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Carl Zeiss axio imager a1 microscope
Effects of anti-HER2 antibody BH1 and tumor necrosis factor-α on DNA synthesis and cell cycle in SK-BR-3 cells. ( A ) Effects on DNA synthesis were tested by 24-h BrdU incorporation assay. Cells were plated on coverslips in 12-well plates, treated as described in Figure 5 , and were exposed to BrdU during 24 h prior to indicated days. Nuclear BrdU was detected by indirect immunofluorescence assay. Nuclei were counterstained with DAPI, examined using Zeiss <t>Axio</t> Imager.A1 microscope. Representative photographs (3–5 frames per coverslip) were acquired. Percent BrdU incorporation was calculated after manual counting of BrdU + and BrdU - nuclei. * Denotes p-values ≤ 0.05 (BH1 vs. IgG1, BH1 + TNF-α vs. IgG1 + TNF-α). T-bars: SD. ( B - D ). Effects on cell cycle were analyzed by flow cytometry. SK-BR-3 cells were treated with 20 μg/ml BH1 or IgG isotype control antibody in the presence or absence of 1000 U/ml TNF-α. Cells were fixed on day 1 ( B ), day 3 ( C ) and day 6 ( D ), stained with propidium iodide and the cell cycle distribution was analysed with flow cytometry. Fraction of cells present in G2/M-phase (G2/M), S-phase (S) and G1-phase (G1) are shown in purple, green and orange respectively. Fraction of apoptotic cells observed as a SubG1 peak is shown in black.
Axio Imager A1 Microscope, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 99/100, based on 346 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/axio imager a1 microscope/product/Carl Zeiss
Average 99 stars, based on 346 article reviews
Price from $9.99 to $1999.99
axio imager a1 microscope - by Bioz Stars, 2020-11
99/100 stars

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1) Product Images from "Novel anti-HER2 monoclonal antibodies: synergy and antagonism with tumor necrosis factor-?"

Article Title: Novel anti-HER2 monoclonal antibodies: synergy and antagonism with tumor necrosis factor-?

Journal: BMC Cancer

doi: 10.1186/1471-2407-12-450

Effects of anti-HER2 antibody BH1 and tumor necrosis factor-α on DNA synthesis and cell cycle in SK-BR-3 cells. ( A ) Effects on DNA synthesis were tested by 24-h BrdU incorporation assay. Cells were plated on coverslips in 12-well plates, treated as described in Figure 5 , and were exposed to BrdU during 24 h prior to indicated days. Nuclear BrdU was detected by indirect immunofluorescence assay. Nuclei were counterstained with DAPI, examined using Zeiss Axio Imager.A1 microscope. Representative photographs (3–5 frames per coverslip) were acquired. Percent BrdU incorporation was calculated after manual counting of BrdU + and BrdU - nuclei. * Denotes p-values ≤ 0.05 (BH1 vs. IgG1, BH1 + TNF-α vs. IgG1 + TNF-α). T-bars: SD. ( B - D ). Effects on cell cycle were analyzed by flow cytometry. SK-BR-3 cells were treated with 20 μg/ml BH1 or IgG isotype control antibody in the presence or absence of 1000 U/ml TNF-α. Cells were fixed on day 1 ( B ), day 3 ( C ) and day 6 ( D ), stained with propidium iodide and the cell cycle distribution was analysed with flow cytometry. Fraction of cells present in G2/M-phase (G2/M), S-phase (S) and G1-phase (G1) are shown in purple, green and orange respectively. Fraction of apoptotic cells observed as a SubG1 peak is shown in black.
Figure Legend Snippet: Effects of anti-HER2 antibody BH1 and tumor necrosis factor-α on DNA synthesis and cell cycle in SK-BR-3 cells. ( A ) Effects on DNA synthesis were tested by 24-h BrdU incorporation assay. Cells were plated on coverslips in 12-well plates, treated as described in Figure 5 , and were exposed to BrdU during 24 h prior to indicated days. Nuclear BrdU was detected by indirect immunofluorescence assay. Nuclei were counterstained with DAPI, examined using Zeiss Axio Imager.A1 microscope. Representative photographs (3–5 frames per coverslip) were acquired. Percent BrdU incorporation was calculated after manual counting of BrdU + and BrdU - nuclei. * Denotes p-values ≤ 0.05 (BH1 vs. IgG1, BH1 + TNF-α vs. IgG1 + TNF-α). T-bars: SD. ( B - D ). Effects on cell cycle were analyzed by flow cytometry. SK-BR-3 cells were treated with 20 μg/ml BH1 or IgG isotype control antibody in the presence or absence of 1000 U/ml TNF-α. Cells were fixed on day 1 ( B ), day 3 ( C ) and day 6 ( D ), stained with propidium iodide and the cell cycle distribution was analysed with flow cytometry. Fraction of cells present in G2/M-phase (G2/M), S-phase (S) and G1-phase (G1) are shown in purple, green and orange respectively. Fraction of apoptotic cells observed as a SubG1 peak is shown in black.

Techniques Used: DNA Synthesis, BrdU Incorporation Assay, Immunofluorescence, Microscopy, Flow Cytometry, Cytometry, Staining

Strong binding of anti-HER2 antibodies to ERBB2 -amplified breast cancer cell lines. ERRB2 amplification was analyzed by FISH analysis. Cells were harvested at confluence, fixed and subjected to dual-color FISH using Texas Red-labeled ERBB2 (red) and FITC-labeled chromosome 17 α-satellite CEP17 (green) DNA probes (left panel). For generation of anti-HER2 monoclonal antibodies, mice were immunized with SK-BR-3 cells, followed by a recombinant protein composed of extracellular domain of HER2 fused to human IgG1 Fc domain (HER2 ECD). Antibodies were purified from conditioned hybridoma cell culture media by affinity chromatography. For immunofluorescence assay, cells were seeded on coverslips in 6-well plates, incubated 36 h in cell culture medium, fixed, and permeabilized. Fixed cells were incubated with anti-HER2 antibodies, and the primary antibody binding was detected using Alexa 488- conjugated anti-mouse IgG (BH1, BH2, BH5, BH6, BH7 panels; green). Nuclei were counterstained with DAPI (blue) and pictures were acquired using Zeiss Axio Imager.A1 microscope.
Figure Legend Snippet: Strong binding of anti-HER2 antibodies to ERBB2 -amplified breast cancer cell lines. ERRB2 amplification was analyzed by FISH analysis. Cells were harvested at confluence, fixed and subjected to dual-color FISH using Texas Red-labeled ERBB2 (red) and FITC-labeled chromosome 17 α-satellite CEP17 (green) DNA probes (left panel). For generation of anti-HER2 monoclonal antibodies, mice were immunized with SK-BR-3 cells, followed by a recombinant protein composed of extracellular domain of HER2 fused to human IgG1 Fc domain (HER2 ECD). Antibodies were purified from conditioned hybridoma cell culture media by affinity chromatography. For immunofluorescence assay, cells were seeded on coverslips in 6-well plates, incubated 36 h in cell culture medium, fixed, and permeabilized. Fixed cells were incubated with anti-HER2 antibodies, and the primary antibody binding was detected using Alexa 488- conjugated anti-mouse IgG (BH1, BH2, BH5, BH6, BH7 panels; green). Nuclei were counterstained with DAPI (blue) and pictures were acquired using Zeiss Axio Imager.A1 microscope.

Techniques Used: Binding Assay, Amplification, Fluorescence In Situ Hybridization, Labeling, Mouse Assay, Recombinant, Purification, Cell Culture, Affinity Chromatography, Immunofluorescence, Incubation, Microscopy

2) Product Images from "Novel anti-HER2 monoclonal antibodies: synergy and antagonism with tumor necrosis factor-?"

Article Title: Novel anti-HER2 monoclonal antibodies: synergy and antagonism with tumor necrosis factor-?

Journal: BMC Cancer

doi: 10.1186/1471-2407-12-450

Effects of anti-HER2 antibody BH1 and tumor necrosis factor-α on DNA synthesis and cell cycle in SK-BR-3 cells. ( A ) Effects on DNA synthesis were tested by 24-h BrdU incorporation assay. Cells were plated on coverslips in 12-well plates, treated as described in Figure 5 , and were exposed to BrdU during 24 h prior to indicated days. Nuclear BrdU was detected by indirect immunofluorescence assay. Nuclei were counterstained with DAPI, examined using Zeiss Axio Imager.A1 microscope. Representative photographs (3–5 frames per coverslip) were acquired. Percent BrdU incorporation was calculated after manual counting of BrdU + and BrdU - nuclei. * Denotes p-values ≤ 0.05 (BH1 vs. IgG1, BH1 + TNF-α vs. IgG1 + TNF-α). T-bars: SD. ( B - D ). Effects on cell cycle were analyzed by flow cytometry. SK-BR-3 cells were treated with 20 μg/ml BH1 or IgG isotype control antibody in the presence or absence of 1000 U/ml TNF-α. Cells were fixed on day 1 ( B ), day 3 ( C ) and day 6 ( D ), stained with propidium iodide and the cell cycle distribution was analysed with flow cytometry. Fraction of cells present in G2/M-phase (G2/M), S-phase (S) and G1-phase (G1) are shown in purple, green and orange respectively. Fraction of apoptotic cells observed as a SubG1 peak is shown in black.
Figure Legend Snippet: Effects of anti-HER2 antibody BH1 and tumor necrosis factor-α on DNA synthesis and cell cycle in SK-BR-3 cells. ( A ) Effects on DNA synthesis were tested by 24-h BrdU incorporation assay. Cells were plated on coverslips in 12-well plates, treated as described in Figure 5 , and were exposed to BrdU during 24 h prior to indicated days. Nuclear BrdU was detected by indirect immunofluorescence assay. Nuclei were counterstained with DAPI, examined using Zeiss Axio Imager.A1 microscope. Representative photographs (3–5 frames per coverslip) were acquired. Percent BrdU incorporation was calculated after manual counting of BrdU + and BrdU - nuclei. * Denotes p-values ≤ 0.05 (BH1 vs. IgG1, BH1 + TNF-α vs. IgG1 + TNF-α). T-bars: SD. ( B - D ). Effects on cell cycle were analyzed by flow cytometry. SK-BR-3 cells were treated with 20 μg/ml BH1 or IgG isotype control antibody in the presence or absence of 1000 U/ml TNF-α. Cells were fixed on day 1 ( B ), day 3 ( C ) and day 6 ( D ), stained with propidium iodide and the cell cycle distribution was analysed with flow cytometry. Fraction of cells present in G2/M-phase (G2/M), S-phase (S) and G1-phase (G1) are shown in purple, green and orange respectively. Fraction of apoptotic cells observed as a SubG1 peak is shown in black.

Techniques Used: DNA Synthesis, BrdU Incorporation Assay, Immunofluorescence, Microscopy, Flow Cytometry, Cytometry, Staining

Strong binding of anti-HER2 antibodies to ERBB2 -amplified breast cancer cell lines. ERRB2 amplification was analyzed by FISH analysis. Cells were harvested at confluence, fixed and subjected to dual-color FISH using Texas Red-labeled ERBB2 (red) and FITC-labeled chromosome 17 α-satellite CEP17 (green) DNA probes (left panel). For generation of anti-HER2 monoclonal antibodies, mice were immunized with SK-BR-3 cells, followed by a recombinant protein composed of extracellular domain of HER2 fused to human IgG1 Fc domain (HER2 ECD). Antibodies were purified from conditioned hybridoma cell culture media by affinity chromatography. For immunofluorescence assay, cells were seeded on coverslips in 6-well plates, incubated 36 h in cell culture medium, fixed, and permeabilized. Fixed cells were incubated with anti-HER2 antibodies, and the primary antibody binding was detected using Alexa 488- conjugated anti-mouse IgG (BH1, BH2, BH5, BH6, BH7 panels; green). Nuclei were counterstained with DAPI (blue) and pictures were acquired using Zeiss Axio Imager.A1 microscope.
Figure Legend Snippet: Strong binding of anti-HER2 antibodies to ERBB2 -amplified breast cancer cell lines. ERRB2 amplification was analyzed by FISH analysis. Cells were harvested at confluence, fixed and subjected to dual-color FISH using Texas Red-labeled ERBB2 (red) and FITC-labeled chromosome 17 α-satellite CEP17 (green) DNA probes (left panel). For generation of anti-HER2 monoclonal antibodies, mice were immunized with SK-BR-3 cells, followed by a recombinant protein composed of extracellular domain of HER2 fused to human IgG1 Fc domain (HER2 ECD). Antibodies were purified from conditioned hybridoma cell culture media by affinity chromatography. For immunofluorescence assay, cells were seeded on coverslips in 6-well plates, incubated 36 h in cell culture medium, fixed, and permeabilized. Fixed cells were incubated with anti-HER2 antibodies, and the primary antibody binding was detected using Alexa 488- conjugated anti-mouse IgG (BH1, BH2, BH5, BH6, BH7 panels; green). Nuclei were counterstained with DAPI (blue) and pictures were acquired using Zeiss Axio Imager.A1 microscope.

Techniques Used: Binding Assay, Amplification, Fluorescence In Situ Hybridization, Labeling, Mouse Assay, Recombinant, Purification, Cell Culture, Affinity Chromatography, Immunofluorescence, Incubation, Microscopy

3) Product Images from "The protective effect of non-invasive low intensity pulsed electric field and fucoidan in preventing oxidative stress-induced motor neuron death via ROCK/Akt pathway"

Article Title: The protective effect of non-invasive low intensity pulsed electric field and fucoidan in preventing oxidative stress-induced motor neuron death via ROCK/Akt pathway

Journal: PLoS ONE

doi: 10.1371/journal.pone.0214100

Effect of the combination treatment on the H 2 O 2 -induced neurite retraction. (A) The morphology of neuron cells was observed using immunofluorescence staining of beta-III tubulin under Zeiss Axio Imager A1 microscope. Scale bar = 20 μm. The average number of neurites per cell (B) and the average neurite length (C) were quantified to evaluate the neuroprotective effect. (n = 8, one-way ANOVA, Turkey’s test; *** is used for P
Figure Legend Snippet: Effect of the combination treatment on the H 2 O 2 -induced neurite retraction. (A) The morphology of neuron cells was observed using immunofluorescence staining of beta-III tubulin under Zeiss Axio Imager A1 microscope. Scale bar = 20 μm. The average number of neurites per cell (B) and the average neurite length (C) were quantified to evaluate the neuroprotective effect. (n = 8, one-way ANOVA, Turkey’s test; *** is used for P

Techniques Used: Immunofluorescence, Staining, Microscopy

4) Product Images from "OmpA Binding Mediates the Effect of Antimicrobial Peptide LL-37 on Acinetobacter baumannii"

Article Title: OmpA Binding Mediates the Effect of Antimicrobial Peptide LL-37 on Acinetobacter baumannii

Journal: PLoS ONE

doi: 10.1371/journal.pone.0141107

BA-LL37 binding to A . baumannii . (A) LL-37 binding to A . baumannii cells was determined by flow cytometry. Cells were incubated with different concentrations of BA-LL37 at 4°C in ice-cold PBS overnight. The binding between BA-LL37 and A . baumannii was detected by adding SA-DTAF. The increase of signal was detected and correlated to cells treated with increasing concentrations of LL-37, indicating that LL-37 binds directly to A . baumannii . These data are representative of three independent experiments with similar results. FL1-H indicates the extent of the fluorescence intensity. (B) An immunofluorescence staining assay was performed to verify LL-37 binding to A . baumannii . In the presence of 20 μg/ml LL-37, fluorescence was observed compared to the control (without BA-LL37 treatment). Samples were observed using a Carl Zeiss AXIO IMAGER A1 microscope.
Figure Legend Snippet: BA-LL37 binding to A . baumannii . (A) LL-37 binding to A . baumannii cells was determined by flow cytometry. Cells were incubated with different concentrations of BA-LL37 at 4°C in ice-cold PBS overnight. The binding between BA-LL37 and A . baumannii was detected by adding SA-DTAF. The increase of signal was detected and correlated to cells treated with increasing concentrations of LL-37, indicating that LL-37 binds directly to A . baumannii . These data are representative of three independent experiments with similar results. FL1-H indicates the extent of the fluorescence intensity. (B) An immunofluorescence staining assay was performed to verify LL-37 binding to A . baumannii . In the presence of 20 μg/ml LL-37, fluorescence was observed compared to the control (without BA-LL37 treatment). Samples were observed using a Carl Zeiss AXIO IMAGER A1 microscope.

Techniques Used: Binding Assay, Flow Cytometry, Cytometry, Incubation, Fluorescence, Immunofluorescence, Staining, Microscopy

5) Product Images from "Sclerotial Formation of Polyporus umbellatus by Low Temperature Treatment under Artificial Conditions"

Article Title: Sclerotial Formation of Polyporus umbellatus by Low Temperature Treatment under Artificial Conditions

Journal: PLoS ONE

doi: 10.1371/journal.pone.0056190

Microscopic characteristics of P. umbellatus mycelia during sclerotial formation. P. umbellatus mycelia was subjected to morphological examination using Zeiss Axio Imager A1 microscope. (A) Mycelia with little branches at 30 days of cultivation. (B) Mycelia with multiple clamp connections 60 days after inoculation. (C) Thick and slim mycelia coexited at 90 days after inoculation. (D) Slim mycelia with multiple branches after 120 days of cultivation. (E) Colorless conidia and spore-producing structures were observed at 120 days of cultivation. (F) and (G) indicated the sclerine of the conidia (red arrows). Representative images were from three independent experiments. Scale bar, 10 µm.
Figure Legend Snippet: Microscopic characteristics of P. umbellatus mycelia during sclerotial formation. P. umbellatus mycelia was subjected to morphological examination using Zeiss Axio Imager A1 microscope. (A) Mycelia with little branches at 30 days of cultivation. (B) Mycelia with multiple clamp connections 60 days after inoculation. (C) Thick and slim mycelia coexited at 90 days after inoculation. (D) Slim mycelia with multiple branches after 120 days of cultivation. (E) Colorless conidia and spore-producing structures were observed at 120 days of cultivation. (F) and (G) indicated the sclerine of the conidia (red arrows). Representative images were from three independent experiments. Scale bar, 10 µm.

Techniques Used: Microscopy

Microscopic structure of P. umbellatus artificial sclerotia at different stages of cultivation. The pictures were examined using Zeiss Axio Imager A1 microscope. (A) The cultivation of artificial sclerotia for 105 day. (B) The cultivation of artificial sclerotia for 120 days. The outermost membrane in (A) and (B) was indicated with a red arrow. (C) The cultivation of artificial sclerotia for 150 days. 1 represented the loose hyphae near the outermost membrane, 2 represented the pigmented layer, and 3 represented the thick and interwoven hyphae. Representative images were from three independent experiments. Scale bar, (A) and (B) 10 µm; (C) 20 µm.
Figure Legend Snippet: Microscopic structure of P. umbellatus artificial sclerotia at different stages of cultivation. The pictures were examined using Zeiss Axio Imager A1 microscope. (A) The cultivation of artificial sclerotia for 105 day. (B) The cultivation of artificial sclerotia for 120 days. The outermost membrane in (A) and (B) was indicated with a red arrow. (C) The cultivation of artificial sclerotia for 150 days. 1 represented the loose hyphae near the outermost membrane, 2 represented the pigmented layer, and 3 represented the thick and interwoven hyphae. Representative images were from three independent experiments. Scale bar, (A) and (B) 10 µm; (C) 20 µm.

Techniques Used: Microscopy

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Microscopy:

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Fluorescence:

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    Carl Zeiss axio imager a1 microscope
    Effects of anti-HER2 antibody BH1 and tumor necrosis factor-α on DNA synthesis and cell cycle in SK-BR-3 cells. ( A ) Effects on DNA synthesis were tested by 24-h BrdU incorporation assay. Cells were plated on coverslips in 12-well plates, treated as described in Figure 5 , and were exposed to BrdU during 24 h prior to indicated days. Nuclear BrdU was detected by indirect immunofluorescence assay. Nuclei were counterstained with DAPI, examined using Zeiss <t>Axio</t> Imager.A1 microscope. Representative photographs (3–5 frames per coverslip) were acquired. Percent BrdU incorporation was calculated after manual counting of BrdU + and BrdU - nuclei. * Denotes p-values ≤ 0.05 (BH1 vs. IgG1, BH1 + TNF-α vs. IgG1 + TNF-α). T-bars: SD. ( B - D ). Effects on cell cycle were analyzed by flow cytometry. SK-BR-3 cells were treated with 20 μg/ml BH1 or IgG isotype control antibody in the presence or absence of 1000 U/ml TNF-α. Cells were fixed on day 1 ( B ), day 3 ( C ) and day 6 ( D ), stained with propidium iodide and the cell cycle distribution was analysed with flow cytometry. Fraction of cells present in G2/M-phase (G2/M), S-phase (S) and G1-phase (G1) are shown in purple, green and orange respectively. Fraction of apoptotic cells observed as a SubG1 peak is shown in black.
    Axio Imager A1 Microscope, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 93/100, based on 346 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/axio imager a1 microscope/product/Carl Zeiss
    Average 93 stars, based on 346 article reviews
    Price from $9.99 to $1999.99
    axio imager a1 microscope - by Bioz Stars, 2020-11
    93/100 stars
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    Effects of anti-HER2 antibody BH1 and tumor necrosis factor-α on DNA synthesis and cell cycle in SK-BR-3 cells. ( A ) Effects on DNA synthesis were tested by 24-h BrdU incorporation assay. Cells were plated on coverslips in 12-well plates, treated as described in Figure 5 , and were exposed to BrdU during 24 h prior to indicated days. Nuclear BrdU was detected by indirect immunofluorescence assay. Nuclei were counterstained with DAPI, examined using Zeiss Axio Imager.A1 microscope. Representative photographs (3–5 frames per coverslip) were acquired. Percent BrdU incorporation was calculated after manual counting of BrdU + and BrdU - nuclei. * Denotes p-values ≤ 0.05 (BH1 vs. IgG1, BH1 + TNF-α vs. IgG1 + TNF-α). T-bars: SD. ( B - D ). Effects on cell cycle were analyzed by flow cytometry. SK-BR-3 cells were treated with 20 μg/ml BH1 or IgG isotype control antibody in the presence or absence of 1000 U/ml TNF-α. Cells were fixed on day 1 ( B ), day 3 ( C ) and day 6 ( D ), stained with propidium iodide and the cell cycle distribution was analysed with flow cytometry. Fraction of cells present in G2/M-phase (G2/M), S-phase (S) and G1-phase (G1) are shown in purple, green and orange respectively. Fraction of apoptotic cells observed as a SubG1 peak is shown in black.

    Journal: BMC Cancer

    Article Title: Novel anti-HER2 monoclonal antibodies: synergy and antagonism with tumor necrosis factor-?

    doi: 10.1186/1471-2407-12-450

    Figure Lengend Snippet: Effects of anti-HER2 antibody BH1 and tumor necrosis factor-α on DNA synthesis and cell cycle in SK-BR-3 cells. ( A ) Effects on DNA synthesis were tested by 24-h BrdU incorporation assay. Cells were plated on coverslips in 12-well plates, treated as described in Figure 5 , and were exposed to BrdU during 24 h prior to indicated days. Nuclear BrdU was detected by indirect immunofluorescence assay. Nuclei were counterstained with DAPI, examined using Zeiss Axio Imager.A1 microscope. Representative photographs (3–5 frames per coverslip) were acquired. Percent BrdU incorporation was calculated after manual counting of BrdU + and BrdU - nuclei. * Denotes p-values ≤ 0.05 (BH1 vs. IgG1, BH1 + TNF-α vs. IgG1 + TNF-α). T-bars: SD. ( B - D ). Effects on cell cycle were analyzed by flow cytometry. SK-BR-3 cells were treated with 20 μg/ml BH1 or IgG isotype control antibody in the presence or absence of 1000 U/ml TNF-α. Cells were fixed on day 1 ( B ), day 3 ( C ) and day 6 ( D ), stained with propidium iodide and the cell cycle distribution was analysed with flow cytometry. Fraction of cells present in G2/M-phase (G2/M), S-phase (S) and G1-phase (G1) are shown in purple, green and orange respectively. Fraction of apoptotic cells observed as a SubG1 peak is shown in black.

    Article Snippet: Nuclei were counterstained with DAPI and cells were observed using Zeiss Axio Imager.A1 microscope (Jena, Germany).

    Techniques: DNA Synthesis, BrdU Incorporation Assay, Immunofluorescence, Microscopy, Flow Cytometry, Cytometry, Staining

    Strong binding of anti-HER2 antibodies to ERBB2 -amplified breast cancer cell lines. ERRB2 amplification was analyzed by FISH analysis. Cells were harvested at confluence, fixed and subjected to dual-color FISH using Texas Red-labeled ERBB2 (red) and FITC-labeled chromosome 17 α-satellite CEP17 (green) DNA probes (left panel). For generation of anti-HER2 monoclonal antibodies, mice were immunized with SK-BR-3 cells, followed by a recombinant protein composed of extracellular domain of HER2 fused to human IgG1 Fc domain (HER2 ECD). Antibodies were purified from conditioned hybridoma cell culture media by affinity chromatography. For immunofluorescence assay, cells were seeded on coverslips in 6-well plates, incubated 36 h in cell culture medium, fixed, and permeabilized. Fixed cells were incubated with anti-HER2 antibodies, and the primary antibody binding was detected using Alexa 488- conjugated anti-mouse IgG (BH1, BH2, BH5, BH6, BH7 panels; green). Nuclei were counterstained with DAPI (blue) and pictures were acquired using Zeiss Axio Imager.A1 microscope.

    Journal: BMC Cancer

    Article Title: Novel anti-HER2 monoclonal antibodies: synergy and antagonism with tumor necrosis factor-?

    doi: 10.1186/1471-2407-12-450

    Figure Lengend Snippet: Strong binding of anti-HER2 antibodies to ERBB2 -amplified breast cancer cell lines. ERRB2 amplification was analyzed by FISH analysis. Cells were harvested at confluence, fixed and subjected to dual-color FISH using Texas Red-labeled ERBB2 (red) and FITC-labeled chromosome 17 α-satellite CEP17 (green) DNA probes (left panel). For generation of anti-HER2 monoclonal antibodies, mice were immunized with SK-BR-3 cells, followed by a recombinant protein composed of extracellular domain of HER2 fused to human IgG1 Fc domain (HER2 ECD). Antibodies were purified from conditioned hybridoma cell culture media by affinity chromatography. For immunofluorescence assay, cells were seeded on coverslips in 6-well plates, incubated 36 h in cell culture medium, fixed, and permeabilized. Fixed cells were incubated with anti-HER2 antibodies, and the primary antibody binding was detected using Alexa 488- conjugated anti-mouse IgG (BH1, BH2, BH5, BH6, BH7 panels; green). Nuclei were counterstained with DAPI (blue) and pictures were acquired using Zeiss Axio Imager.A1 microscope.

    Article Snippet: Nuclei were counterstained with DAPI and cells were observed using Zeiss Axio Imager.A1 microscope (Jena, Germany).

    Techniques: Binding Assay, Amplification, Fluorescence In Situ Hybridization, Labeling, Mouse Assay, Recombinant, Purification, Cell Culture, Affinity Chromatography, Immunofluorescence, Incubation, Microscopy