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ovarian cancer cell line ov  (ATCC)


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    Structured Review

    ATCC ovarian cancer cell line ov
    Ovarian Cancer Cell Line Ov, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 419 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ov+90/OV-90/us12648946-1282-2-9
    Average 96 stars, based on 419 article reviews
    ovarian cancer cell line ov - by Bioz Stars, 2026-09
    96/100 stars

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    Cell Culture:

    Article Title: Newcastle Disease Virus Vaccine Strain H as a Potential Oncolytic Agent in Ovarian Cancer Therapy
    Article Snippet: Ovarian cancer remains one of the most lethal malignancies with a five-year survival rate around 20% at III–IV stages, which determines the urgent need to develop new therapeutic approaches.. Newcastle disease virus (NDV) has demonstrated considerable promise as an oncolytic agent, capable of selectively lysing tumor cells, suppressing the metastatic potential and stimulating anti-tumor immunity.. Despite the established therapeutic potential, studies that investigate oncolytic properties of this virus within the context of ovarian cancer remain limited.

    Article Title: Antibody-pyrrolobenzodiazepine derivative conjugate which binds caludin-6 and claudin-9
    Article Snippet: .. OV-90 (ATCC CRL-11732), a human ovarian cancer cell line of CLDN6 antigen-positive cells, was cultured in 1:1 mixed medium (hereinafter, referred to as the medium) of Medium199 (Thermo Fisher Scientific) and MCDB 105 Medium (Sigma-Aldrich Co. LLC) containing 15% fetal bovine serum (Hyclone). ..

    Article Title: A novel CLDN6 nanobody-based bispecific T-cell engager delivered by self-amplifying RNA platform exhibits potent antitumor efficacy
    Article Snippet: .. HEK-293T, HeLa, OV-90 and PA-1 were purchased from the American Type Culture Collection and cultured in DMEM (Gibco) or RIPM-1640 (Gibco). ..

    Expressing:

    Article Title: Claudin-6 binding molecules and uses thereof
    Article Snippet: .. The human cancer cell lines expressing human CLDN6 (HuH-7 (Health Science Research Resources Bank), OV-90 (ATCC) or OVCAR-3 (ATCC)) was transplanted subcutaneously into NOD/ShiJic-scid mice, and human PBMC was injected into the mice (so-called T cell injection model). ..

    Article Title: CLDN6 Expression Plasticity in Ovarian Cancer: Insights into Therapeutic Optimization for CLDN6-Targeted Immunotherapy
    Article Snippet: .. To analyze the cellular characteristics, we selected seven serous ovarian cancer cell lines, as a previous study demonstrated that serous adenocarcinomas show the most frequent expression of CLDN6 among ovarian adenocarcinomas ( ): OV-90 (RRID: CVCL_3768, purchased in May 2012 from the ATCC), NIH:OVCAR-3 (RRID: CVCL_0465, purchased in November 2019 from the ATCC), COV362 [RRID: CVCL_2420, purchased in September 2017 from the European Collection of Animal Cell Cultures (ECACC)], COV318 (RRID: CVCL_2419, purchased in July 2018 from the ECACC), COV413A (RRID: CVCL_2422, purchased in September 2017 from the ECACC), COV413B (RRID: CVCL_2423, purchased in September 2017 from the ECACC), and JHOS4 (RRID: CVCL_4649, purchased in June 2012 from RIKEN BRC). .. We included a lung adenocarcinoma cell line, NCI-H1435 (RRID: CVCL_1470, purchased in January 2014 from the ATCC), as a comparative CLDN6-positive cancer of a different tissue origin.

    Injection:

    Article Title: Claudin-6 binding molecules and uses thereof
    Article Snippet: .. The human cancer cell lines expressing human CLDN6 (HuH-7 (Health Science Research Resources Bank), OV-90 (ATCC) or OVCAR-3 (ATCC)) was transplanted subcutaneously into NOD/ShiJic-scid mice, and human PBMC was injected into the mice (so-called T cell injection model). ..

    Multiple Displacement Amplification:

    Article Title: CDCP1-targeting ADC outperforms standard therapies in Ras-mutant pancreatic cancer
    Article Snippet: .. HL-60, AsPC-1, BxPC-3, COS-7, MDA-MB-231, MDA-MB-453, MDA-MB-468, DU4475, SK-OV-3, OV-90, UWB1.289, SW626, SW480, SW620, HCT116, p53 wild-type, PC-3, PANC-1, CT26, DU145, LNCaP, and MJ cells were purchased from the American Type Culture Collection (Manassas, VA, USA). .. MIA PaCa-2 and MCF-7 were purchased from the Korean Cell Line Bank.



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    ov90  (ATCC)
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    ATCC ov90
    a Chemical structures of KLHL41-based PROTACs, referred to as KLHL41-BRD4 Degraders (KBDs). Carbon atoms in the linker are color-coded in yellow for clear visualization. b BRD4 degradation by KBDs is structure-dependent. KBDs were treated to RH30 cell with the indicated concentrations for 12 h. BRD4 degradation by KBDs were monitored by western blot. c Quantification of BRD4 band intensities at 40 μM in b ( n = 3, biological replicates). d KBD-1-induced BRD4 degradation is inhibited by co-treatment of either MG132 or MLN4924 in RH30 cells, indicating that BRD4 degradation by KBD-1 is mediated by CRL-mediated ubiquitination. e Quantification of BRD4 band intensities in ( d ) ( n = 3, biological replicates). f KBD-1 induced BRD4 degradation only in myosarcoma cell lines (RD and RH30 cells) after 24 h treatment. BRD4 was not degraded by KBD-1 in non-muscle related cancer cell lines <t>(OV90,</t> A549, SW480, and HeLa cells). g Quantification of BRD4 band intensities at 20 μM in f ( n = 3, biological replicates). h KBD-1 (40 μM) exhibited cytotoxicity only in myosarcoma cell lines after 24 h treatment ( n = 5, technical replicates). i – l KLHL41-dependent BRD4 degradation by KBD-1. i KLHL41 knockdown disturbed KBD-1 mediated BRD4 degradation in RH30 cells. j Quantification of BRD4 band intensities in i ( n = 3, biological replicates). k KLHL41 overexpression induced BRD4 degradation by KBD-1 in HeLa cells. l Quantification of BRD4 band intensities in k ( n = 3, biological replicates). Data in ( b , d , f , i , k ) are representative of three independent experiments. Data in ( c , e , g , h , j , l ) are presented as the mean ± standard deviation, with error bars indicating the standard deviation. Statistical significance was determined using a two-tailed unpaired Student’s t-test. ns, not significant ( P ≥ 0.05); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.
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    96
    ATCC ovarian cancer cell line ov90
    a Chemical structures of KLHL41-based PROTACs, referred to as KLHL41-BRD4 Degraders (KBDs). Carbon atoms in the linker are color-coded in yellow for clear visualization. b BRD4 degradation by KBDs is structure-dependent. KBDs were treated to RH30 cell with the indicated concentrations for 12 h. BRD4 degradation by KBDs were monitored by western blot. c Quantification of BRD4 band intensities at 40 μM in b ( n = 3, biological replicates). d KBD-1-induced BRD4 degradation is inhibited by co-treatment of either MG132 or MLN4924 in RH30 cells, indicating that BRD4 degradation by KBD-1 is mediated by CRL-mediated ubiquitination. e Quantification of BRD4 band intensities in ( d ) ( n = 3, biological replicates). f KBD-1 induced BRD4 degradation only in myosarcoma cell lines (RD and RH30 cells) after 24 h treatment. BRD4 was not degraded by KBD-1 in non-muscle related cancer cell lines <t>(OV90,</t> A549, SW480, and HeLa cells). g Quantification of BRD4 band intensities at 20 μM in f ( n = 3, biological replicates). h KBD-1 (40 μM) exhibited cytotoxicity only in myosarcoma cell lines after 24 h treatment ( n = 5, technical replicates). i – l KLHL41-dependent BRD4 degradation by KBD-1. i KLHL41 knockdown disturbed KBD-1 mediated BRD4 degradation in RH30 cells. j Quantification of BRD4 band intensities in i ( n = 3, biological replicates). k KLHL41 overexpression induced BRD4 degradation by KBD-1 in HeLa cells. l Quantification of BRD4 band intensities in k ( n = 3, biological replicates). Data in ( b , d , f , i , k ) are representative of three independent experiments. Data in ( c , e , g , h , j , l ) are presented as the mean ± standard deviation, with error bars indicating the standard deviation. Statistical significance was determined using a two-tailed unpaired Student’s t-test. ns, not significant ( P ≥ 0.05); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.
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    ov 90  (ATCC)
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    ATCC ov 90
    a Chemical structures of KLHL41-based PROTACs, referred to as KLHL41-BRD4 Degraders (KBDs). Carbon atoms in the linker are color-coded in yellow for clear visualization. b BRD4 degradation by KBDs is structure-dependent. KBDs were treated to RH30 cell with the indicated concentrations for 12 h. BRD4 degradation by KBDs were monitored by western blot. c Quantification of BRD4 band intensities at 40 μM in b ( n = 3, biological replicates). d KBD-1-induced BRD4 degradation is inhibited by co-treatment of either MG132 or MLN4924 in RH30 cells, indicating that BRD4 degradation by KBD-1 is mediated by CRL-mediated ubiquitination. e Quantification of BRD4 band intensities in ( d ) ( n = 3, biological replicates). f KBD-1 induced BRD4 degradation only in myosarcoma cell lines (RD and RH30 cells) after 24 h treatment. BRD4 was not degraded by KBD-1 in non-muscle related cancer cell lines <t>(OV90,</t> A549, SW480, and HeLa cells). g Quantification of BRD4 band intensities at 20 μM in f ( n = 3, biological replicates). h KBD-1 (40 μM) exhibited cytotoxicity only in myosarcoma cell lines after 24 h treatment ( n = 5, technical replicates). i – l KLHL41-dependent BRD4 degradation by KBD-1. i KLHL41 knockdown disturbed KBD-1 mediated BRD4 degradation in RH30 cells. j Quantification of BRD4 band intensities in i ( n = 3, biological replicates). k KLHL41 overexpression induced BRD4 degradation by KBD-1 in HeLa cells. l Quantification of BRD4 band intensities in k ( n = 3, biological replicates). Data in ( b , d , f , i , k ) are representative of three independent experiments. Data in ( c , e , g , h , j , l ) are presented as the mean ± standard deviation, with error bars indicating the standard deviation. Statistical significance was determined using a two-tailed unpaired Student’s t-test. ns, not significant ( P ≥ 0.05); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.
    Ov 90, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC ov 90 cells
    a Chemical structures of KLHL41-based PROTACs, referred to as KLHL41-BRD4 Degraders (KBDs). Carbon atoms in the linker are color-coded in yellow for clear visualization. b BRD4 degradation by KBDs is structure-dependent. KBDs were treated to RH30 cell with the indicated concentrations for 12 h. BRD4 degradation by KBDs were monitored by western blot. c Quantification of BRD4 band intensities at 40 μM in b ( n = 3, biological replicates). d KBD-1-induced BRD4 degradation is inhibited by co-treatment of either MG132 or MLN4924 in RH30 cells, indicating that BRD4 degradation by KBD-1 is mediated by CRL-mediated ubiquitination. e Quantification of BRD4 band intensities in ( d ) ( n = 3, biological replicates). f KBD-1 induced BRD4 degradation only in myosarcoma cell lines (RD and RH30 cells) after 24 h treatment. BRD4 was not degraded by KBD-1 in non-muscle related cancer cell lines <t>(OV90,</t> A549, SW480, and HeLa cells). g Quantification of BRD4 band intensities at 20 μM in f ( n = 3, biological replicates). h KBD-1 (40 μM) exhibited cytotoxicity only in myosarcoma cell lines after 24 h treatment ( n = 5, technical replicates). i – l KLHL41-dependent BRD4 degradation by KBD-1. i KLHL41 knockdown disturbed KBD-1 mediated BRD4 degradation in RH30 cells. j Quantification of BRD4 band intensities in i ( n = 3, biological replicates). k KLHL41 overexpression induced BRD4 degradation by KBD-1 in HeLa cells. l Quantification of BRD4 band intensities in k ( n = 3, biological replicates). Data in ( b , d , f , i , k ) are representative of three independent experiments. Data in ( c , e , g , h , j , l ) are presented as the mean ± standard deviation, with error bars indicating the standard deviation. Statistical significance was determined using a two-tailed unpaired Student’s t-test. ns, not significant ( P ≥ 0.05); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.
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    Image Search Results


    a Chemical structures of KLHL41-based PROTACs, referred to as KLHL41-BRD4 Degraders (KBDs). Carbon atoms in the linker are color-coded in yellow for clear visualization. b BRD4 degradation by KBDs is structure-dependent. KBDs were treated to RH30 cell with the indicated concentrations for 12 h. BRD4 degradation by KBDs were monitored by western blot. c Quantification of BRD4 band intensities at 40 μM in b ( n = 3, biological replicates). d KBD-1-induced BRD4 degradation is inhibited by co-treatment of either MG132 or MLN4924 in RH30 cells, indicating that BRD4 degradation by KBD-1 is mediated by CRL-mediated ubiquitination. e Quantification of BRD4 band intensities in ( d ) ( n = 3, biological replicates). f KBD-1 induced BRD4 degradation only in myosarcoma cell lines (RD and RH30 cells) after 24 h treatment. BRD4 was not degraded by KBD-1 in non-muscle related cancer cell lines (OV90, A549, SW480, and HeLa cells). g Quantification of BRD4 band intensities at 20 μM in f ( n = 3, biological replicates). h KBD-1 (40 μM) exhibited cytotoxicity only in myosarcoma cell lines after 24 h treatment ( n = 5, technical replicates). i – l KLHL41-dependent BRD4 degradation by KBD-1. i KLHL41 knockdown disturbed KBD-1 mediated BRD4 degradation in RH30 cells. j Quantification of BRD4 band intensities in i ( n = 3, biological replicates). k KLHL41 overexpression induced BRD4 degradation by KBD-1 in HeLa cells. l Quantification of BRD4 band intensities in k ( n = 3, biological replicates). Data in ( b , d , f , i , k ) are representative of three independent experiments. Data in ( c , e , g , h , j , l ) are presented as the mean ± standard deviation, with error bars indicating the standard deviation. Statistical significance was determined using a two-tailed unpaired Student’s t-test. ns, not significant ( P ≥ 0.05); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

    Journal: Nature Communications

    Article Title: Discovery of a KLHL41 Ligand for Muscle Specific Protein Degradation

    doi: 10.1038/s41467-026-73252-4

    Figure Lengend Snippet: a Chemical structures of KLHL41-based PROTACs, referred to as KLHL41-BRD4 Degraders (KBDs). Carbon atoms in the linker are color-coded in yellow for clear visualization. b BRD4 degradation by KBDs is structure-dependent. KBDs were treated to RH30 cell with the indicated concentrations for 12 h. BRD4 degradation by KBDs were monitored by western blot. c Quantification of BRD4 band intensities at 40 μM in b ( n = 3, biological replicates). d KBD-1-induced BRD4 degradation is inhibited by co-treatment of either MG132 or MLN4924 in RH30 cells, indicating that BRD4 degradation by KBD-1 is mediated by CRL-mediated ubiquitination. e Quantification of BRD4 band intensities in ( d ) ( n = 3, biological replicates). f KBD-1 induced BRD4 degradation only in myosarcoma cell lines (RD and RH30 cells) after 24 h treatment. BRD4 was not degraded by KBD-1 in non-muscle related cancer cell lines (OV90, A549, SW480, and HeLa cells). g Quantification of BRD4 band intensities at 20 μM in f ( n = 3, biological replicates). h KBD-1 (40 μM) exhibited cytotoxicity only in myosarcoma cell lines after 24 h treatment ( n = 5, technical replicates). i – l KLHL41-dependent BRD4 degradation by KBD-1. i KLHL41 knockdown disturbed KBD-1 mediated BRD4 degradation in RH30 cells. j Quantification of BRD4 band intensities in i ( n = 3, biological replicates). k KLHL41 overexpression induced BRD4 degradation by KBD-1 in HeLa cells. l Quantification of BRD4 band intensities in k ( n = 3, biological replicates). Data in ( b , d , f , i , k ) are representative of three independent experiments. Data in ( c , e , g , h , j , l ) are presented as the mean ± standard deviation, with error bars indicating the standard deviation. Statistical significance was determined using a two-tailed unpaired Student’s t-test. ns, not significant ( P ≥ 0.05); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

    Article Snippet: HeLa (human cervical adenocarcinoma, CCL-2), A549 (human lung carcinoma, CCL-185), and OV90 (human ovarian adenocarcinoma, CRL-3585) cells were obtained from the American Type Culture Collection (ATCC) and cultured in Roswell Park Memorial Institute (RPMI) medium (Welgene; LM011-01) supplemented with 1% (v/v) antibiotic-antimycotic solution (Welgene; LS203-01) and 10% (v/v) heat-inactivated fetal bovine serum (FBS, Gibco; #16000-044).

    Techniques: Western Blot, Ubiquitin Proteomics, Knockdown, Over Expression, Standard Deviation, Two Tailed Test

    a cKBD-1 induced BRD4 degradation only in myosarcoma cell lines (RD and RH30 cells). BRD4 was not degraded by cKBD-1 in non-muscle related cancer cell lines (OV90, A549, SW480, and HeLa cells). b Quantification of BRD4 band intensities at 0.1 μM in a ( n = 3, biological replicates). c cKBD-1 exhibited cytotoxicity only in myosarcoma cell lines at 5 μM ( n = 5, technical replicates). d – i KLHL41-dependent BRD4 degradation by cKBD-1. d KLHL41 knockdown disturbed cKBD-1 mediated BRD4 degradation in RH30 cells. e Quantification of BRD4 band intensities in d ( n = 3, biological replicates). f KLHL41 overexpression induced BRD4 degradation by cKBD-1 in HeLa cells. g Quantification of BRD4 band intensities in f ( n = 3, biological replicates). h cKBD-1 (5 μM) did not induce BRD4 degradation in undifferentiated C2C12 cells (myoblast, low KLHL41 expression). In differentiated C2C12 cells (myocyte, high KLHL41 expression), cKBD-1 (5 μM) induced BRD4 degradation. i Quantification of BRD4 band intensities in h (n = 3, biological replicates). j Mass spectrometry analysis of the tryptic peptide of KLHL41 containing Cys593 (amino acids 587–597): cKBD-1 binding peptide. k Docking analysis showed that Cys593 of KLHL41 is proximal to EN10. l BLI analysis revealed K D between the KLHL41/cKBD-1 complex and BRD4 to be 27.04 ± 0.93 nM ( n = 5, technical replicates). Experimental data using a series of BRD4 concentrations (colored lines) are overlaid with globally fitted curves (black lines) using a 1:1 Langmuir binding model. The fitting yielded an association rate constant (k on ) of 9.64 × 10³ M⁻¹ s⁻¹ and a dissociation rate constant (k off ) of 2.73 × 10⁻⁴ s⁻¹. The maximum binding response (R max ) was 0.36 nm, and the goodness of fit was indicated by the the coefficient of determination (R² = 0.998) and a residual sum of squares (RSS) value of 0.50. m Quantitative proteome profiling showed that cKBD-1 selectively degraded BRD4 without affecting KLHL41 level ( n = 4 per group, technical replicates). n Schematic of in vivo experiment. Mice were treated with vehicle or cKBD-1 (5 mpk) via IV or IP injection and sacrificed after 24 h for tissue collection (n = 3 mice per group, biological replicates). Created in BioRender. Park, J. BioRender.com/wlh07p2. o Immunoblot showing muscle-specific KLHL41 expression in vivo. Representative data are shown from three independent experiments with similar results. p cKBD-1 induced BRD4 degradation in muscle tissue, but not in other organs in in vivo mouse model. Representative data are shown from three independent experiments with similar results. q Quantification of BRD4 band intensities in ( p ). Data shown in ( a , d , f , h ) are representative of three independent experiments. Data shown in ( b , c , e , g , i ) are presented as the mean ± standard deviation, with error bars indicating the standard deviation. Statistical significance was determined using a two-tailed unpaired Student’s t-test. ns, not significant ( P ≥ 0.05); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

    Journal: Nature Communications

    Article Title: Discovery of a KLHL41 Ligand for Muscle Specific Protein Degradation

    doi: 10.1038/s41467-026-73252-4

    Figure Lengend Snippet: a cKBD-1 induced BRD4 degradation only in myosarcoma cell lines (RD and RH30 cells). BRD4 was not degraded by cKBD-1 in non-muscle related cancer cell lines (OV90, A549, SW480, and HeLa cells). b Quantification of BRD4 band intensities at 0.1 μM in a ( n = 3, biological replicates). c cKBD-1 exhibited cytotoxicity only in myosarcoma cell lines at 5 μM ( n = 5, technical replicates). d – i KLHL41-dependent BRD4 degradation by cKBD-1. d KLHL41 knockdown disturbed cKBD-1 mediated BRD4 degradation in RH30 cells. e Quantification of BRD4 band intensities in d ( n = 3, biological replicates). f KLHL41 overexpression induced BRD4 degradation by cKBD-1 in HeLa cells. g Quantification of BRD4 band intensities in f ( n = 3, biological replicates). h cKBD-1 (5 μM) did not induce BRD4 degradation in undifferentiated C2C12 cells (myoblast, low KLHL41 expression). In differentiated C2C12 cells (myocyte, high KLHL41 expression), cKBD-1 (5 μM) induced BRD4 degradation. i Quantification of BRD4 band intensities in h (n = 3, biological replicates). j Mass spectrometry analysis of the tryptic peptide of KLHL41 containing Cys593 (amino acids 587–597): cKBD-1 binding peptide. k Docking analysis showed that Cys593 of KLHL41 is proximal to EN10. l BLI analysis revealed K D between the KLHL41/cKBD-1 complex and BRD4 to be 27.04 ± 0.93 nM ( n = 5, technical replicates). Experimental data using a series of BRD4 concentrations (colored lines) are overlaid with globally fitted curves (black lines) using a 1:1 Langmuir binding model. The fitting yielded an association rate constant (k on ) of 9.64 × 10³ M⁻¹ s⁻¹ and a dissociation rate constant (k off ) of 2.73 × 10⁻⁴ s⁻¹. The maximum binding response (R max ) was 0.36 nm, and the goodness of fit was indicated by the the coefficient of determination (R² = 0.998) and a residual sum of squares (RSS) value of 0.50. m Quantitative proteome profiling showed that cKBD-1 selectively degraded BRD4 without affecting KLHL41 level ( n = 4 per group, technical replicates). n Schematic of in vivo experiment. Mice were treated with vehicle or cKBD-1 (5 mpk) via IV or IP injection and sacrificed after 24 h for tissue collection (n = 3 mice per group, biological replicates). Created in BioRender. Park, J. BioRender.com/wlh07p2. o Immunoblot showing muscle-specific KLHL41 expression in vivo. Representative data are shown from three independent experiments with similar results. p cKBD-1 induced BRD4 degradation in muscle tissue, but not in other organs in in vivo mouse model. Representative data are shown from three independent experiments with similar results. q Quantification of BRD4 band intensities in ( p ). Data shown in ( a , d , f , h ) are representative of three independent experiments. Data shown in ( b , c , e , g , i ) are presented as the mean ± standard deviation, with error bars indicating the standard deviation. Statistical significance was determined using a two-tailed unpaired Student’s t-test. ns, not significant ( P ≥ 0.05); * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

    Article Snippet: HeLa (human cervical adenocarcinoma, CCL-2), A549 (human lung carcinoma, CCL-185), and OV90 (human ovarian adenocarcinoma, CRL-3585) cells were obtained from the American Type Culture Collection (ATCC) and cultured in Roswell Park Memorial Institute (RPMI) medium (Welgene; LM011-01) supplemented with 1% (v/v) antibiotic-antimycotic solution (Welgene; LS203-01) and 10% (v/v) heat-inactivated fetal bovine serum (FBS, Gibco; #16000-044).

    Techniques: Knockdown, Over Expression, Expressing, Mass Spectrometry, Binding Assay, In Vivo, Injection, Western Blot, Standard Deviation, Two Tailed Test