thin root cryosections of plants stably expressing AtCLC-d–GFP. (a, b) Anti-GFP antibodies were detected with silver-enhanced Nanogold. Gold particles accumulated in the TGN region close to the trans -Golgi cisternae of cortex and epidermal cells of root tips. The trans-Golgi side is marked with (T) and is always shown on the lower side of the Golgi stack (G). (c) No labeling above background was seen in controls not expressing AtCLC-d–GFP. (d) Labeling in plants stably expressing VHA-a1–GFP. Scale bar = 200 nm.

    Article Snippet: Immunogold labeling was performed on ultra-thin (80–100 nm) thawed Tokuyasu cryosections of formaldehyde-fixed (8%, 2 h) and sucrose-infiltrated (2.1 M) root tips using rabbit anti-GFP serum (1:250, 60 min; Abcam, http://www.abcam.com ) and silver-enhanced (HQ Silver, 8 min; Nanoprobes, http://www.nanoprobes.com ) goat (Fab′) anti-rabbit IgG coupled to Nanogold (1:50; no. 2004, Nanoprobes) ( ).

    Techniques: Labeling, Stable Transfection, Expressing

    Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A 10-nm thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.

    Journal: The Journal of Cell Biology

    Article Title: Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g

    doi: 10.1083/jcb.200811099

    Figure Lengend Snippet: Δfcj1 mitochondria contain zipperlike structures typical of oligomers of the F 1 F O –ATP synthase. Cryo-EM tomograms of isolated mitochondria. (A) Slice through a tomogram of a vitrified wild-type mitochondrion. (B) A CJ magnified (left) and surface rendered (right) corresponding to the boxed area in A is shown. Panels A and B are reprinted from Zick et al. (2009) with permission from Biochimica et Biophysica Acta . (C–G) Δfcj1 mitochondria. (C) Slice through a tomogram of a vitrified Δfcj1 mitochondrion. (D) Magnified view of boxed area in C (left) and surface-rendered representation (right) showing a zipperlike, regular arrangement with characteristics of the F 1 parts of F 1 F O –ATP synthase. The IM is shown in yellow, and F 1 F O –ATP synthases are shown in red. (E) A 10-nm thick slice of a tomogram cutting through particles typical of the F 1 parts of F 1 F O –ATP synthase in side views (arrow) and top views (boxed area). (F and G) Sections through the tomogram and volume-rendered top views of putative F 1 F O –ATP synthases arranged in double-row hexagonal stripes (F) and double-row square stripes (G) are shown. Bars: (A–C and E) 100 nm; (D, F, and G) 50 nm.

    Article Snippet: Cells were immunogold labeled using the indicated antibodies and goat anti–rabbit IgG conjugated to 10-nm gold particles (Dianova).

    Techniques: Isolation

    Flotillin-2 is found in pre-fusion myoblasts after cholesterol depletion. Immunofluorescence of flotillin-2, desmin and DAPI in cultures treated with methyl-β-cyclodextrin (MbCD) showing flotillin-2 expression in mononucleated cells that are fusing with myotubes. Chick myogenic cells were grown for 24 hours, treated with 2 mM MbCD for 30 min and grown for the next 24 hours ( B and C ). Some cells were not treated and were fixed at 48 hours of culture (control, A ). All cells were fixed with paraformaldehyde and stained with antibodies against desmin ( red ) and flotillin-2 ( green ) and with the nuclear dye DAPI ( blue ). Merged images are shown in A–C . Note an increase in the number of flotillin-2 positive-mononucleated cells in close contact with the membrane of multinucleated myotubes (arrows in B and C ). Scale bar in A represents 20 µm.

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Flotillin-2 is found in pre-fusion myoblasts after cholesterol depletion. Immunofluorescence of flotillin-2, desmin and DAPI in cultures treated with methyl-β-cyclodextrin (MbCD) showing flotillin-2 expression in mononucleated cells that are fusing with myotubes. Chick myogenic cells were grown for 24 hours, treated with 2 mM MbCD for 30 min and grown for the next 24 hours ( B and C ). Some cells were not treated and were fixed at 48 hours of culture (control, A ). All cells were fixed with paraformaldehyde and stained with antibodies against desmin ( red ) and flotillin-2 ( green ) and with the nuclear dye DAPI ( blue ). Merged images are shown in A–C . Note an increase in the number of flotillin-2 positive-mononucleated cells in close contact with the membrane of multinucleated myotubes (arrows in B and C ). Scale bar in A represents 20 µm.

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: Immunofluorescence, Expressing, Staining

    Distribution of flotillin-2 in human neonatal muscle cells. Human neonatal muscle cells were grown as described in Materials and Methods section. Cells were fixed with methanol and stained with an anti-flotillin-2 antibody ( green , A and B ) and the nuclear dye DAPI ( blue , A and B ). Merged images are shown in A and B . Note that flotillin-2 is present in human myoblasts and myotubes in vesicle-like structures (arrows in A and B ). Scale bar in A represents 10 µm.

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Distribution of flotillin-2 in human neonatal muscle cells. Human neonatal muscle cells were grown as described in Materials and Methods section. Cells were fixed with methanol and stained with an anti-flotillin-2 antibody ( green , A and B ) and the nuclear dye DAPI ( blue , A and B ). Merged images are shown in A and B . Note that flotillin-2 is present in human myoblasts and myotubes in vesicle-like structures (arrows in A and B ). Scale bar in A represents 10 µm.

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: Staining

    Cholesterol depletion enhances the expression of flotillin-2 protein and mRNA. Chick myogenic cells were grown 24(control, Ct ). Cell culture extracts were analyzed in Western blot using an antibody against flotillin-2 ( A ). Lower Western blot shows α-tubulin reactivity of the same samples, and was used to normalize sample loading ( A ). Quantification of protein bands revealed a 40% increase in the levels of flotillin-2 expression after cholesterol depletion ( B ). RT-PCR analysis (for details, see Materials and Methods ) of the expression of flotillin-2 in control and in MbCD-treated cells is shown in C . Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used for normalization. Analysis of the expression of flotillin-2 shows a more than 2-fold increase in the levels of mRNA expression in MbCD-treated cells compared with control cells. *p

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Cholesterol depletion enhances the expression of flotillin-2 protein and mRNA. Chick myogenic cells were grown 24(control, Ct ). Cell culture extracts were analyzed in Western blot using an antibody against flotillin-2 ( A ). Lower Western blot shows α-tubulin reactivity of the same samples, and was used to normalize sample loading ( A ). Quantification of protein bands revealed a 40% increase in the levels of flotillin-2 expression after cholesterol depletion ( B ). RT-PCR analysis (for details, see Materials and Methods ) of the expression of flotillin-2 in control and in MbCD-treated cells is shown in C . Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used for normalization. Analysis of the expression of flotillin-2 shows a more than 2-fold increase in the levels of mRNA expression in MbCD-treated cells compared with control cells. *p

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: Expressing, Cell Culture, Western Blot, Reverse Transcription Polymerase Chain Reaction

    Cryo-immunogold EM labeling of flotillin-2 in myogenic cells. Chick myogenic cells were grown for 48-flotillin-2 antibody followed by a 10- η m gold-conjugated secondary antibody. Note that gold particles are present in vesicles ( a ) and associated with Golgi stacks ( b ). GC, Golgi complex. Scale bar in a represents 100 η m and in b represents 250 η m.

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Cryo-immunogold EM labeling of flotillin-2 in myogenic cells. Chick myogenic cells were grown for 48-flotillin-2 antibody followed by a 10- η m gold-conjugated secondary antibody. Note that gold particles are present in vesicles ( a ) and associated with Golgi stacks ( b ). GC, Golgi complex. Scale bar in a represents 100 η m and in b represents 250 η m.

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: Labeling

    Brefeldin A induces a major reduction in the number of flotillin-2 containing vesicles. Chick myogenic cells were grown for 24(5 µg/ml) for 3 hours or with nocodazole (10 µg/ml) for 3 hours. After treatment, cells were grown in fresh culture medium for the next 3 hours. In images ( A–F ) cells were fixed with paraformaldehyde and stained with an antibody against flotillin-2 ( green, A,C,E ) and with the nuclear dye DAPI ( blue, B,D,F ). Note that while nocodazole have no effect in the presence and distribution of flotillin-2 positive vesicles ( C,D ), brefeldin A induced a major reduction in flotillin-2 containing vesicles ( E,F ). In images ( G–I ) cells were analyzed under phase contrast microscopy and superimposed with DAPI (blue). Scale bars represents 50 µm (in A–F and G–I ).

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Brefeldin A induces a major reduction in the number of flotillin-2 containing vesicles. Chick myogenic cells were grown for 24(5 µg/ml) for 3 hours or with nocodazole (10 µg/ml) for 3 hours. After treatment, cells were grown in fresh culture medium for the next 3 hours. In images ( A–F ) cells were fixed with paraformaldehyde and stained with an antibody against flotillin-2 ( green, A,C,E ) and with the nuclear dye DAPI ( blue, B,D,F ). Note that while nocodazole have no effect in the presence and distribution of flotillin-2 positive vesicles ( C,D ), brefeldin A induced a major reduction in flotillin-2 containing vesicles ( E,F ). In images ( G–I ) cells were analyzed under phase contrast microscopy and superimposed with DAPI (blue). Scale bars represents 50 µm (in A–F and G–I ).

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: Staining, Microscopy

    Flotillin-2 is down-regulated during in vitro chick skeletal myogenesis. Chick myogenic cells were grown for 24, 48 and 72-2. ( A ) Upper Western blot shows flotillin-2 reactivity and lower Western blot shows α-tubulin reactivity of the same samples, and was used to normalize sample loading. ( B ) Quantification of protein bands revealed a progressive decrease in the levels of flotillin-2 expression during skeletal muscle differentiation. *p

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Flotillin-2 is down-regulated during in vitro chick skeletal myogenesis. Chick myogenic cells were grown for 24, 48 and 72-2. ( A ) Upper Western blot shows flotillin-2 reactivity and lower Western blot shows α-tubulin reactivity of the same samples, and was used to normalize sample loading. ( B ) Quantification of protein bands revealed a progressive decrease in the levels of flotillin-2 expression during skeletal muscle differentiation. *p

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: In Vitro, Western Blot, Expressing

    Flotillin-2 is mainly expressed in fibroblasts and weakly expressed in myoblasts. Myogenic cells were grown for 24( A and B ). Cells were fixed with paraformaldehyde and stained with antibodies against MyoD ( red , A and B ) and flotillin-2 ( green , A , and B ) and with the nuclear dye DAPI ( blue , B ). Merged images are shown in A and B . Note that flotillin-2 is highly expressed in MyoD-negative cells and weakly expressed in MyoD-positive cells ( A and B ). Scale bar in B represents 20 µm.

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Flotillin-2 is mainly expressed in fibroblasts and weakly expressed in myoblasts. Myogenic cells were grown for 24( A and B ). Cells were fixed with paraformaldehyde and stained with antibodies against MyoD ( red , A and B ) and flotillin-2 ( green , A , and B ) and with the nuclear dye DAPI ( blue , B ). Merged images are shown in A and B . Note that flotillin-2 is highly expressed in MyoD-negative cells and weakly expressed in MyoD-positive cells ( A and B ). Scale bar in B represents 20 µm.

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: Staining

    Flotillin-2 distribution in myogenic cells during skeletal muscle differentiation. Myogenic cells were grown for 24( A and B ) or 72 hours ( C ). Cells were fixed with paraformaldehyde and stained with antibodies against desmin ( red , A and C ) and flotillin-2 ( green , A, B and C ) and with the nuclear dye DAPI ( blue , A and C ). Merged images are shown in A and C . Note that with paraformaldehyde fixation it is possible to see flotillin-2 almost exclusively in mononucleated cells in vesicle-like structures ( B ) and nearly absent from myotubes ( A and C ). Scale bar in A and C represents 20 µm and in B represents 10 µm.

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Flotillin-2 distribution in myogenic cells during skeletal muscle differentiation. Myogenic cells were grown for 24( A and B ) or 72 hours ( C ). Cells were fixed with paraformaldehyde and stained with antibodies against desmin ( red , A and C ) and flotillin-2 ( green , A, B and C ) and with the nuclear dye DAPI ( blue , A and C ). Merged images are shown in A and C . Note that with paraformaldehyde fixation it is possible to see flotillin-2 almost exclusively in mononucleated cells in vesicle-like structures ( B ) and nearly absent from myotubes ( A and C ). Scale bar in A and C represents 20 µm and in B represents 10 µm.

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: Staining

    Distribution of flotillin-2 in C2C12 mouse muscle cell line. C2C12 cells were grown as described in Materials and Methods section. Cells were fixed with methanol and stained with an anti-flotillin-2 antibody ( green , A and C ) and the nuclear dye DAPI ( blue , B and C ). A merged image is shown in C . Note that flotillin-2 is present in C2C12 cells in vesicle-like structures (arrows in A and C ). Scale bar in C represents 20 µm.

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Distribution of flotillin-2 in C2C12 mouse muscle cell line. C2C12 cells were grown as described in Materials and Methods section. Cells were fixed with methanol and stained with an anti-flotillin-2 antibody ( green , A and C ) and the nuclear dye DAPI ( blue , B and C ). A merged image is shown in C . Note that flotillin-2 is present in C2C12 cells in vesicle-like structures (arrows in A and C ). Scale bar in C represents 20 µm.

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: Staining

    Flotillin-2 distribution in multinucleated myotubes. Myogenic cells were grown for 72-flotillin-2 antibodies (green, A and C ) and the nuclear dye DAPI (blue, B and D ). Note that with methanol fixation it is possible to see that flotillin-2 is present in elongated dots in myotubes (arrows in A and C ). Scale bar in D represents 20 µm.

    Journal: PLoS ONE

    Article Title: Differences in the Expression and Distribution of Flotillin-2 in Chick, Mice and Human Muscle Cells

    doi: 10.1371/journal.pone.0103990

    Figure Lengend Snippet: Flotillin-2 distribution in multinucleated myotubes. Myogenic cells were grown for 72-flotillin-2 antibodies (green, A and C ) and the nuclear dye DAPI (blue, B and D ). Note that with methanol fixation it is possible to see that flotillin-2 is present in elongated dots in myotubes (arrows in A and C ). Scale bar in D represents 20 µm.

    Article Snippet: The sections were blocked in 50 mM NH4 Cl and 3% bovine serum albumin in PBS, pH 8.0 for 30 min, and incubated with a monoclonal anti-flotillin-2 antibody (BD Transduction Laboratories, USA) diluted at 1∶5, followed by a goat anti-mouse 10-η m gold-conjugated (BB International, USA) diluted at 1∶100.

    Techniques: