cell cycle regulation antibody sampler kit  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cell cycle regulation antibody sampler kit
    Cell Cycle Regulation Antibody Sampler Kit, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cell cycle regulation antibody sampler kit  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cell cycle regulation antibody sampler kit
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    anti cycle d1  (Cell Signaling Technology Inc)


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    chimeric proteins  (Cell Signaling Technology Inc)


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    regulation  (Cell Signaling Technology Inc)


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    regulation  (Cell Signaling Technology Inc)


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    cell cycle regulation antibody sampler kit  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cell cycle regulation antibody sampler kit
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    anti cyclind1 antibodies  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti cyclind1 antibodies
    05D causes G1 phase arrest by inactivating CDK2/CDK4–E2F–Rb and <t>cyclinD1–CDK4–p21</t> checkpoint pathways. Notes: ( A ) HCT116 cells were treated with various concentrations of 05D (5, 10, 20, and 40 μg/mL) for 24 hours and cycle analysis was performed by flow cytometric analysis. ( B ) Cell cycle arrest-associated protein was analyzed by Western blot and the quantitative analysis is displayed. * P <0.05; ** P <0.01. Abbreviation: PI, propidium iodide.
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    1) Product Images from "Sophoridinol derivative 05D induces tumor cells apoptosis by topoisomerase1-mediated DNA breakage"

    Article Title: Sophoridinol derivative 05D induces tumor cells apoptosis by topoisomerase1-mediated DNA breakage

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S103671

    05D causes G1 phase arrest by inactivating CDK2/CDK4–E2F–Rb and cyclinD1–CDK4–p21 checkpoint pathways. Notes: ( A ) HCT116 cells were treated with various concentrations of 05D (5, 10, 20, and 40 μg/mL) for 24 hours and cycle analysis was performed by flow cytometric analysis. ( B ) Cell cycle arrest-associated protein was analyzed by Western blot and the quantitative analysis is displayed. * P <0.05; ** P <0.01. Abbreviation: PI, propidium iodide.
    Figure Legend Snippet: 05D causes G1 phase arrest by inactivating CDK2/CDK4–E2F–Rb and cyclinD1–CDK4–p21 checkpoint pathways. Notes: ( A ) HCT116 cells were treated with various concentrations of 05D (5, 10, 20, and 40 μg/mL) for 24 hours and cycle analysis was performed by flow cytometric analysis. ( B ) Cell cycle arrest-associated protein was analyzed by Western blot and the quantitative analysis is displayed. * P <0.05; ** P <0.01. Abbreviation: PI, propidium iodide.

    Techniques Used: Western Blot

    anti oxidant defense mechanisms  (Cell Signaling Technology Inc)


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    protein kinases mapks  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc protein kinases mapks
    Effect of oxyresveratrol on CXCR4 signaling. ( A ) Jurkat cells were pre-treated with oxyresveratrol (2.5 μg/ml), resveratrol (2.5 μg/ml) or DMSO vehicle for 1 h at 37°C. After extensive washing, the cells were stained with αCXCR4 (1 μg/ml) and FITC-conjugated secondary antibody (1 μg/ml) or not. The expression level of CXCR4 on the cell membrane is shown in the histogram. Data are representative examples of 3 experiments. ( B & C ) The cells, pre-treated with oxyresveratrol or DMSO, were stimulated with SDF-1 (100 ng/ml) for 0 to 15 min. Cell lysates were analyzed by Western blot with <t>primary</t> <t>antibodies</t> (1 μg/ml) against <t>MAPKs</t> ( B ), MEK1/2 ( C ) or their phosphorylated forms ( B & C ) plus secondary antibodies (0.3 μg/ml). The ratio was obtained by normalizing the signal of the phosphorylated protein to that of the total protein. ( D ) A schematic model describing the mechanism by which oxyresveratrol present in M. alba can inhibit inflammation.
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    1) Product Images from "Morus alba and active compound oxyresveratrol exert anti-inflammatory activity via inhibition of leukocyte migration involving MEK/ERK signaling"

    Article Title: Morus alba and active compound oxyresveratrol exert anti-inflammatory activity via inhibition of leukocyte migration involving MEK/ERK signaling

    Journal: BMC Complementary and Alternative Medicine

    doi: 10.1186/1472-6882-13-45

    Effect of oxyresveratrol on CXCR4 signaling. ( A ) Jurkat cells were pre-treated with oxyresveratrol (2.5 μg/ml), resveratrol (2.5 μg/ml) or DMSO vehicle for 1 h at 37°C. After extensive washing, the cells were stained with αCXCR4 (1 μg/ml) and FITC-conjugated secondary antibody (1 μg/ml) or not. The expression level of CXCR4 on the cell membrane is shown in the histogram. Data are representative examples of 3 experiments. ( B & C ) The cells, pre-treated with oxyresveratrol or DMSO, were stimulated with SDF-1 (100 ng/ml) for 0 to 15 min. Cell lysates were analyzed by Western blot with primary antibodies (1 μg/ml) against MAPKs ( B ), MEK1/2 ( C ) or their phosphorylated forms ( B & C ) plus secondary antibodies (0.3 μg/ml). The ratio was obtained by normalizing the signal of the phosphorylated protein to that of the total protein. ( D ) A schematic model describing the mechanism by which oxyresveratrol present in M. alba can inhibit inflammation.
    Figure Legend Snippet: Effect of oxyresveratrol on CXCR4 signaling. ( A ) Jurkat cells were pre-treated with oxyresveratrol (2.5 μg/ml), resveratrol (2.5 μg/ml) or DMSO vehicle for 1 h at 37°C. After extensive washing, the cells were stained with αCXCR4 (1 μg/ml) and FITC-conjugated secondary antibody (1 μg/ml) or not. The expression level of CXCR4 on the cell membrane is shown in the histogram. Data are representative examples of 3 experiments. ( B & C ) The cells, pre-treated with oxyresveratrol or DMSO, were stimulated with SDF-1 (100 ng/ml) for 0 to 15 min. Cell lysates were analyzed by Western blot with primary antibodies (1 μg/ml) against MAPKs ( B ), MEK1/2 ( C ) or their phosphorylated forms ( B & C ) plus secondary antibodies (0.3 μg/ml). The ratio was obtained by normalizing the signal of the phosphorylated protein to that of the total protein. ( D ) A schematic model describing the mechanism by which oxyresveratrol present in M. alba can inhibit inflammation.

    Techniques Used: Staining, Expressing, Western Blot

    9932 cdkn1b p27kip1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc 9932 cdkn1b p27kip1
    NUPR1 depletion causes premature senescence in vitro and represses tumorigenesis in vivo. (A) Representative images of GLB1 activity in NUPR1-depleted and control cells as indicated (left panels). Quantification of GLB1-positive cells was determined in 10 different fields from 3 independent experiments (mean ± SEM) (right panel). Scale bars: 10 µm. (B) NUPR1-depleted A549 cells were collected for cell cycle analysis by flow cytometry. The percentage of cells in G0/G1, S, and G2/M phases from 3 independent experiments is shown (right panel, mean ± SEM). (C) Western blot analysis of the indicated proteins in A549 and H460 cells infected with NUPR1 shRNA, with ACTB as a loading control. (D) Cellular proliferation of control and NUPR1-shRNA A549 cells was assessed using a 5-bromodeoxyuridine (BrdU) assay. The data are represented as the mean ± SEM of 6 experiments. (E) Clonogenic assays performed with control and NUPR1-shRNA A549 cells. A total of 1,500 cells were seeded in 24-well plates and grown for 2 wk. The graph shows the quantification of the mean number of colonies at different time point as indicated. ** P < 0.01 compared to control. (F) Western blot analysis of CASP3, cleaved CASP3, CASP7, CASP9, and ACTB in NUPR1-depleted A549 cells. (G) Western blot analysis of <t>CDKN1B</t> in A549 cells by NUPR1 depletion and/or its reexpression, with ACTB as a loading control. (H) A549 cells with lentivirus-delivered NUPR1 knockdown were subcutaneously implanted into female athymic nude mice (n = 6 for each experimental condition). The tumor image (left panel) on d 24 and tumor growth curve (right panel, mean ± SEM) are shown. ** P < 0.01 compared to control.
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    1) Product Images from "NUPR1 maintains autolysosomal efflux by activating SNAP25 transcription in cancer cells"

    Article Title: NUPR1 maintains autolysosomal efflux by activating SNAP25 transcription in cancer cells

    Journal: Autophagy

    doi: 10.1080/15548627.2017.1338556

    NUPR1 depletion causes premature senescence in vitro and represses tumorigenesis in vivo. (A) Representative images of GLB1 activity in NUPR1-depleted and control cells as indicated (left panels). Quantification of GLB1-positive cells was determined in 10 different fields from 3 independent experiments (mean ± SEM) (right panel). Scale bars: 10 µm. (B) NUPR1-depleted A549 cells were collected for cell cycle analysis by flow cytometry. The percentage of cells in G0/G1, S, and G2/M phases from 3 independent experiments is shown (right panel, mean ± SEM). (C) Western blot analysis of the indicated proteins in A549 and H460 cells infected with NUPR1 shRNA, with ACTB as a loading control. (D) Cellular proliferation of control and NUPR1-shRNA A549 cells was assessed using a 5-bromodeoxyuridine (BrdU) assay. The data are represented as the mean ± SEM of 6 experiments. (E) Clonogenic assays performed with control and NUPR1-shRNA A549 cells. A total of 1,500 cells were seeded in 24-well plates and grown for 2 wk. The graph shows the quantification of the mean number of colonies at different time point as indicated. ** P < 0.01 compared to control. (F) Western blot analysis of CASP3, cleaved CASP3, CASP7, CASP9, and ACTB in NUPR1-depleted A549 cells. (G) Western blot analysis of CDKN1B in A549 cells by NUPR1 depletion and/or its reexpression, with ACTB as a loading control. (H) A549 cells with lentivirus-delivered NUPR1 knockdown were subcutaneously implanted into female athymic nude mice (n = 6 for each experimental condition). The tumor image (left panel) on d 24 and tumor growth curve (right panel, mean ± SEM) are shown. ** P < 0.01 compared to control.
    Figure Legend Snippet: NUPR1 depletion causes premature senescence in vitro and represses tumorigenesis in vivo. (A) Representative images of GLB1 activity in NUPR1-depleted and control cells as indicated (left panels). Quantification of GLB1-positive cells was determined in 10 different fields from 3 independent experiments (mean ± SEM) (right panel). Scale bars: 10 µm. (B) NUPR1-depleted A549 cells were collected for cell cycle analysis by flow cytometry. The percentage of cells in G0/G1, S, and G2/M phases from 3 independent experiments is shown (right panel, mean ± SEM). (C) Western blot analysis of the indicated proteins in A549 and H460 cells infected with NUPR1 shRNA, with ACTB as a loading control. (D) Cellular proliferation of control and NUPR1-shRNA A549 cells was assessed using a 5-bromodeoxyuridine (BrdU) assay. The data are represented as the mean ± SEM of 6 experiments. (E) Clonogenic assays performed with control and NUPR1-shRNA A549 cells. A total of 1,500 cells were seeded in 24-well plates and grown for 2 wk. The graph shows the quantification of the mean number of colonies at different time point as indicated. ** P < 0.01 compared to control. (F) Western blot analysis of CASP3, cleaved CASP3, CASP7, CASP9, and ACTB in NUPR1-depleted A549 cells. (G) Western blot analysis of CDKN1B in A549 cells by NUPR1 depletion and/or its reexpression, with ACTB as a loading control. (H) A549 cells with lentivirus-delivered NUPR1 knockdown were subcutaneously implanted into female athymic nude mice (n = 6 for each experimental condition). The tumor image (left panel) on d 24 and tumor growth curve (right panel, mean ± SEM) are shown. ** P < 0.01 compared to control.

    Techniques Used: In Vitro, In Vivo, Activity Assay, Cell Cycle Assay, Flow Cytometry, Western Blot, Infection, shRNA, BrdU Staining

    Primary antibodies used in this study.
    Figure Legend Snippet: Primary antibodies used in this study.

    Techniques Used:

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    05D causes G1 phase arrest by inactivating CDK2/CDK4–E2F–Rb and <t>cyclinD1–CDK4–p21</t> checkpoint pathways. Notes: ( A ) HCT116 cells were treated with various concentrations of 05D (5, 10, 20, and 40 μg/mL) for 24 hours and cycle analysis was performed by flow cytometric analysis. ( B ) Cell cycle arrest-associated protein was analyzed by Western blot and the quantitative analysis is displayed. * P <0.05; ** P <0.01. Abbreviation: PI, propidium iodide.
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    05D causes G1 phase arrest by inactivating CDK2/CDK4–E2F–Rb and <t>cyclinD1–CDK4–p21</t> checkpoint pathways. Notes: ( A ) HCT116 cells were treated with various concentrations of 05D (5, 10, 20, and 40 μg/mL) for 24 hours and cycle analysis was performed by flow cytometric analysis. ( B ) Cell cycle arrest-associated protein was analyzed by Western blot and the quantitative analysis is displayed. * P <0.05; ** P <0.01. Abbreviation: PI, propidium iodide.
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    Effect of oxyresveratrol on CXCR4 signaling. ( A ) Jurkat cells were pre-treated with oxyresveratrol (2.5 μg/ml), resveratrol (2.5 μg/ml) or DMSO vehicle for 1 h at 37°C. After extensive washing, the cells were stained with αCXCR4 (1 μg/ml) and FITC-conjugated secondary antibody (1 μg/ml) or not. The expression level of CXCR4 on the cell membrane is shown in the histogram. Data are representative examples of 3 experiments. ( B & C ) The cells, pre-treated with oxyresveratrol or DMSO, were stimulated with SDF-1 (100 ng/ml) for 0 to 15 min. Cell lysates were analyzed by Western blot with <t>primary</t> <t>antibodies</t> (1 μg/ml) against <t>MAPKs</t> ( B ), MEK1/2 ( C ) or their phosphorylated forms ( B & C ) plus secondary antibodies (0.3 μg/ml). The ratio was obtained by normalizing the signal of the phosphorylated protein to that of the total protein. ( D ) A schematic model describing the mechanism by which oxyresveratrol present in M. alba can inhibit inflammation.
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    NUPR1 depletion causes premature senescence in vitro and represses tumorigenesis in vivo. (A) Representative images of GLB1 activity in NUPR1-depleted and control cells as indicated (left panels). Quantification of GLB1-positive cells was determined in 10 different fields from 3 independent experiments (mean ± SEM) (right panel). Scale bars: 10 µm. (B) NUPR1-depleted A549 cells were collected for cell cycle analysis by flow cytometry. The percentage of cells in G0/G1, S, and G2/M phases from 3 independent experiments is shown (right panel, mean ± SEM). (C) Western blot analysis of the indicated proteins in A549 and H460 cells infected with NUPR1 shRNA, with ACTB as a loading control. (D) Cellular proliferation of control and NUPR1-shRNA A549 cells was assessed using a 5-bromodeoxyuridine (BrdU) assay. The data are represented as the mean ± SEM of 6 experiments. (E) Clonogenic assays performed with control and NUPR1-shRNA A549 cells. A total of 1,500 cells were seeded in 24-well plates and grown for 2 wk. The graph shows the quantification of the mean number of colonies at different time point as indicated. ** P < 0.01 compared to control. (F) Western blot analysis of CASP3, cleaved CASP3, CASP7, CASP9, and ACTB in NUPR1-depleted A549 cells. (G) Western blot analysis of <t>CDKN1B</t> in A549 cells by NUPR1 depletion and/or its reexpression, with ACTB as a loading control. (H) A549 cells with lentivirus-delivered NUPR1 knockdown were subcutaneously implanted into female athymic nude mice (n = 6 for each experimental condition). The tumor image (left panel) on d 24 and tumor growth curve (right panel, mean ± SEM) are shown. ** P < 0.01 compared to control.
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    05D causes G1 phase arrest by inactivating CDK2/CDK4–E2F–Rb and cyclinD1–CDK4–p21 checkpoint pathways. Notes: ( A ) HCT116 cells were treated with various concentrations of 05D (5, 10, 20, and 40 μg/mL) for 24 hours and cycle analysis was performed by flow cytometric analysis. ( B ) Cell cycle arrest-associated protein was analyzed by Western blot and the quantitative analysis is displayed. * P <0.05; ** P <0.01. Abbreviation: PI, propidium iodide.

    Journal: OncoTargets and therapy

    Article Title: Sophoridinol derivative 05D induces tumor cells apoptosis by topoisomerase1-mediated DNA breakage

    doi: 10.2147/OTT.S103671

    Figure Lengend Snippet: 05D causes G1 phase arrest by inactivating CDK2/CDK4–E2F–Rb and cyclinD1–CDK4–p21 checkpoint pathways. Notes: ( A ) HCT116 cells were treated with various concentrations of 05D (5, 10, 20, and 40 μg/mL) for 24 hours and cycle analysis was performed by flow cytometric analysis. ( B ) Cell cycle arrest-associated protein was analyzed by Western blot and the quantitative analysis is displayed. * P <0.05; ** P <0.01. Abbreviation: PI, propidium iodide.

    Article Snippet: Anti-γ-H2AX, anti-caspase 3, anti-caspase 7, anti-PARP, anti-phospho-DNA-PK, anti-DNA-PK, anti-phospho-ataxia telangiectasia mutated (ATM), anti-phospho-ATM and rad3-related (ATR), anti-ATM, anti-ATR, anti-cdc25A, anti-phospho-cdc25A, anti-phospho-cdc2 anti-cdc25A, anti-cdc2, anti-E2F, and anti-cyclinD1 antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA), γ-H2AX antibody conjugated fluorescein isothiocyanate (FITC) was from BD (Franklin Lakes, NJ, USA).

    Techniques: Western Blot

    Effect of oxyresveratrol on CXCR4 signaling. ( A ) Jurkat cells were pre-treated with oxyresveratrol (2.5 μg/ml), resveratrol (2.5 μg/ml) or DMSO vehicle for 1 h at 37°C. After extensive washing, the cells were stained with αCXCR4 (1 μg/ml) and FITC-conjugated secondary antibody (1 μg/ml) or not. The expression level of CXCR4 on the cell membrane is shown in the histogram. Data are representative examples of 3 experiments. ( B & C ) The cells, pre-treated with oxyresveratrol or DMSO, were stimulated with SDF-1 (100 ng/ml) for 0 to 15 min. Cell lysates were analyzed by Western blot with primary antibodies (1 μg/ml) against MAPKs ( B ), MEK1/2 ( C ) or their phosphorylated forms ( B & C ) plus secondary antibodies (0.3 μg/ml). The ratio was obtained by normalizing the signal of the phosphorylated protein to that of the total protein. ( D ) A schematic model describing the mechanism by which oxyresveratrol present in M. alba can inhibit inflammation.

    Journal: BMC Complementary and Alternative Medicine

    Article Title: Morus alba and active compound oxyresveratrol exert anti-inflammatory activity via inhibition of leukocyte migration involving MEK/ERK signaling

    doi: 10.1186/1472-6882-13-45

    Figure Lengend Snippet: Effect of oxyresveratrol on CXCR4 signaling. ( A ) Jurkat cells were pre-treated with oxyresveratrol (2.5 μg/ml), resveratrol (2.5 μg/ml) or DMSO vehicle for 1 h at 37°C. After extensive washing, the cells were stained with αCXCR4 (1 μg/ml) and FITC-conjugated secondary antibody (1 μg/ml) or not. The expression level of CXCR4 on the cell membrane is shown in the histogram. Data are representative examples of 3 experiments. ( B & C ) The cells, pre-treated with oxyresveratrol or DMSO, were stimulated with SDF-1 (100 ng/ml) for 0 to 15 min. Cell lysates were analyzed by Western blot with primary antibodies (1 μg/ml) against MAPKs ( B ), MEK1/2 ( C ) or their phosphorylated forms ( B & C ) plus secondary antibodies (0.3 μg/ml). The ratio was obtained by normalizing the signal of the phosphorylated protein to that of the total protein. ( D ) A schematic model describing the mechanism by which oxyresveratrol present in M. alba can inhibit inflammation.

    Article Snippet: Antibodies against mitogen-activated protein kinases (MAPKs) and their phosphorylated proteins were purchased from Cell Signaling Technology (MA, USA).

    Techniques: Staining, Expressing, Western Blot

    NUPR1 depletion causes premature senescence in vitro and represses tumorigenesis in vivo. (A) Representative images of GLB1 activity in NUPR1-depleted and control cells as indicated (left panels). Quantification of GLB1-positive cells was determined in 10 different fields from 3 independent experiments (mean ± SEM) (right panel). Scale bars: 10 µm. (B) NUPR1-depleted A549 cells were collected for cell cycle analysis by flow cytometry. The percentage of cells in G0/G1, S, and G2/M phases from 3 independent experiments is shown (right panel, mean ± SEM). (C) Western blot analysis of the indicated proteins in A549 and H460 cells infected with NUPR1 shRNA, with ACTB as a loading control. (D) Cellular proliferation of control and NUPR1-shRNA A549 cells was assessed using a 5-bromodeoxyuridine (BrdU) assay. The data are represented as the mean ± SEM of 6 experiments. (E) Clonogenic assays performed with control and NUPR1-shRNA A549 cells. A total of 1,500 cells were seeded in 24-well plates and grown for 2 wk. The graph shows the quantification of the mean number of colonies at different time point as indicated. ** P < 0.01 compared to control. (F) Western blot analysis of CASP3, cleaved CASP3, CASP7, CASP9, and ACTB in NUPR1-depleted A549 cells. (G) Western blot analysis of CDKN1B in A549 cells by NUPR1 depletion and/or its reexpression, with ACTB as a loading control. (H) A549 cells with lentivirus-delivered NUPR1 knockdown were subcutaneously implanted into female athymic nude mice (n = 6 for each experimental condition). The tumor image (left panel) on d 24 and tumor growth curve (right panel, mean ± SEM) are shown. ** P < 0.01 compared to control.

    Journal: Autophagy

    Article Title: NUPR1 maintains autolysosomal efflux by activating SNAP25 transcription in cancer cells

    doi: 10.1080/15548627.2017.1338556

    Figure Lengend Snippet: NUPR1 depletion causes premature senescence in vitro and represses tumorigenesis in vivo. (A) Representative images of GLB1 activity in NUPR1-depleted and control cells as indicated (left panels). Quantification of GLB1-positive cells was determined in 10 different fields from 3 independent experiments (mean ± SEM) (right panel). Scale bars: 10 µm. (B) NUPR1-depleted A549 cells were collected for cell cycle analysis by flow cytometry. The percentage of cells in G0/G1, S, and G2/M phases from 3 independent experiments is shown (right panel, mean ± SEM). (C) Western blot analysis of the indicated proteins in A549 and H460 cells infected with NUPR1 shRNA, with ACTB as a loading control. (D) Cellular proliferation of control and NUPR1-shRNA A549 cells was assessed using a 5-bromodeoxyuridine (BrdU) assay. The data are represented as the mean ± SEM of 6 experiments. (E) Clonogenic assays performed with control and NUPR1-shRNA A549 cells. A total of 1,500 cells were seeded in 24-well plates and grown for 2 wk. The graph shows the quantification of the mean number of colonies at different time point as indicated. ** P < 0.01 compared to control. (F) Western blot analysis of CASP3, cleaved CASP3, CASP7, CASP9, and ACTB in NUPR1-depleted A549 cells. (G) Western blot analysis of CDKN1B in A549 cells by NUPR1 depletion and/or its reexpression, with ACTB as a loading control. (H) A549 cells with lentivirus-delivered NUPR1 knockdown were subcutaneously implanted into female athymic nude mice (n = 6 for each experimental condition). The tumor image (left panel) on d 24 and tumor growth curve (right panel, mean ± SEM) are shown. ** P < 0.01 compared to control.

    Article Snippet: DNA sequences for shRNA are listed in Table S2 . table ft1 table-wrap mode="anchored" t5 Table 1. caption a7 Primary Antibody Dilution Ratio Supplier ATG5 (rabbit polyclonal) 1:1,000 Cell Signaling Technology, 2630 ACTB (mouse monoclonal) 1:3,000 Sigma-Aldrich, A-3853 BECN1(rabbit polyclonal) 1:2,000 Cell Signaling Technology, 3738 CASP3 (rabbit polyclonal) 1:1000 Cell Signaling Technology, 9665 CDKN1A/p21Waf1 (rabbit monoclonal) 1:2,000 Cell Signaling Technology, 9932 CDKN1B/p27Kip1(rabbit monoclonal) 1:2,000 Cell Signaling Technology, 9932 CDKN2A/p16INK4a (rabbit monoclonal) 1:2,000 Abcam, ab108349 CTSB (mouse monoclonal) 1:1,000 Santa Cruz Biotechnology, sc-365558 CTSD (mouse monoclonal) 1:1,000 Santa Cruz Biotechnology, sc-377299 Cleaved CASP3 (rabbit polyclonal) 1:1000 Cell Signaling Technology, 9664 Cleaved CASP7 (rabbit polyclonal) 1:1000 Cell Signaling Technology, 8438 Cleaved CASP9 (rabbit polyclonal) 1:1000 Cell Signaling Technology, 7237 FLAG (mouse monoclonal) 1:4,000 Sigma-Aldrich, F3165 GAPDH (rabbit polyclonal) 1:3,000 Trevigen, 2275 HA (rabbit monoclonal) 1:2.000 Cell Signaling Technology, 3724S LC3B (rabbit polyclonal) 1:2,000 Sigma-Aldrich, L7543 MTOR (rabbit monoclonal) 1:2,000 Cell Signaling Technology, 2983 NUPR1 (mouse monoclonal) 1:1,000 Abcam, ab87454 p-MTOR(S2448) (rabbit monoclonal) 1:2,000 Cell Signaling Technology, 5536 PCNA (rabbit polyclonal) 1:1,000 Abcam, ab18197 SNAP25 (rabbit polyclonal) 1:1,000 Abcam, ab109105 SQSTM1/p62 (rabbit polyclonal) 1:1,000 Cell Signaling Technology, 7695 VAMP8 (mouse monoclonal) 1:1,000 Santa Cruz Biotechnology, sc-166820 Open in a separate window Primary antibodies used in this study.

    Techniques: In Vitro, In Vivo, Activity Assay, Cell Cycle Assay, Flow Cytometry, Western Blot, Infection, shRNA, BrdU Staining

    Primary antibodies used in this study.

    Journal: Autophagy

    Article Title: NUPR1 maintains autolysosomal efflux by activating SNAP25 transcription in cancer cells

    doi: 10.1080/15548627.2017.1338556

    Figure Lengend Snippet: Primary antibodies used in this study.

    Article Snippet: DNA sequences for shRNA are listed in Table S2 . table ft1 table-wrap mode="anchored" t5 Table 1. caption a7 Primary Antibody Dilution Ratio Supplier ATG5 (rabbit polyclonal) 1:1,000 Cell Signaling Technology, 2630 ACTB (mouse monoclonal) 1:3,000 Sigma-Aldrich, A-3853 BECN1(rabbit polyclonal) 1:2,000 Cell Signaling Technology, 3738 CASP3 (rabbit polyclonal) 1:1000 Cell Signaling Technology, 9665 CDKN1A/p21Waf1 (rabbit monoclonal) 1:2,000 Cell Signaling Technology, 9932 CDKN1B/p27Kip1(rabbit monoclonal) 1:2,000 Cell Signaling Technology, 9932 CDKN2A/p16INK4a (rabbit monoclonal) 1:2,000 Abcam, ab108349 CTSB (mouse monoclonal) 1:1,000 Santa Cruz Biotechnology, sc-365558 CTSD (mouse monoclonal) 1:1,000 Santa Cruz Biotechnology, sc-377299 Cleaved CASP3 (rabbit polyclonal) 1:1000 Cell Signaling Technology, 9664 Cleaved CASP7 (rabbit polyclonal) 1:1000 Cell Signaling Technology, 8438 Cleaved CASP9 (rabbit polyclonal) 1:1000 Cell Signaling Technology, 7237 FLAG (mouse monoclonal) 1:4,000 Sigma-Aldrich, F3165 GAPDH (rabbit polyclonal) 1:3,000 Trevigen, 2275 HA (rabbit monoclonal) 1:2.000 Cell Signaling Technology, 3724S LC3B (rabbit polyclonal) 1:2,000 Sigma-Aldrich, L7543 MTOR (rabbit monoclonal) 1:2,000 Cell Signaling Technology, 2983 NUPR1 (mouse monoclonal) 1:1,000 Abcam, ab87454 p-MTOR(S2448) (rabbit monoclonal) 1:2,000 Cell Signaling Technology, 5536 PCNA (rabbit polyclonal) 1:1,000 Abcam, ab18197 SNAP25 (rabbit polyclonal) 1:1,000 Abcam, ab109105 SQSTM1/p62 (rabbit polyclonal) 1:1,000 Cell Signaling Technology, 7695 VAMP8 (mouse monoclonal) 1:1,000 Santa Cruz Biotechnology, sc-166820 Open in a separate window Primary antibodies used in this study.

    Techniques: