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rabbit polyclonal anti p rb s780  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc rabbit polyclonal anti p rb s780
    KEY RESOURCES TABLE
    Rabbit Polyclonal Anti P Rb S780, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 872 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+p+rb/Phospho-Rb+(Ser780)+Antibody/pmc06230553-15-0-5
    Average 96 stars, based on 872 article reviews
    rabbit polyclonal anti p rb s780 - by Bioz Stars, 2026-10
    96/100 stars

    Images

    1) Product Images from "β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4"

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4

    Journal: Molecular cell

    doi: 10.1016/j.molcel.2018.07.036

    KEY RESOURCES TABLE
    Figure Legend Snippet: KEY RESOURCES TABLE

    Techniques Used: Recombinant, Magnetic Beads, Staining, cDNA Synthesis, Colorimetric Assay, Enzyme-linked Immunosorbent Assay, CRISPR, Software, Microscopy

    Related Articles

    Recombinant:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.

    Magnetic Beads:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.

    Staining:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.

    cDNA Synthesis:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.

    Colorimetric Assay:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.

    Enzyme-linked Immunosorbent Assay:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.

    CRISPR:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.

    Software:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.

    Microscopy:

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4
    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat9308S; RRID: AB_331472.

    Article Title: N-terminal truncation mutations of adenomatous polyposis coli are associated with primary cilia defects.
    Article Snippet: Adenomatous polyposis coli (APC) gene is a tumor suppressor gene and its truncated mutations cause a few cilia-related diseases such as Gardner’s syndrome.. However, little is known about the mechanism that links APC mutations and cilia disorder.. APC mutations lead to the expression of N-terminal fragments, which have dominant effects in tumors owing to loss of the C-terminal region or a gain of function.



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    Direct comparison of exon skipping efficiencies of LNA/2′ O Me chimeras and corresponding 2′ O Me analogues in vivo. ( A ) RT-PCR analysis of unskipped (+Ex) and exon 23-skipped (-Ex) <t>dystrophin</t> mRNAs in TA muscles of mdx mice treated with an equimolar dose (4.35 nmol) of the indicated AON or saline only (representative image shown). Dystrophin expression in a WT control is also shown. Quantification of exon 23-skipped mRNA is expressed as the percentage of total dystrophin mRNA. n = 3–4 mice per group; values are mean ± SD. Square brackets and asterisks indicate statistically significant differences using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment. * denotes p ≤ 0.05 and ** denotes p ≤ 0.01. ( B ) Detection of exon 23-skipped dystrophin mRNA in TA muscles of mdx mice injected with an equimolar dose of a scrambled LNA/2′ O Me sequence (n = 2). The contralateral TA was injected with saline only. Positive exon skipping control AONs (LNA-6 and sLNA-5) and a WT control mouse are also shown. ( C ) Percentage exon 23 skipping in isolated primary mdx myoblasts treated with increasing concentrations of 20mer LNA-6 AON (30% LNAs). RNA extraction was carried out 24 h post transfection. Values are mean ± SD from three independent transfection experiments.
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    Image Search Results


    Direct comparison of exon skipping efficiencies of LNA/2′ O Me chimeras and corresponding 2′ O Me analogues in vivo. ( A ) RT-PCR analysis of unskipped (+Ex) and exon 23-skipped (-Ex) dystrophin mRNAs in TA muscles of mdx mice treated with an equimolar dose (4.35 nmol) of the indicated AON or saline only (representative image shown). Dystrophin expression in a WT control is also shown. Quantification of exon 23-skipped mRNA is expressed as the percentage of total dystrophin mRNA. n = 3–4 mice per group; values are mean ± SD. Square brackets and asterisks indicate statistically significant differences using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment. * denotes p ≤ 0.05 and ** denotes p ≤ 0.01. ( B ) Detection of exon 23-skipped dystrophin mRNA in TA muscles of mdx mice injected with an equimolar dose of a scrambled LNA/2′ O Me sequence (n = 2). The contralateral TA was injected with saline only. Positive exon skipping control AONs (LNA-6 and sLNA-5) and a WT control mouse are also shown. ( C ) Percentage exon 23 skipping in isolated primary mdx myoblasts treated with increasing concentrations of 20mer LNA-6 AON (30% LNAs). RNA extraction was carried out 24 h post transfection. Values are mean ± SD from three independent transfection experiments.

    Journal: Pharmaceuticals

    Article Title: Intramuscular Evaluation of Chimeric Locked Nucleic Acid/2′ O Methyl-Modified Antisense Oligonucleotides for Targeted Exon 23 Skipping in Mdx Mice

    doi: 10.3390/ph14111113

    Figure Lengend Snippet: Direct comparison of exon skipping efficiencies of LNA/2′ O Me chimeras and corresponding 2′ O Me analogues in vivo. ( A ) RT-PCR analysis of unskipped (+Ex) and exon 23-skipped (-Ex) dystrophin mRNAs in TA muscles of mdx mice treated with an equimolar dose (4.35 nmol) of the indicated AON or saline only (representative image shown). Dystrophin expression in a WT control is also shown. Quantification of exon 23-skipped mRNA is expressed as the percentage of total dystrophin mRNA. n = 3–4 mice per group; values are mean ± SD. Square brackets and asterisks indicate statistically significant differences using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment. * denotes p ≤ 0.05 and ** denotes p ≤ 0.01. ( B ) Detection of exon 23-skipped dystrophin mRNA in TA muscles of mdx mice injected with an equimolar dose of a scrambled LNA/2′ O Me sequence (n = 2). The contralateral TA was injected with saline only. Positive exon skipping control AONs (LNA-6 and sLNA-5) and a WT control mouse are also shown. ( C ) Percentage exon 23 skipping in isolated primary mdx myoblasts treated with increasing concentrations of 20mer LNA-6 AON (30% LNAs). RNA extraction was carried out 24 h post transfection. Values are mean ± SD from three independent transfection experiments.

    Article Snippet: Transverse cryosections of 7 μm thickness were examined for dystrophin expression using a rabbit polyclonal anti-dystrophin antibody (1:400 dilution, RB-9024-P Thermo Scientific), which was detected using the Alexa Fluor 594 goat anti-rabbit antibody (molecular probes ref 37117).

    Techniques: Comparison, Analogues, In Vivo, Reverse Transcription Polymerase Chain Reaction, Muscles, Saline, Expressing, Control, Injection, Sequencing, Isolation, RNA Extraction, Transfection

    Evaluation of dystrophin restoration by immunofluorescence. ( A ) Representative images of dystrophin immunostaining on transverse muscle cryosections from a WT control and mdx mice treated with an intramuscular injection of the indicated AONs or saline only (mdx; scale bar = 100 µm). ( B ) Quantification of the number of dystrophin positive fibres, expressed as a percentage of the WT, in TA muscle cross sections from mdx mice treated with an intramuscular injection of the indicated AONs. n = 3 mice per group; values are mean ± SD. Square brackets and asterisks indicate statistically significant differences using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment. * denotes p ≤ 0.05 and ** denotes p ≤ 0.01.

    Journal: Pharmaceuticals

    Article Title: Intramuscular Evaluation of Chimeric Locked Nucleic Acid/2′ O Methyl-Modified Antisense Oligonucleotides for Targeted Exon 23 Skipping in Mdx Mice

    doi: 10.3390/ph14111113

    Figure Lengend Snippet: Evaluation of dystrophin restoration by immunofluorescence. ( A ) Representative images of dystrophin immunostaining on transverse muscle cryosections from a WT control and mdx mice treated with an intramuscular injection of the indicated AONs or saline only (mdx; scale bar = 100 µm). ( B ) Quantification of the number of dystrophin positive fibres, expressed as a percentage of the WT, in TA muscle cross sections from mdx mice treated with an intramuscular injection of the indicated AONs. n = 3 mice per group; values are mean ± SD. Square brackets and asterisks indicate statistically significant differences using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment. * denotes p ≤ 0.05 and ** denotes p ≤ 0.01.

    Article Snippet: Transverse cryosections of 7 μm thickness were examined for dystrophin expression using a rabbit polyclonal anti-dystrophin antibody (1:400 dilution, RB-9024-P Thermo Scientific), which was detected using the Alexa Fluor 594 goat anti-rabbit antibody (molecular probes ref 37117).

    Techniques: Immunofluorescence, Immunostaining, Control, Injection, Saline

    Targeted MS quantification of total dystrophin protein in WT and AON-treated mdx TA muscles. ( A ) Quantification of the IFLTEQPLEGLEK peptide in WT protein concentration standards (10, 50 and 100%) showing the peak area values of its three product ions (y11+, y10+ and y7+). The peak area of each product ion, as well as the sum peak area of all three transitions (last column), increase proportionally to the concentration of the WT standard (table values and bar chart). ( B ) Quantification of dystrophin expression, plotted as a percentage of the WT, in TA muscles of mdx mice after intramuscular delivery with the indicated AONs. n = 3 mice per group; values are mean ± SD. Square brackets and asterisks indicate pairwise p -values ≤ 0.05 using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment.

    Journal: Pharmaceuticals

    Article Title: Intramuscular Evaluation of Chimeric Locked Nucleic Acid/2′ O Methyl-Modified Antisense Oligonucleotides for Targeted Exon 23 Skipping in Mdx Mice

    doi: 10.3390/ph14111113

    Figure Lengend Snippet: Targeted MS quantification of total dystrophin protein in WT and AON-treated mdx TA muscles. ( A ) Quantification of the IFLTEQPLEGLEK peptide in WT protein concentration standards (10, 50 and 100%) showing the peak area values of its three product ions (y11+, y10+ and y7+). The peak area of each product ion, as well as the sum peak area of all three transitions (last column), increase proportionally to the concentration of the WT standard (table values and bar chart). ( B ) Quantification of dystrophin expression, plotted as a percentage of the WT, in TA muscles of mdx mice after intramuscular delivery with the indicated AONs. n = 3 mice per group; values are mean ± SD. Square brackets and asterisks indicate pairwise p -values ≤ 0.05 using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment.

    Article Snippet: Transverse cryosections of 7 μm thickness were examined for dystrophin expression using a rabbit polyclonal anti-dystrophin antibody (1:400 dilution, RB-9024-P Thermo Scientific), which was detected using the Alexa Fluor 594 goat anti-rabbit antibody (molecular probes ref 37117).

    Techniques: Muscles, Protein Concentration, Concentration Assay, Expressing

    WB quantification of total dystrophin protein in WT and AON-treated mdx TA muscles. ( A ) A four-point standard curve for WT dystrophin was created, with concentration range of 2.5 to 20%, by spiking pooled WT protein extracts into pooled mdx lysates to maintain equal loading of protein (100 μg). The dystrophin signal (bottom bands in top gel; n.s. = non-specific band) normalized to the intensity of the vinculin signal (bottom gel) was graphed in linear format. The identified equation and R2 value of the linear regression analysis are shown on the graph. ( B ) Detection and quantification of total dystrophin protein in TA muscles of mdx mice, 2 weeks after intramuscular injection with the indicated AONs (representative image shown). To minimize saturation issues on the gel, the dystrophin band signal in the WT lane corresponds to only 10 μg of loaded protein (i.e., 10% of total protein extract loaded for saline and AON-treated samples). Dystrophin band signals were normalised to the intensity of the respective vinculin signals and the amount of rescued protein, expressed as a percentage of the WT, was calculated using the equation identified in the linear regression analysis. n = 3 mice per group; values are mean ± SD. Square brackets and asterisks indicate pairwise p -values ≤ 0.05 using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment.

    Journal: Pharmaceuticals

    Article Title: Intramuscular Evaluation of Chimeric Locked Nucleic Acid/2′ O Methyl-Modified Antisense Oligonucleotides for Targeted Exon 23 Skipping in Mdx Mice

    doi: 10.3390/ph14111113

    Figure Lengend Snippet: WB quantification of total dystrophin protein in WT and AON-treated mdx TA muscles. ( A ) A four-point standard curve for WT dystrophin was created, with concentration range of 2.5 to 20%, by spiking pooled WT protein extracts into pooled mdx lysates to maintain equal loading of protein (100 μg). The dystrophin signal (bottom bands in top gel; n.s. = non-specific band) normalized to the intensity of the vinculin signal (bottom gel) was graphed in linear format. The identified equation and R2 value of the linear regression analysis are shown on the graph. ( B ) Detection and quantification of total dystrophin protein in TA muscles of mdx mice, 2 weeks after intramuscular injection with the indicated AONs (representative image shown). To minimize saturation issues on the gel, the dystrophin band signal in the WT lane corresponds to only 10 μg of loaded protein (i.e., 10% of total protein extract loaded for saline and AON-treated samples). Dystrophin band signals were normalised to the intensity of the respective vinculin signals and the amount of rescued protein, expressed as a percentage of the WT, was calculated using the equation identified in the linear regression analysis. n = 3 mice per group; values are mean ± SD. Square brackets and asterisks indicate pairwise p -values ≤ 0.05 using Dunn’s multiple comparisons test followed by Benjamini–Hochberg adjustment.

    Article Snippet: Transverse cryosections of 7 μm thickness were examined for dystrophin expression using a rabbit polyclonal anti-dystrophin antibody (1:400 dilution, RB-9024-P Thermo Scientific), which was detected using the Alexa Fluor 594 goat anti-rabbit antibody (molecular probes ref 37117).

    Techniques: Muscles, Concentration Assay, Injection, Saline

    KEY RESOURCES TABLE

    Journal: Molecular cell

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4

    doi: 10.1016/j.molcel.2018.07.036

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Rabbit polyclonal anti-p-RB (S780) , Cell Signaling , Cat#9307S; RRID: AB_330015.

    Techniques: Recombinant, Magnetic Beads, Staining, cDNA Synthesis, Colorimetric Assay, Enzyme-linked Immunosorbent Assay, CRISPR, Software, Microscopy

    KEY RESOURCES TABLE

    Journal: Molecular cell

    Article Title: β-Hydroxybutyrate prevents vascular senescence through hnRNP A1-mediated upregulation of Oct 4

    doi: 10.1016/j.molcel.2018.07.036

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Rabbit polyclonal anti-p-RB (S807, S811) , Cell Signaling , Cat#9308S; RRID: AB_331472.

    Techniques: Recombinant, Magnetic Beads, Staining, cDNA Synthesis, Colorimetric Assay, Enzyme-linked Immunosorbent Assay, CRISPR, Software, Microscopy

    Illustration of the proposed multifunctional anti-HER2 gold nanoshell with HER2 receptor targeting and photothermal therapy

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Pulsed-laser irradiation of multifunctional gold nanoshells to overcome trastuzumab resistance in HER2-overexpressing breast cancer

    doi: 10.1186/s13046-019-1305-x

    Figure Lengend Snippet: Illustration of the proposed multifunctional anti-HER2 gold nanoshell with HER2 receptor targeting and photothermal therapy

    Article Snippet: Anti-human HER2 rabbit polyclonal antibody (RB-9040-P) was purchased from Fisher Scientific.

    Techniques:

    a Diagram showing steps in anti-HER2 gold nanoshell (GN) synthesis with corresponding TEM images. b UV-Vis absorption spectra of anti-HER2 GNs. c HER2 gene copy number, mRNA expression and immunostaining (brown) for BT474-R cell line (* P < 0.05). d Immunostaining of BT474-R cells incubated with trastuzumab-FITC (green, left panel). Dark field images of BT474-R cells incubated with anti-HER2 gold nanoshells (right panel)

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Pulsed-laser irradiation of multifunctional gold nanoshells to overcome trastuzumab resistance in HER2-overexpressing breast cancer

    doi: 10.1186/s13046-019-1305-x

    Figure Lengend Snippet: a Diagram showing steps in anti-HER2 gold nanoshell (GN) synthesis with corresponding TEM images. b UV-Vis absorption spectra of anti-HER2 GNs. c HER2 gene copy number, mRNA expression and immunostaining (brown) for BT474-R cell line (* P < 0.05). d Immunostaining of BT474-R cells incubated with trastuzumab-FITC (green, left panel). Dark field images of BT474-R cells incubated with anti-HER2 gold nanoshells (right panel)

    Article Snippet: Anti-human HER2 rabbit polyclonal antibody (RB-9040-P) was purchased from Fisher Scientific.

    Techniques: Expressing, Immunostaining, Incubation

    a Kinetic bio-distribution of anti-HER2 gold nanoshells (GNs) after intravenous administration of 3.5 × 10 13 nanoshells in mice using magnetic resonance imaging (MRI). Results are expressed as percentages of initial signal variations (ΔSI), each signal intensity being compared with a pre-contrast signal. b Absolute gold concentration in blood and tissue samples after intravenous administration of 3.5 × 10 13 anti-HER2 GNs using ICP-MS. Data is expressed as mean ± standard deviation, and comparisons between the liver and spleen concentrations were made using Student’s t-test (* P < 0.05). c Dark field images of tissue sections obtained from the liver and spleen after injection of anti-HER2 GNs. d TEM images of anti-HER2 GNs internalized in liver and spleen cells

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Pulsed-laser irradiation of multifunctional gold nanoshells to overcome trastuzumab resistance in HER2-overexpressing breast cancer

    doi: 10.1186/s13046-019-1305-x

    Figure Lengend Snippet: a Kinetic bio-distribution of anti-HER2 gold nanoshells (GNs) after intravenous administration of 3.5 × 10 13 nanoshells in mice using magnetic resonance imaging (MRI). Results are expressed as percentages of initial signal variations (ΔSI), each signal intensity being compared with a pre-contrast signal. b Absolute gold concentration in blood and tissue samples after intravenous administration of 3.5 × 10 13 anti-HER2 GNs using ICP-MS. Data is expressed as mean ± standard deviation, and comparisons between the liver and spleen concentrations were made using Student’s t-test (* P < 0.05). c Dark field images of tissue sections obtained from the liver and spleen after injection of anti-HER2 GNs. d TEM images of anti-HER2 GNs internalized in liver and spleen cells

    Article Snippet: Anti-human HER2 rabbit polyclonal antibody (RB-9040-P) was purchased from Fisher Scientific.

    Techniques: Magnetic Resonance Imaging, Concentration Assay, Standard Deviation, Injection

    a T2-weighted magnetic resonance imaging of one xenografted tumor (circle) before and 72 h after intravenous administration of 3.5 × 10 13 non-functionalized gold nanoshells (GNs) or anti-HER2 GNs, with corresponding histograms for percentage of signal initial variations (ΔSI). Each signal intensity is compared with a pre-contrast signal. b Absolute gold concentration in xenografted tumor over time after intravenous administration of non-functionalized gold nanoshells (GNs) or of 3.5 × 10 13 anti-HER2 GNs using ICP-MS. Data is expressed as mean ± standard deviation, and comparisons between mice injected with non-functionalized GNs or with anti-HER2 GNs were made using Student’s t-test (* P < 0.05). c Dark field images of tumor sections at 72 h after injection of GNs. d TEM images of tumors at 72 h showing the presence of GNs within the cytoplasm of cancer cells. e Merged dark field images with immunofluorescence staining of human xenografted tumors 72 h after injection of anti-HER2 GNs, using anti-Cytokeratin (red) or anti-CD31 (green) antibodies (T: tumor; V: microvessel)

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Pulsed-laser irradiation of multifunctional gold nanoshells to overcome trastuzumab resistance in HER2-overexpressing breast cancer

    doi: 10.1186/s13046-019-1305-x

    Figure Lengend Snippet: a T2-weighted magnetic resonance imaging of one xenografted tumor (circle) before and 72 h after intravenous administration of 3.5 × 10 13 non-functionalized gold nanoshells (GNs) or anti-HER2 GNs, with corresponding histograms for percentage of signal initial variations (ΔSI). Each signal intensity is compared with a pre-contrast signal. b Absolute gold concentration in xenografted tumor over time after intravenous administration of non-functionalized gold nanoshells (GNs) or of 3.5 × 10 13 anti-HER2 GNs using ICP-MS. Data is expressed as mean ± standard deviation, and comparisons between mice injected with non-functionalized GNs or with anti-HER2 GNs were made using Student’s t-test (* P < 0.05). c Dark field images of tumor sections at 72 h after injection of GNs. d TEM images of tumors at 72 h showing the presence of GNs within the cytoplasm of cancer cells. e Merged dark field images with immunofluorescence staining of human xenografted tumors 72 h after injection of anti-HER2 GNs, using anti-Cytokeratin (red) or anti-CD31 (green) antibodies (T: tumor; V: microvessel)

    Article Snippet: Anti-human HER2 rabbit polyclonal antibody (RB-9040-P) was purchased from Fisher Scientific.

    Techniques: Magnetic Resonance Imaging, Concentration Assay, Standard Deviation, Injection, Immunofluorescence, Staining

    a Human xenografted tumor growth curves using mice grafted with trastuzumab-resistant HER2-overexpressing BT474-R cell lines. For each treatment group (non-irradiated tumors, irradiated tumors after intravenous administration of non-functionalized GNs, and irradiated tumors after intravenous administration of anti-HER2 GNs), 10 xenografted mice are used. Comparisons between the three treatment groups are made using ANOVA (* P < 0.05, *** P < 0.001). b Quantitative comparisons of tumor necrosis (N), cell proliferation, cell apoptosis and microvessel density between irradiated and non-irradiated tumors. Comparisons between groups are made using Student’s t-test (* P < 0.05, ** P < 0.01). c Double immunofluorescence staining of irradiated human xenografted tumor using anti-cleaved-caspase3 and anti-CD31 antibodies (T: tumor; V: microvessel)

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Pulsed-laser irradiation of multifunctional gold nanoshells to overcome trastuzumab resistance in HER2-overexpressing breast cancer

    doi: 10.1186/s13046-019-1305-x

    Figure Lengend Snippet: a Human xenografted tumor growth curves using mice grafted with trastuzumab-resistant HER2-overexpressing BT474-R cell lines. For each treatment group (non-irradiated tumors, irradiated tumors after intravenous administration of non-functionalized GNs, and irradiated tumors after intravenous administration of anti-HER2 GNs), 10 xenografted mice are used. Comparisons between the three treatment groups are made using ANOVA (* P < 0.05, *** P < 0.001). b Quantitative comparisons of tumor necrosis (N), cell proliferation, cell apoptosis and microvessel density between irradiated and non-irradiated tumors. Comparisons between groups are made using Student’s t-test (* P < 0.05, ** P < 0.01). c Double immunofluorescence staining of irradiated human xenografted tumor using anti-cleaved-caspase3 and anti-CD31 antibodies (T: tumor; V: microvessel)

    Article Snippet: Anti-human HER2 rabbit polyclonal antibody (RB-9040-P) was purchased from Fisher Scientific.

    Techniques: Irradiation, Double Immunofluorescence Staining