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    Cell Signaling Technology Inc anti brd9 rabbit
    a Signature analysis of six BRD-containing proteins that have been associated with homologous recombination (HR)-related mutation signatures (signature 3) in ovarian cancer in the TCGA database. p Values were calculated by one-sided Fisher Exact test. b Quantification of HR- and NHEJ-mediated DSB repair as assessed using GFP reporter assay in HCT-116 cells following knockdown of bromodomain-containing proteins. The indicated bromodomain-containing proteins were individually knocked down in HCT-116 cells transfected with GFP-tagged reporter plasmid. Thirty-six hours later, repair efficiency was assessed using flow cytometry. The BRCA1- and 53BP1-knockdown cells were used as positive control for HR and NHEJ, respectively. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples; * p < 0.05, ** p < 0.005, *** p < 0.001 by two-sided unpaired t test. c , d Knockdown of <t>BRD9</t> causes HR but not NHEJ deficiency. OVCAR8 cells were infected with lentivirus expressing the indicated BRD9 shRNAs. Thirty-six hours later, HR- ( c ) and NHEJ- ( d ) mediated repair capacity was assessed using flow cytometry. The BRCA1 and 53BP1 shRNAs were used as positive controls for HR and NHEJ, respectively. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, ** p < 0.01, *** p < 0.001 by two-sided unpaired t test. e , f BRD9 inhibitor (I-BRD9) selectively inhibits HR and not NHEJ activity. OVCAR8 cells were treated with 10 or 20 µM I-BRD9 for 36 h, and then subjected to HR ( e ) and NHEJ ( f ) assay as described in c , d . Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, ** p < 0.01, *** p < 0.001 by two-sided unpaired t test. g – j Knockdown of BRD9 delays clearance of γ-H2AX and RAD51 foci. OVCAR8 cells were infected with lentivirus-expressing control (Ctrl) or BRD9 shRNA. Cells were exposed to 2-Gy irradiation and fixed at the indicated time points. Cells were stained for the indicated foci. g , i Representative images are shown of γ-H2AX and Rad51 foci after the indicated treatments and indicated time following 2-Gy irradiation. h , j γ-H2AX and Rad51 foci in OVCAR8 cells after the indicated treatment and time following 2-Gy irradiation were quantified. Representative data (mean ± SEM) are shown from three independent experiments. *** p < 0.001 by two-sided unpaired t test. Scale bar, 10 μm.
    Anti Brd9 Rabbit, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a Signature analysis of six BRD-containing proteins that have been associated with homologous recombination (HR)-related mutation signatures (signature 3) in ovarian cancer in the TCGA database. p Values were calculated by one-sided Fisher Exact test. b Quantification of HR- and NHEJ-mediated DSB repair as assessed using GFP reporter assay in HCT-116 cells following knockdown of bromodomain-containing proteins. The indicated bromodomain-containing proteins were individually knocked down in HCT-116 cells transfected with GFP-tagged reporter plasmid. Thirty-six hours later, repair efficiency was assessed using flow cytometry. The BRCA1- and 53BP1-knockdown cells were used as positive control for HR and NHEJ, respectively. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples; * p < 0.05, ** p < 0.005, *** p < 0.001 by two-sided unpaired t test. c , d Knockdown of BRD9 causes HR but not NHEJ deficiency. OVCAR8 cells were infected with lentivirus expressing the indicated BRD9 shRNAs. Thirty-six hours later, HR- ( c ) and NHEJ- ( d ) mediated repair capacity was assessed using flow cytometry. The BRCA1 and 53BP1 shRNAs were used as positive controls for HR and NHEJ, respectively. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, ** p < 0.01, *** p < 0.001 by two-sided unpaired t test. e , f BRD9 inhibitor (I-BRD9) selectively inhibits HR and not NHEJ activity. OVCAR8 cells were treated with 10 or 20 µM I-BRD9 for 36 h, and then subjected to HR ( e ) and NHEJ ( f ) assay as described in c , d . Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, ** p < 0.01, *** p < 0.001 by two-sided unpaired t test. g – j Knockdown of BRD9 delays clearance of γ-H2AX and RAD51 foci. OVCAR8 cells were infected with lentivirus-expressing control (Ctrl) or BRD9 shRNA. Cells were exposed to 2-Gy irradiation and fixed at the indicated time points. Cells were stained for the indicated foci. g , i Representative images are shown of γ-H2AX and Rad51 foci after the indicated treatments and indicated time following 2-Gy irradiation. h , j γ-H2AX and Rad51 foci in OVCAR8 cells after the indicated treatment and time following 2-Gy irradiation were quantified. Representative data (mean ± SEM) are shown from three independent experiments. *** p < 0.001 by two-sided unpaired t test. Scale bar, 10 μm.

    Journal: Nature Communications

    Article Title: The bromodomain containing protein BRD-9 orchestrates RAD51–RAD54 complex formation and regulates homologous recombination-mediated repair

    doi: 10.1038/s41467-020-16443-x

    Figure Lengend Snippet: a Signature analysis of six BRD-containing proteins that have been associated with homologous recombination (HR)-related mutation signatures (signature 3) in ovarian cancer in the TCGA database. p Values were calculated by one-sided Fisher Exact test. b Quantification of HR- and NHEJ-mediated DSB repair as assessed using GFP reporter assay in HCT-116 cells following knockdown of bromodomain-containing proteins. The indicated bromodomain-containing proteins were individually knocked down in HCT-116 cells transfected with GFP-tagged reporter plasmid. Thirty-six hours later, repair efficiency was assessed using flow cytometry. The BRCA1- and 53BP1-knockdown cells were used as positive control for HR and NHEJ, respectively. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples; * p < 0.05, ** p < 0.005, *** p < 0.001 by two-sided unpaired t test. c , d Knockdown of BRD9 causes HR but not NHEJ deficiency. OVCAR8 cells were infected with lentivirus expressing the indicated BRD9 shRNAs. Thirty-six hours later, HR- ( c ) and NHEJ- ( d ) mediated repair capacity was assessed using flow cytometry. The BRCA1 and 53BP1 shRNAs were used as positive controls for HR and NHEJ, respectively. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, ** p < 0.01, *** p < 0.001 by two-sided unpaired t test. e , f BRD9 inhibitor (I-BRD9) selectively inhibits HR and not NHEJ activity. OVCAR8 cells were treated with 10 or 20 µM I-BRD9 for 36 h, and then subjected to HR ( e ) and NHEJ ( f ) assay as described in c , d . Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, ** p < 0.01, *** p < 0.001 by two-sided unpaired t test. g – j Knockdown of BRD9 delays clearance of γ-H2AX and RAD51 foci. OVCAR8 cells were infected with lentivirus-expressing control (Ctrl) or BRD9 shRNA. Cells were exposed to 2-Gy irradiation and fixed at the indicated time points. Cells were stained for the indicated foci. g , i Representative images are shown of γ-H2AX and Rad51 foci after the indicated treatments and indicated time following 2-Gy irradiation. h , j γ-H2AX and Rad51 foci in OVCAR8 cells after the indicated treatment and time following 2-Gy irradiation were quantified. Representative data (mean ± SEM) are shown from three independent experiments. *** p < 0.001 by two-sided unpaired t test. Scale bar, 10 μm.

    Article Snippet: Anti-BRD9 (rabbit) and anti-53BP1 (rabbit) for IF was homemade; anti-SMARCC1 (11956 rabbit), anti-BRG1 (3508 rabbit), anti-BAF250 (12354 rabbit), and anti-BRM (11966 rabbit) for WB (1:1000) were purchased from Cell Signaling Technology.

    Techniques: Homologous Recombination, Mutagenesis, Reporter Assay, Transfection, Plasmid Preparation, Flow Cytometry, Positive Control, Infection, Expressing, Activity Assay, shRNA, Irradiation, Staining

    a – d Representative immunofluorescence images of OVCAR8 cells demonstrating that BRD9 knockdown reduces RAD54 foci formation and RAD51/RAD54 co-localization. a – c OVCAR8 cells were infected with lentivirus-expressing control (Ctrl) or BRD9 shRNA and exposed to 2-Gy IR. Eight hours later, cells were stained with RAD51 (red) and RAD54 (green) antibodies. Representative immunofluorescence images are shown in a . RAD51 foci/cell ( b ), RAD54 foci/cell ( c ), and RAD51/RAD54 co-localized foci ( d ) after the indicated treatment were quantified. Representative data (mean ± SEM) are shown from three independent experiments. n = 50 cells examined over three independent experiments. *** p < 0.001 by two-sided unpaired t test. Scale bar, 10 μm. e , f DNA damage-induced RAD51–RAD54 interaction is dependent on BRD9. Endogenous BRD9 was knocked out in HEK293T cells using shRNA, and the indicated constructs were expressed. Cells were exposed to 10-Gy irradiation. Lysates were collected after 8 h, and immunoprecipitation with the indicated antibodies was performed. Blots were probed with the indicated antibodies. g RAD51 is necessary for BRD9 foci formation. OVCAR8 cells were infected with lentivirus-expressing RAD51 shRNA, exposed to 2-Gy IR, and fixed after 8 h. Cells were stained with BRD9 (green) and RAD51 (red) antibodies. Representative images of the indicated foci are shown. BRD9 foci/cell were quantified. Representative data (mean ± SEM) are shown from three independent experiments. n = 50 cells examined over three independent experiments. *** p < 0.001 by two-sided unpaired t test. Scale bar, 10 μm.

    Journal: Nature Communications

    Article Title: The bromodomain containing protein BRD-9 orchestrates RAD51–RAD54 complex formation and regulates homologous recombination-mediated repair

    doi: 10.1038/s41467-020-16443-x

    Figure Lengend Snippet: a – d Representative immunofluorescence images of OVCAR8 cells demonstrating that BRD9 knockdown reduces RAD54 foci formation and RAD51/RAD54 co-localization. a – c OVCAR8 cells were infected with lentivirus-expressing control (Ctrl) or BRD9 shRNA and exposed to 2-Gy IR. Eight hours later, cells were stained with RAD51 (red) and RAD54 (green) antibodies. Representative immunofluorescence images are shown in a . RAD51 foci/cell ( b ), RAD54 foci/cell ( c ), and RAD51/RAD54 co-localized foci ( d ) after the indicated treatment were quantified. Representative data (mean ± SEM) are shown from three independent experiments. n = 50 cells examined over three independent experiments. *** p < 0.001 by two-sided unpaired t test. Scale bar, 10 μm. e , f DNA damage-induced RAD51–RAD54 interaction is dependent on BRD9. Endogenous BRD9 was knocked out in HEK293T cells using shRNA, and the indicated constructs were expressed. Cells were exposed to 10-Gy irradiation. Lysates were collected after 8 h, and immunoprecipitation with the indicated antibodies was performed. Blots were probed with the indicated antibodies. g RAD51 is necessary for BRD9 foci formation. OVCAR8 cells were infected with lentivirus-expressing RAD51 shRNA, exposed to 2-Gy IR, and fixed after 8 h. Cells were stained with BRD9 (green) and RAD51 (red) antibodies. Representative images of the indicated foci are shown. BRD9 foci/cell were quantified. Representative data (mean ± SEM) are shown from three independent experiments. n = 50 cells examined over three independent experiments. *** p < 0.001 by two-sided unpaired t test. Scale bar, 10 μm.

    Article Snippet: Anti-BRD9 (rabbit) and anti-53BP1 (rabbit) for IF was homemade; anti-SMARCC1 (11956 rabbit), anti-BRG1 (3508 rabbit), anti-BAF250 (12354 rabbit), and anti-BRM (11966 rabbit) for WB (1:1000) were purchased from Cell Signaling Technology.

    Techniques: Immunofluorescence, Infection, Expressing, shRNA, Staining, Construct, Irradiation, Immunoprecipitation

    a , b BRD9 interacts with RAD54 and RAD51. a 293T cells were transfected with HA-tagged BRD9 plasmid. Forty-eight hours after transfection, cells were exposed to 10-Gy IR and collected at the indicated time points. Immunoprecipitation with anti-HA beads was performed. Blots were probed with the indicated antibodies. b OVCAR8 cells were exposed to 10-Gy IR. Lysates were collected after 8 h, and co-immunoprecipitation with anti-BRD9 antibody was performed. Blots were probed with the indicated antibodies. c – g BRD9 interacts with RAD51 through the C terminus, and its bromodomain mediates its interaction with RAD54. c Schematic diagram depicting a set of HA-tagged BRD9 expression constructs. d 293T cells were transfected with the indicated constructs of HA-BRD9 and exposed to 10-Gy IR. Lysates were collected after 8 h. Immunoprecipitation with anti-HA beads was performed. Blots were probed with the indicated antibodies. e 293T cells were transfected with the indicated constructs. Forty-eight hours later, cells were treated with 10-Gy IR 8 h before immunoprecipitation with anti-HA beads. Blots were probed with indicated antibodies. f , g 293T cells were transfected with the indicated constructs. Twenty-four hours later, cells were exposed to BRD9i, 10-Gy IR, or both. Lysates were collected after 8 h. Immunoprecipitation with anti-HA beads was performed. Blots were probed with the indicated antibodies. h , k Bromodomain of BRD9 is essential for its HR activity. h BRD9-knockdown 293T cells were infected with the indicated lentiviral plasmids. Twenty-four hours after transfection, cells were exposed to IR. Lysates were collected after 8 h, and immunoprecipitation with anti-HA beads was performed. Blots were probed with the indicated antibodies. i BRD9-knockdown 293T cells expressing the DR-GFP reporter were infected with lentivirus expressing the indicated proteins. Twenty-four hours later, cells were subjected to flow cytometry. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, *** p < 0.001 by two-sided unpaired t test. j , k BRD9-knockdown OVCAR8 cells were infected with lentivirus expressing the indicated proteins, and subjected to colony-formation assay to assess the sensitivity to PARPi ( j ) and cisplatin ( k ). Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, ** p < 0.01, *** p < 0.001 by two-sided unpaired t test.

    Journal: Nature Communications

    Article Title: The bromodomain containing protein BRD-9 orchestrates RAD51–RAD54 complex formation and regulates homologous recombination-mediated repair

    doi: 10.1038/s41467-020-16443-x

    Figure Lengend Snippet: a , b BRD9 interacts with RAD54 and RAD51. a 293T cells were transfected with HA-tagged BRD9 plasmid. Forty-eight hours after transfection, cells were exposed to 10-Gy IR and collected at the indicated time points. Immunoprecipitation with anti-HA beads was performed. Blots were probed with the indicated antibodies. b OVCAR8 cells were exposed to 10-Gy IR. Lysates were collected after 8 h, and co-immunoprecipitation with anti-BRD9 antibody was performed. Blots were probed with the indicated antibodies. c – g BRD9 interacts with RAD51 through the C terminus, and its bromodomain mediates its interaction with RAD54. c Schematic diagram depicting a set of HA-tagged BRD9 expression constructs. d 293T cells were transfected with the indicated constructs of HA-BRD9 and exposed to 10-Gy IR. Lysates were collected after 8 h. Immunoprecipitation with anti-HA beads was performed. Blots were probed with the indicated antibodies. e 293T cells were transfected with the indicated constructs. Forty-eight hours later, cells were treated with 10-Gy IR 8 h before immunoprecipitation with anti-HA beads. Blots were probed with indicated antibodies. f , g 293T cells were transfected with the indicated constructs. Twenty-four hours later, cells were exposed to BRD9i, 10-Gy IR, or both. Lysates were collected after 8 h. Immunoprecipitation with anti-HA beads was performed. Blots were probed with the indicated antibodies. h , k Bromodomain of BRD9 is essential for its HR activity. h BRD9-knockdown 293T cells were infected with the indicated lentiviral plasmids. Twenty-four hours after transfection, cells were exposed to IR. Lysates were collected after 8 h, and immunoprecipitation with anti-HA beads was performed. Blots were probed with the indicated antibodies. i BRD9-knockdown 293T cells expressing the DR-GFP reporter were infected with lentivirus expressing the indicated proteins. Twenty-four hours later, cells were subjected to flow cytometry. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, *** p < 0.001 by two-sided unpaired t test. j , k BRD9-knockdown OVCAR8 cells were infected with lentivirus expressing the indicated proteins, and subjected to colony-formation assay to assess the sensitivity to PARPi ( j ) and cisplatin ( k ). Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. * p < 0.05, ** p < 0.01, *** p < 0.001 by two-sided unpaired t test.

    Article Snippet: Anti-BRD9 (rabbit) and anti-53BP1 (rabbit) for IF was homemade; anti-SMARCC1 (11956 rabbit), anti-BRG1 (3508 rabbit), anti-BAF250 (12354 rabbit), and anti-BRM (11966 rabbit) for WB (1:1000) were purchased from Cell Signaling Technology.

    Techniques: Transfection, Plasmid Preparation, Immunoprecipitation, Expressing, Construct, Activity Assay, Infection, Flow Cytometry, Colony Assay

    a – c BRD9 is overexpressed in ovarian cancer patient samples and cell lines, and is associated with decreased patient survival. a Analysis of BRD9 expression in ovarian cancer patient samples from the TCGA database. Red indicates BRD9 amplification. b Kaplan–Meier curve showing the survival of ovarian cancer patients with low ( n = 720) and high ( n = 715) expression of BRD9. Statistical analysis with the two-sided log-rank (Mantel–Cox) test revealed statistically significant differences as shown on the graph. c Immunoblot of indicated proteins in the indicated ovarian cancer cell lines. d – g Depletion/inhibition of BRD9 sensitizes OVCAR8 cells to PARPi and cisplatin. d – f OVCAR8 cells infected with indicated shRNAs and subjected to WB assay ( d ) to assess knockdown efficiency, and colony-formation assay to assess the sensitivity to olaparib ( e ) and cisplatin ( f ). g OVCAR8 cells were exposed to olaparib and/or BRD9i and subjected to colony-formation assay. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. ** p < 0.01,*** p < 0.001 by two-sided unpaired t test. h – j Overexpression of BRD9 confers resistance to PARPi/cisplatin. OVCAR7 cells infected with the indicated lentivirus and subjected to colony-formation assay to assess the sensitivity to olaparib ( i ) and cisplatin ( j ). Protein expression was assessed by Western blot ( h ). Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. ** p < 0.01,*** p < 0.001 by two-sided unpaired t test. k , l Depletion/inhibition of BRD9 sensitizes OVCAR8 cells to PARPi in vivo. k OVCAR8 cells expressing the indicated shRNAs were subcutaneously injected into the flank of NOD-SCID mice. Mice were treated with or without olaparib (50 mg/kg i.p. 3 days × 8 times). Tumor volume and weight were assessed ( l ). OVCAR8 cells were subcutaneously injected into the flank of NOD-SCID mice. Mice were treated with vehicle (normal saline, NS), olaparib (PARPi, 50 mg/kg), BRD9i (40 mg/kg i.p. 3 days × 8 times), or olaparib + BRD9i. Tumor volume and weight were assessed. Representative data (mean ± SEM) are shown from n = 6 biologically independent samples by two-sided unpaired t test.

    Journal: Nature Communications

    Article Title: The bromodomain containing protein BRD-9 orchestrates RAD51–RAD54 complex formation and regulates homologous recombination-mediated repair

    doi: 10.1038/s41467-020-16443-x

    Figure Lengend Snippet: a – c BRD9 is overexpressed in ovarian cancer patient samples and cell lines, and is associated with decreased patient survival. a Analysis of BRD9 expression in ovarian cancer patient samples from the TCGA database. Red indicates BRD9 amplification. b Kaplan–Meier curve showing the survival of ovarian cancer patients with low ( n = 720) and high ( n = 715) expression of BRD9. Statistical analysis with the two-sided log-rank (Mantel–Cox) test revealed statistically significant differences as shown on the graph. c Immunoblot of indicated proteins in the indicated ovarian cancer cell lines. d – g Depletion/inhibition of BRD9 sensitizes OVCAR8 cells to PARPi and cisplatin. d – f OVCAR8 cells infected with indicated shRNAs and subjected to WB assay ( d ) to assess knockdown efficiency, and colony-formation assay to assess the sensitivity to olaparib ( e ) and cisplatin ( f ). g OVCAR8 cells were exposed to olaparib and/or BRD9i and subjected to colony-formation assay. Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. ** p < 0.01,*** p < 0.001 by two-sided unpaired t test. h – j Overexpression of BRD9 confers resistance to PARPi/cisplatin. OVCAR7 cells infected with the indicated lentivirus and subjected to colony-formation assay to assess the sensitivity to olaparib ( i ) and cisplatin ( j ). Protein expression was assessed by Western blot ( h ). Representative data (mean ± SEM) are shown from n = 3 biologically independent samples. ** p < 0.01,*** p < 0.001 by two-sided unpaired t test. k , l Depletion/inhibition of BRD9 sensitizes OVCAR8 cells to PARPi in vivo. k OVCAR8 cells expressing the indicated shRNAs were subcutaneously injected into the flank of NOD-SCID mice. Mice were treated with or without olaparib (50 mg/kg i.p. 3 days × 8 times). Tumor volume and weight were assessed ( l ). OVCAR8 cells were subcutaneously injected into the flank of NOD-SCID mice. Mice were treated with vehicle (normal saline, NS), olaparib (PARPi, 50 mg/kg), BRD9i (40 mg/kg i.p. 3 days × 8 times), or olaparib + BRD9i. Tumor volume and weight were assessed. Representative data (mean ± SEM) are shown from n = 6 biologically independent samples by two-sided unpaired t test.

    Article Snippet: Anti-BRD9 (rabbit) and anti-53BP1 (rabbit) for IF was homemade; anti-SMARCC1 (11956 rabbit), anti-BRG1 (3508 rabbit), anti-BAF250 (12354 rabbit), and anti-BRM (11966 rabbit) for WB (1:1000) were purchased from Cell Signaling Technology.

    Techniques: Expressing, Amplification, Western Blot, Inhibition, Infection, Colony Assay, Over Expression, In Vivo, Injection

    Bromodomain-containing protein–HR signature.

    Journal: Nature Communications

    Article Title: The bromodomain containing protein BRD-9 orchestrates RAD51–RAD54 complex formation and regulates homologous recombination-mediated repair

    doi: 10.1038/s41467-020-16443-x

    Figure Lengend Snippet: Bromodomain-containing protein–HR signature.

    Article Snippet: Anti-BRD9 (rabbit) and anti-53BP1 (rabbit) for IF was homemade; anti-SMARCC1 (11956 rabbit), anti-BRG1 (3508 rabbit), anti-BAF250 (12354 rabbit), and anti-BRM (11966 rabbit) for WB (1:1000) were purchased from Cell Signaling Technology.

    Techniques: Mutagenesis