Journal: Brain Pathology

Article Title: Tumor cells with neuronal intermediate progenitor features define a subgroup of 1p/19q co‐deleted anaplastic gliomas

doi: 10.1111/bpa.12434

Figure Lengend Snippet: List of primary antibodies used for immunohistochemistry.

Article Snippet: Micrographs were acquired with Axiocam ICc 1 camera and Axiovision 4.8.2 software (Zeiss ® ). table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Species Antigen Dilution Reference Provider Rabbit polyclonal ELAVL2 1/500 14008‐1‐AP Proteintech Mouse monoclonal H09 IDH1 R132H 1/50 DIA‐H09 Dianova Mouse monoclonal 2E3 INA 1/100 NB300‐140 Novus Biologicals Goat polyclonal Ki67 1/80 sc‐7844 Santa Cruz Mouse monoclonal INSM1 1/250 sc‐271408 Santa Cruz Rabbit polyclonal NFIA 1/400 NBP1‐81406 Novus Biological Rabbit polyclonal SOX9 1/50 sc‐20095 Santa Cruz Rabbit polyclonal SOX11 1/100 HPA000356 Sigma‐Aldrich Open in a separate window List of primary antibodies used for immunohistochemistry.

Techniques: Immunohistochemistry

Journal: Brain Pathology

Article Title: Tumor cells with neuronal intermediate progenitor features define a subgroup of 1p/19q co‐deleted anaplastic gliomas

doi: 10.1111/bpa.12434

Figure Lengend Snippet: INSM1 immunolabeling in anaplastic oligodendroglial tumors. a–c. three sections of the same anaplastic oligodendroglial tumor of the NIPhigh subgroup were immunolabeled for IDH1 R132H (brown signal in a, c), and INSM1 (blue signal in b, c). Some tumor cells showed cytoplasmic immunolabeling for IDH1 R132H and nuclear immunolabeling for INSM1 (c). d, e. Immunolabeling of INSM1 (brown signal) and counterstaining (blue signal) in anaplastic oligodendroglioma of the NIPhigh and NIPlow subgroups. f. Quantification of INSM1 immunolabeling in NIPhigh vs. NIPlow and non 1p/19q co‐deleted tumors with significant difference (P = 0.0163 Kruskal–Wallis test; asterisk NIPhigh vs. NIPlow P = 0.0454; asterisk NIPhigh vs. non 1p/19q co‐deleted AOT P = 0.0143; Mann–Whitney test). g–i. Double immunolabeling of an anaplastic oligodendroglial tumors of the NIPhigh subgroup by INSM1 (green, g, i) and SOX9 (red, h, i) with quantification (j). Both markers are expressed by two mainly exclusive tumor cell populations. k–m, double immunolabeling of an anaplastic oligodendroglial tumors of the NIPhigh subgroup by INSM1 (green, k, m) and Ki‐67 (red, l, m) with quantification (n). Most INSM1+ cells are negative for Ki‐67 (open arrowhead, f–h) and a minority of INSM1+ cells are positive for Ki‐67 (solid arrowhead, f–h). Scale bars. A–C: 10 µm, D–E: 50 µm. G–I, K–M: 20 µm.

Article Snippet: Micrographs were acquired with Axiocam ICc 1 camera and Axiovision 4.8.2 software (Zeiss ® ). table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Species Antigen Dilution Reference Provider Rabbit polyclonal ELAVL2 1/500 14008‐1‐AP Proteintech Mouse monoclonal H09 IDH1 R132H 1/50 DIA‐H09 Dianova Mouse monoclonal 2E3 INA 1/100 NB300‐140 Novus Biologicals Goat polyclonal Ki67 1/80 sc‐7844 Santa Cruz Mouse monoclonal INSM1 1/250 sc‐271408 Santa Cruz Rabbit polyclonal NFIA 1/400 NBP1‐81406 Novus Biological Rabbit polyclonal SOX9 1/50 sc‐20095 Santa Cruz Rabbit polyclonal SOX11 1/100 HPA000356 Sigma‐Aldrich Open in a separate window List of primary antibodies used for immunohistochemistry.

Techniques: Immunolabeling, MANN-WHITNEY

Journal: bioRxiv

Article Title: Oncogenic Ppm1d mutations deregulate the p53 pathway in primary mouse gliomas

doi: 10.1101/2025.11.25.690483

Figure Lengend Snippet: a) Intracranial injection of DF1 producing cells carrying RCAS vectors encoding PDGFB, Cre, and luciferase to enable conditional targeting of neural stem cells. b) Mice were injected at postnatal day 3-5 and monitored for tumor development through symptom assessment and bioluminescence imaging starting at week 4 to detect tumor-associated signals. Kaplan-Meier survival estimates and and log-rank (Mantel-Cox) test p= 0.0277, Ppm1d flex- /wt ; p53 fl/wt n=21, Ppm1d wt/wt ; p53 fl/wt n=19 c) Immunohistochemistry (IHC) with Ki67, Olig2, and GFAP for tumor-bearing brains from wild-type Ppm1d (Ppm1d wt/wt ; p53 fl/wt ) and truncated Ppm1d (Ppm1d flex- /wt ; p53 fl/wt ) mice. Tumor and normal regions were denoted in GFAP staining; GFAP exhibited cytoplasmic localization. Scale bar: 100 μm. d) Quantification of Ki67 and Olig2 staining. GFAP expression was excluded from quantification due to its cytoplasmic distribution. Data are presented as mean ± SEM; n = 3. Student paired t-test, * p< 0.05 and ** p< 0.01 e) IHC staining for Myc-tag was performed on brain sections from wild-type Ppm1d (Ppm1d wt/wt ; p53 fl/wt ) and truncated Ppm1d (Ppm1d flex- /wt ; p53 fl/wt ) mice. Whole-mount sections (scale bar 2 mm) and tumor-region sections (scale bar 100 μm). Red boxes represent tumor regions. f) Quantification of Myc Tag IHC staining. Data are shown as mean ± SEM; n = 3. Student unpaired t-test, ** p< 0.01

Article Snippet: IHC staining for Ki67 (Cat #Bethyl IHC-00375), Olig2 (Cat #ab109186), GFAP (Cat #NB300-141) and MYC (Cat #ab32072) was conducted by HistoWiz.

Techniques: Injection, Luciferase, Imaging, Immunohistochemistry, Staining, Expressing

Journal: Advanced Science

Article Title: Disruption of ARID1B Recruitment to the Nuclear Pore Complex as a New Anticancer Therapeutic Strategy

doi: 10.1002/advs.202415585

Figure Lengend Snippet: Elevated expression of ARID1B correlates with a poor prognosis of breast cancer. A) Genetic alterations in breast cancer were analyzed using the oncomatrix databases, and the frequencies of gene alterations were plotted. ARID1A is one of the most common and significant alterations observed in breast cancer. B) ARID1A and ARID1B mRNA expression levels were analyzed in human TNBC samples using the TCGA dataset. C) Heatmap and hierarchical clustering are based on the protein expression levels of the cancer cell proliferation‐ and stemness‐related proteins from 56 human TNBC samples. Each column represents a sample; each row represents a protein. The log 2 relative protein expression scale is depicted on the top left. D) Spearman's rank correlation analysis using the CPTAC TNBC dataset shows that ARID1B protein expression is highly positively correlated with cell proliferation‐ and stemness‐related proteins. E) 4X and 20X IHC of ARID1B and Ki67 in breast cancer and normal tissues. Cyto, cytoplasmic; Nuc, nuclear. F) Correlation between ARID1B and proliferative marker Ki67 in breast cancer. G) Correlation between nuclear ARID1B and proliferative marker Ki67 in breast cancer. H) Kaplan–Meier survival plot for breast cancer patients with ARID1B high‐ ( n = 23) and low‐ ( n = 42) expressing tumors. High protein levels of ARID1B are associated with worse prognosis in breast cancer patients. The Tang 2018 database and Kaplan–Meier Plotter were used for analysis. [ ⁸⁷ ] Time to follow‐up was measured up to 150 months. Logrank p‐value = 0.024. I) Kaplan–Meier survival plot for breast cancer patients with ARID1A high‐ ( n = 43) and low‐ (n = 22) expressing tumors. Although the data were not statistically significant, high protein levels of ARID1A showed a trend of better survival in breast cancer patients, which didnot reach statistical significance. The Tang 2018 database and Kaplan–Meier Plotter were used for analysis. [ ⁸⁷ ] Time to follow‐up was measured up to 150 months. Logrank p ‐value = 0.4. J) Comparison of ssGSEA enrichment scores for cell proliferation‐related pathways between patients with ARID1B low levels and ARID1B high levels. All P ‐values are from Wilcoxon tests. *: p < 0.05; **: p < 0.01; ***: p < 0.001; ****: p < 0.0001.Elevated expression of ARID1B correlates with a poor prognosis of breast cancer. A) Genetic alterations in breast cancer were analyzed using the oncomatrix databases, and the frequencies of gene alterations were plotted. ARID1A is one of the most common and significant alterations observed in breast cancer. B) ARID1A and ARID1B mRNA expression levels were analyzed in human TNBC samples using the TCGA dataset. C) Heatmap and hierarchical clustering are based on the protein expression levels of the cancer cell proliferation‐ and stemness‐related proteins from 56 human TNBC samples. Each column represents a sample; each row represents a protein. The log 2 relative protein expression scale is depicted on the top left. D) Spearman's rank correlation analysis using the CPTAC TNBC dataset shows that ARID1B protein expression is highly positively correlated with cell proliferation‐ and stemness‐related proteins. E) 4X and 20X IHC of ARID1B and Ki67 in breast cancer and normal tissues. Cyto, cytoplasmic; Nuc, nuclear. F) Correlation between ARID1B and proliferative marker Ki67 in breast cancer. G) Correlation between nuclear ARID1B and proliferative marker Ki67 in breast cancer. H) Kaplan–Meier survival plot for breast cancer patients with ARID1B high‐ ( n = 23) and low‐ ( n = 42) expressing tumors. High protein levels of ARID1B are associated with worse prognosis in breast cancer patients. The Tang 2018 database and Kaplan–Meier Plotter were used for analysis. [ ⁸⁷ ] Time to follow‐up was measured up to 150 months. Logrank p‐value = 0.024. I) Kaplan–Meier survival plot for breast cancer patients with ARID1A high‐ ( n = 43) and low‐ (n = 22) expressing tumors. Although the data were not statistically significant, high protein levels of ARID1A showed a trend of better survival in breast cancer patients, which didnot reach statistical significance. The Tang 2018 database and Kaplan–Meier Plotter were used for analysis. [ ⁸⁷ ] Time to follow‐up was measured up to 150 months. Logrank p ‐value = 0.4. J) Comparison of ssGSEA enrichment scores for cell proliferation‐related pathways between patients with ARID1B low levels and ARID1B high levels. All P ‐values are from Wilcoxon tests. *: p < 0.05; **: p < 0.01; ***: p < 0.001; ****: p < 0.0001.

Article Snippet: The following antibodies were used: ARID1B (Abcam, ab‐57461), Ki67 (Cell Signaling Technology, 12202), actin (Sigma, A5441), GAPDH (Sigma, G8795), GAPDH (Novus Biologicals, NB300‐221), ARID1A (D2A8U) (Cell Signaling Technology, 123545), ARID1A (Santa Cruz Biotechnology, sc‐32761), SMARCE1 (Cell Signaling Technology, 33360), SMARCA2 (Cell Signaling Technology, 11966), SMARCA4 (Cell Signaling Technology, 49360), RANBP2 (Abcam, ab64276), RANBP2 (Santa Cruz Biotechnology, 74518), HA (C29F4) (Cell Signaling Technology, 3724), Lamin A/C (Cell Signaling Technology, 2032), Histon H3 (D1H2) (Cell Signaling Technology, 4499), KPNA2 (Santa Cruz Biotechnology, sc‐55538), KPNB1 (Abcam, ab2811), KPNB1 (ABclonal, A8610), Flag (Cell Signaling Technology, 14793S), Flag (Proteintech, 20543‐1‐AP).

Techniques: Expressing, Marker, Comparison

Journal: Advanced Science

Article Title: Disruption of ARID1B Recruitment to the Nuclear Pore Complex as a New Anticancer Therapeutic Strategy

doi: 10.1002/advs.202415585

Figure Lengend Snippet: Disruption of KPNA2–KPNB1–RANBP2‐facilitated ARID1B nuclear translocation alters gene expression and suppresses tumor growth. A) 20X IHC of ARID1B, KPNA2, and Ki67 in breast cancer and normal tissues. B) Correlation of Ki67 and KPNA2 in breast cancer. C) Comparison of KPNA2 protein expression between normal tissue samples ( n = 18) and tumor tissue samples from Luminal ( n = 64), HER2+ ( n = 10), and TNBC ( n = 16) patients. Analysis of KPNA2 protein levels using CPTAC database and UALCAN data analysis portal showed significant accumulation of KPNA2 in HER2+ ( p = 0.0097), and TNBC ( p ≤ 0.0001), and no significant difference in Luminal (ns) compared to normal tissues. [ ⁷⁹ , ⁸⁰ ] P ‐values are summarized with asterisks: *** – p ≤ 0.0001, ** – p ≤ 0.01, * – p ≤ 0.05. D) Correlation of ARID1B and KPNA2 in breast cancer. E) Immunofluorescence assay was conducted to detect levels of ARID1B ( green ) in MDA‐MB‐231 cells in response to IPZ treatment. Cells were treated with IPZ (40 µ m ) for 2 h. Nuclei were stained with DAPI ( blue ). The scale bars indicate 5 µm. F) Quantification of relative ARID1B fluorescence intensity in the nuclei of MDA‐MB‐231 cells after 2‐h IPZ treatment. G) Immunoblot analysis of cytosolic and nuclear fractions of MDA‐MB‐231 cells in response to IPZ treatment. MDA‐MB‐231 cells were treated with 40 µM IPZ or DMSO for 2 h. The protein levels of ARID1B, ARID1A, SMARCE1, and KPNB1 in the cytosolic and nuclear fractions were examined. Lamin A/C and Histone H3 were used as nuclear marker proteins. GAPDH was used as a cytoplasmic marker protein. Each lane was loaded with 30 µg of cytoplasmic or nuclear extract. H) Colony formation assay in response to continuous IPZ treatment in MDA‐MB‐231 cells. I) Survival rate of MDA‐MB‐231 cells under continuous IPZ treatment. Cell viability was determined using the CCK‐8 assay. The data is presented as the mean±SD of three independent experiments. Statistical significance was determined by two‐way ANOVA followed by the Bonferroni test. P ‐values are summarized with asterisks: *** – p ≤ 0.0001 J) Immunoblot analysis of ARID1B following 2‐h IPZ (40 µM) treatment in MDA‐MB‐231 cells. Two‐hour IPZ treatment didnot affect total ARID1B levels. K) Differential gene expression in IPZ‐ or BRMi‐treated groups versus the control group. L) Immunoblot analysis of cytosolic and nuclear fractions of control and RANBP2 KO MDA‐MB‐468 cells. The protein levels of RANBP2, ARID1B, SMARCA4, SMARCA2, ARID1A, SMARCE1, KPNB1, and KPNA2 in the cytosolic and nuclear fractions were examined. Lamin A/C and Histone H3 were used as nuclear marker proteins. GAPDH was used as a cytoplasmic marker protein. Each lane was loaded with 30 µg of cytoplasmic or nuclear extract. M) Immunofluorescence assay was conducted to detect levels of ARID1B ( green ) and RANBP2 ( red ) in empty vector control (CRISPRv2) and RANBP2 KO breast cancer cell lines. Nuclei were stained with DAPI ( blue ). The scale bars indicate 5 µm. N,O) Immunoblot analysis of ARID1B in RANBP2 KO and empty vector control (Control) TNBC cells. RANBP2 KO resulted in a significant reduction of ARID1B in MDA‐MB‐231 N) and MDA‐MB‐468 O) cells.Disruption of KPNA2–KPNB1–RANBP2‐facilitated ARID1B nuclear translocation alters gene expression and suppresses tumor growth. A) 20X IHC of ARID1B, KPNA2, and Ki67 in breast cancer and normal tissues. B) Correlation of Ki67 and KPNA2 in breast cancer. C) Comparison of KPNA2 protein expression between normal tissue samples ( n = 18) and tumor tissue samples from Luminal ( n = 64), HER2+ ( n = 10), and TNBC ( n = 16) patients. Analysis of KPNA2 protein levels using CPTAC database and UALCAN data analysis portal showed significant accumulation of KPNA2 in HER2+ ( p = 0.0097), and TNBC ( p ≤ 0.0001), and no significant difference in Luminal (ns) compared to normal tissues. [ ⁷⁹ , ⁸⁰ ] P ‐values are summarized with asterisks: *** – p ≤ 0.0001, ** – p ≤ 0.01, * – p ≤ 0.05. D) Correlation of ARID1B and KPNA2 in breast cancer. E) Immunofluorescence assay was conducted to detect levels of ARID1B ( green ) in MDA‐MB‐231 cells in response to IPZ treatment. Cells were treated with IPZ (40 µ m ) for 2 h. Nuclei were stained with DAPI ( blue ). The scale bars indicate 5 µm. F) Quantification of relative ARID1B fluorescence intensity in the nuclei of MDA‐MB‐231 cells after 2‐h IPZ treatment. G) Immunoblot analysis of cytosolic and nuclear fractions of MDA‐MB‐231 cells in response to IPZ treatment. MDA‐MB‐231 cells were treated with 40 µM IPZ or DMSO for 2 h. The protein levels of ARID1B, ARID1A, SMARCE1, and KPNB1 in the cytosolic and nuclear fractions were examined. Lamin A/C and Histone H3 were used as nuclear marker proteins. GAPDH was used as a cytoplasmic marker protein. Each lane was loaded with 30 µg of cytoplasmic or nuclear extract. H) Colony formation assay in response to continuous IPZ treatment in MDA‐MB‐231 cells. I) Survival rate of MDA‐MB‐231 cells under continuous IPZ treatment. Cell viability was determined using the CCK‐8 assay. The data is presented as the mean±SD of three independent experiments. Statistical significance was determined by two‐way ANOVA followed by the Bonferroni test. P ‐values are summarized with asterisks: *** – p ≤ 0.0001 J) Immunoblot analysis of ARID1B following 2‐h IPZ (40 µM) treatment in MDA‐MB‐231 cells. Two‐hour IPZ treatment didnot affect total ARID1B levels. K) Differential gene expression in IPZ‐ or BRMi‐treated groups versus the control group. L) Immunoblot analysis of cytosolic and nuclear fractions of control and RANBP2 KO MDA‐MB‐468 cells. The protein levels of RANBP2, ARID1B, SMARCA4, SMARCA2, ARID1A, SMARCE1, KPNB1, and KPNA2 in the cytosolic and nuclear fractions were examined. Lamin A/C and Histone H3 were used as nuclear marker proteins. GAPDH was used as a cytoplasmic marker protein. Each lane was loaded with 30 µg of cytoplasmic or nuclear extract. M) Immunofluorescence assay was conducted to detect levels of ARID1B ( green ) and RANBP2 ( red ) in empty vector control (CRISPRv2) and RANBP2 KO breast cancer cell lines. Nuclei were stained with DAPI ( blue ). The scale bars indicate 5 µm. N,O) Immunoblot analysis of ARID1B in RANBP2 KO and empty vector control (Control) TNBC cells. RANBP2 KO resulted in a significant reduction of ARID1B in MDA‐MB‐231 N) and MDA‐MB‐468 O) cells.

Article Snippet: The following antibodies were used: ARID1B (Abcam, ab‐57461), Ki67 (Cell Signaling Technology, 12202), actin (Sigma, A5441), GAPDH (Sigma, G8795), GAPDH (Novus Biologicals, NB300‐221), ARID1A (D2A8U) (Cell Signaling Technology, 123545), ARID1A (Santa Cruz Biotechnology, sc‐32761), SMARCE1 (Cell Signaling Technology, 33360), SMARCA2 (Cell Signaling Technology, 11966), SMARCA4 (Cell Signaling Technology, 49360), RANBP2 (Abcam, ab64276), RANBP2 (Santa Cruz Biotechnology, 74518), HA (C29F4) (Cell Signaling Technology, 3724), Lamin A/C (Cell Signaling Technology, 2032), Histon H3 (D1H2) (Cell Signaling Technology, 4499), KPNA2 (Santa Cruz Biotechnology, sc‐55538), KPNB1 (Abcam, ab2811), KPNB1 (ABclonal, A8610), Flag (Cell Signaling Technology, 14793S), Flag (Proteintech, 20543‐1‐AP).

Techniques: Disruption, Translocation Assay, Gene Expression, Comparison, Expressing, Immunofluorescence, Staining, Fluorescence, Western Blot, Marker, Colony Assay, CCK-8 Assay, Control, Plasmid Preparation

Journal: Advanced Science

Article Title: Disruption of ARID1B Recruitment to the Nuclear Pore Complex as a New Anticancer Therapeutic Strategy

doi: 10.1002/advs.202415585

Figure Lengend Snippet: Downregulation of ARID1B reduces tumor growth and augments the therapeutic efficacy of Niraparib in eliminating breast tumors in vivo. A) Scheme of the animal experiment. B) Tumor growth of ARID1B OE and empty vector control (Control) MDA‐MB‐231 in female nu/nu mice measured for a period of 8 weeks. Tumor‐bearing mice were randomized into treated and non‐treated groups ( n = 5) when the tumor reached a volume of 50 mm 3 . Mice were treated with Niraparib four times per week. One‐way ANOVA followed by the Tukey's multiple‐comparison test were performed for comparison of survival (ns, P > 0.05; * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001). C,D) Size C) and weight D) of tumors formed in female nu/nu mice by ARID1B OE and Control MDA‐MB‐231 cells treated and non‐treated with Niraparib. E) Tumor growth of ARID1B KO and empty vector control (Control) MDA‐MB‐468 in female nu/nu mice measured for a period of 8 weeks. Tumor‐bearing mice were randomized into treated and non‐treated groups ( n = 5) when the tumor reached a volume of 50 mm 3 . Mice were treated with Niraparib four times per week. One‐way ANOVA followed by the Tukey's multiple‐comparison test were performed for comparison of survival (ns, P > 0.05; * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001). F,G) Size F) and weight G) of tumors formed in female nu/nu mice by ARID1B KO and Control MDA‐MB‐468 cells treated and non‐treated with Niraparib. H,I) Body weight of all four groups of mice from Figure H) and Figure I) was measured for a period of 8 weeks. J) 40X IHC of ARID1B and Ki67 in ARID1B KO and Control MDA‐MB‐468 tumors (left panel) and in ARID1B OE and Control MDA‐MB‐231 tumors (right panel) treated with Niraparib or Vehicle (Control). K) IHC analysis of ARID1B and Ki67 positive area (%) in ARID1B KO and Control MDA‐MB‐468 tumors and in ARID1B OE and Control MDA‐MB‐231 tumors treated with Niraparib or Vehicle (Control).Downregulation of ARID1B reduces tumor growth and augments the therapeutic efficacy of Niraparib in eliminating breast tumors in vivo. A) Scheme of the animal experiment. B) Tumor growth of ARID1B OE and empty vector control (Control) MDA‐MB‐231 in female nu/nu mice measured for a period of 8 weeks. Tumor‐bearing mice were randomized into treated and non‐treated groups ( n = 5) when the tumor reached a volume of 50 mm 3 . Mice were treated with Niraparib four times per week. One‐way ANOVA followed by the Tukey's multiple‐comparison test were performed for comparison of survival (ns, P > 0.05; * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001). C,D) Size C) and weight D) of tumors formed in female nu/nu mice by ARID1B OE and Control MDA‐MB‐231 cells treated and non‐treated with Niraparib. E) Tumor growth of ARID1B KO and empty vector control (Control) MDA‐MB‐468 in female nu/nu mice measured for a period of 8 weeks. Tumor‐bearing mice were randomized into treated and non‐treated groups ( n = 5) when the tumor reached a volume of 50 mm 3 . Mice were treated with Niraparib four times per week. One‐way ANOVA followed by the Tukey's multiple‐comparison test were performed for comparison of survival (ns, P > 0.05; * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001). F,G) Size F) and weight G) of tumors formed in female nu/nu mice by ARID1B KO and Control MDA‐MB‐468 cells treated and non‐treated with Niraparib. H,I) Body weight of all four groups of mice from Figure H) and Figure I) was measured for a period of 8 weeks. J) 40X IHC of ARID1B and Ki67 in ARID1B KO and Control MDA‐MB‐468 tumors (left panel) and in ARID1B OE and Control MDA‐MB‐231 tumors (right panel) treated with Niraparib or Vehicle (Control). K) IHC analysis of ARID1B and Ki67 positive area (%) in ARID1B KO and Control MDA‐MB‐468 tumors and in ARID1B OE and Control MDA‐MB‐231 tumors treated with Niraparib or Vehicle (Control).

Article Snippet: The following antibodies were used: ARID1B (Abcam, ab‐57461), Ki67 (Cell Signaling Technology, 12202), actin (Sigma, A5441), GAPDH (Sigma, G8795), GAPDH (Novus Biologicals, NB300‐221), ARID1A (D2A8U) (Cell Signaling Technology, 123545), ARID1A (Santa Cruz Biotechnology, sc‐32761), SMARCE1 (Cell Signaling Technology, 33360), SMARCA2 (Cell Signaling Technology, 11966), SMARCA4 (Cell Signaling Technology, 49360), RANBP2 (Abcam, ab64276), RANBP2 (Santa Cruz Biotechnology, 74518), HA (C29F4) (Cell Signaling Technology, 3724), Lamin A/C (Cell Signaling Technology, 2032), Histon H3 (D1H2) (Cell Signaling Technology, 4499), KPNA2 (Santa Cruz Biotechnology, sc‐55538), KPNB1 (Abcam, ab2811), KPNB1 (ABclonal, A8610), Flag (Cell Signaling Technology, 14793S), Flag (Proteintech, 20543‐1‐AP).

Techniques: Drug discovery, In Vivo, Plasmid Preparation, Control, Comparison