rabbit polyclonal anti adam9 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit polyclonal anti adam9 antibody
    Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection
    Rabbit Polyclonal Anti Adam9 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti adam9 antibody/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti adam9 antibody - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Global secretome characterization of A549 human alveolar epithelial carcinoma cells during Mycoplasma pneumoniae infection"

    Article Title: Global secretome characterization of A549 human alveolar epithelial carcinoma cells during Mycoplasma pneumoniae infection

    Journal: BMC Microbiology

    doi: 10.1186/1471-2180-14-27

    Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection
    Figure Legend Snippet: Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection

    Techniques Used: Migration

    rabbit polyclonal anti adam9 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit polyclonal anti adam9 antibody
    Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection
    Rabbit Polyclonal Anti Adam9 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti adam9 antibody/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti adam9 antibody - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Global secretome characterization of A549 human alveolar epithelial carcinoma cells during Mycoplasma pneumoniae infection"

    Article Title: Global secretome characterization of A549 human alveolar epithelial carcinoma cells during Mycoplasma pneumoniae infection

    Journal: BMC Microbiology

    doi: 10.1186/1471-2180-14-27

    Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection
    Figure Legend Snippet: Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection

    Techniques Used: Migration

    adam9  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc adam9
    (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of <t>ADAM9</t> (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.
    Adam9, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adam9/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adam9 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling"

    Article Title: Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0087014

    (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.
    Figure Legend Snippet: (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Techniques Used: Transfection, Expressing, Western Blot

    (A) and (B) SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4 and combinations of 3 nM siRNA for knock-down of ADAM9 (A9) and ADAM10 (A10), ADAM9 (A9) and ADAM17 (A17), ADAM10 (A10) and ADAM17 (A17) in (A) or ADAM9, 10 and 17 or ADAM9, 10, 17 and MMP9 in (B), were treated with 1 µM prucalopride (5-HT 4 receptor agonist) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) (B) and secretion of sAPPα was analyzed via measuring SEAP. (C) Cell lysates of experiments in (A) and (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.
    Figure Legend Snippet: (A) and (B) SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4 and combinations of 3 nM siRNA for knock-down of ADAM9 (A9) and ADAM10 (A10), ADAM9 (A9) and ADAM17 (A17), ADAM10 (A10) and ADAM17 (A17) in (A) or ADAM9, 10 and 17 or ADAM9, 10, 17 and MMP9 in (B), were treated with 1 µM prucalopride (5-HT 4 receptor agonist) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) (B) and secretion of sAPPα was analyzed via measuring SEAP. (C) Cell lysates of experiments in (A) and (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Techniques Used: Transfection, Expressing, Western Blot

    mmp 9 g657  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc mmp 9 g657
    (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and <t>MMP9</t> and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.
    Mmp 9 G657, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    mmp 9 g657 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling"

    Article Title: Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0087014

    (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.
    Figure Legend Snippet: (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Techniques Used: Transfection, Expressing, Western Blot

    (A) and (B) SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4 and combinations of 3 nM siRNA for knock-down of ADAM9 (A9) and ADAM10 (A10), ADAM9 (A9) and ADAM17 (A17), ADAM10 (A10) and ADAM17 (A17) in (A) or ADAM9, 10 and 17 or ADAM9, 10, 17 and MMP9 in (B), were treated with 1 µM prucalopride (5-HT 4 receptor agonist) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) (B) and secretion of sAPPα was analyzed via measuring SEAP. (C) Cell lysates of experiments in (A) and (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.
    Figure Legend Snippet: (A) and (B) SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4 and combinations of 3 nM siRNA for knock-down of ADAM9 (A9) and ADAM10 (A10), ADAM9 (A9) and ADAM17 (A17), ADAM10 (A10) and ADAM17 (A17) in (A) or ADAM9, 10 and 17 or ADAM9, 10, 17 and MMP9 in (B), were treated with 1 µM prucalopride (5-HT 4 receptor agonist) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) (B) and secretion of sAPPα was analyzed via measuring SEAP. (C) Cell lysates of experiments in (A) and (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Techniques Used: Transfection, Expressing, Western Blot

    adam9  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc adam9
    (A) Quantitative RT-PCR of CDH2 in the aggressive cell line BM7 and its control line, CL1-0; 18S rRNA was used as a loading control. **, P <0.005. (B) Western blot analysis of <t>ADAM9</t> and CDH2 in BM7 and CL1-0 cells. L: long form of ADAM9; S: short form of ADAM9. EF1A was used as a loading control. EF1A: elongation factor 1 alpha. (C) Relative expression levels of CDH2 in BM7 cells transfected with two siRNAs against ADAM9. Two primer sets (I and II) targeting different CDH2 regions were used to amplify the CDH2 products. Two short hairpin RNAs targeted against ADAM9 (sh ADAM9 -C & sh ADAM9 -E) were examined. HPRT was used as a loading control. *, P <0.05. (D) Western blot analysis of CDH2 in the ADAM9 -depleted BM7 cells. EF1A was used as a loading control. CDH1: E-cadherin; VIM: vimentin. (E) Immunohistochemistry analysis of ADAM9 and CDH2 in the ADAM9 -depleted cells. Scale bar: 20 μm. (F) Western blot analysis of CDH2 in parental cells over-expressing ADAM9 . ACTB was used as a loading control.
    Adam9, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "ADAM9 Up-Regulates N-Cadherin via miR-218 Suppression in Lung Adenocarcinoma Cells"

    Article Title: ADAM9 Up-Regulates N-Cadherin via miR-218 Suppression in Lung Adenocarcinoma Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0094065

    (A) Quantitative RT-PCR of CDH2 in the aggressive cell line BM7 and its control line, CL1-0; 18S rRNA was used as a loading control. **, P <0.005. (B) Western blot analysis of ADAM9 and CDH2 in BM7 and CL1-0 cells. L: long form of ADAM9; S: short form of ADAM9. EF1A was used as a loading control. EF1A: elongation factor 1 alpha. (C) Relative expression levels of CDH2 in BM7 cells transfected with two siRNAs against ADAM9. Two primer sets (I and II) targeting different CDH2 regions were used to amplify the CDH2 products. Two short hairpin RNAs targeted against ADAM9 (sh ADAM9 -C & sh ADAM9 -E) were examined. HPRT was used as a loading control. *, P <0.05. (D) Western blot analysis of CDH2 in the ADAM9 -depleted BM7 cells. EF1A was used as a loading control. CDH1: E-cadherin; VIM: vimentin. (E) Immunohistochemistry analysis of ADAM9 and CDH2 in the ADAM9 -depleted cells. Scale bar: 20 μm. (F) Western blot analysis of CDH2 in parental cells over-expressing ADAM9 . ACTB was used as a loading control.
    Figure Legend Snippet: (A) Quantitative RT-PCR of CDH2 in the aggressive cell line BM7 and its control line, CL1-0; 18S rRNA was used as a loading control. **, P <0.005. (B) Western blot analysis of ADAM9 and CDH2 in BM7 and CL1-0 cells. L: long form of ADAM9; S: short form of ADAM9. EF1A was used as a loading control. EF1A: elongation factor 1 alpha. (C) Relative expression levels of CDH2 in BM7 cells transfected with two siRNAs against ADAM9. Two primer sets (I and II) targeting different CDH2 regions were used to amplify the CDH2 products. Two short hairpin RNAs targeted against ADAM9 (sh ADAM9 -C & sh ADAM9 -E) were examined. HPRT was used as a loading control. *, P <0.05. (D) Western blot analysis of CDH2 in the ADAM9 -depleted BM7 cells. EF1A was used as a loading control. CDH1: E-cadherin; VIM: vimentin. (E) Immunohistochemistry analysis of ADAM9 and CDH2 in the ADAM9 -depleted cells. Scale bar: 20 μm. (F) Western blot analysis of CDH2 in parental cells over-expressing ADAM9 . ACTB was used as a loading control.

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing, Transfection, Immunohistochemistry

    The expression levels of ADAM9 (A), SLIT2 (B), miR-218 (C), and CDH2 (D) were measured in BM7 cells transfected with short hairpin RNAs targeted against ADAM9 . 18S rRNA was used as a loading control for ADAM9 , SLIT2 , and CDH2 ; miR-191 was used as a loading control for miR-218. *, P <0.05. (E) Proposed model for the role of ADAM9 in the regulation of CDH2 through the inhibition of miR-218.
    Figure Legend Snippet: The expression levels of ADAM9 (A), SLIT2 (B), miR-218 (C), and CDH2 (D) were measured in BM7 cells transfected with short hairpin RNAs targeted against ADAM9 . 18S rRNA was used as a loading control for ADAM9 , SLIT2 , and CDH2 ; miR-191 was used as a loading control for miR-218. *, P <0.05. (E) Proposed model for the role of ADAM9 in the regulation of CDH2 through the inhibition of miR-218.

    Techniques Used: Expressing, Transfection, Inhibition

    adam9  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc adam9
    Expression of <t>ADAM9</t> in ARPE-19 cells exposed to HG. ( A ) mRNA levels of ADAM9. ( B ) Representative image of ADAM9 protein expression. ( C ) Quantification of densitometries of Western blot bands. Data are expressed as mean ± SD of fold induction relative to β-Actin ( n = 3). *** p < 0.001 vs. CTR.
    Adam9, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adam9/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adam9 - by Bioz Stars, 2023-02
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    Images

    1) Product Images from "High Glucose Impairs Expression and Activation of MerTK in ARPE-19 Cells"

    Article Title: High Glucose Impairs Expression and Activation of MerTK in ARPE-19 Cells

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms23031144

    Expression of ADAM9 in ARPE-19 cells exposed to HG. ( A ) mRNA levels of ADAM9. ( B ) Representative image of ADAM9 protein expression. ( C ) Quantification of densitometries of Western blot bands. Data are expressed as mean ± SD of fold induction relative to β-Actin ( n = 3). *** p < 0.001 vs. CTR.
    Figure Legend Snippet: Expression of ADAM9 in ARPE-19 cells exposed to HG. ( A ) mRNA levels of ADAM9. ( B ) Representative image of ADAM9 protein expression. ( C ) Quantification of densitometries of Western blot bands. Data are expressed as mean ± SD of fold induction relative to β-Actin ( n = 3). *** p < 0.001 vs. CTR.

    Techniques Used: Expressing, Western Blot

    Expression of ADAM9 in ARPE-19 cells cultured for 24 h in standard medium (CTR) and in presence of high glucose (HG), silencing (INHIB), and upregulating (MIM) miR-126 under control conditions. ( A , E ) ADAM9 gene expression normalized vs. housekeeping genes. ( B , F ) Representative Western blot of ADAM9 protein expression with quantification of densitometries of both precursor ( C , G ) and active form ( D , H ). Data are expressed as mean ± SD of fold induction relative to β-actin of three independent experiments ( n = 3). ** p < 0.01 and *** p < 0.001 vs. CTR; § p < 0.05 HG + INHIB vs. HG; §§ p < 0.01 and §§§ p < 0.001 HG + MIM vs. HG.
    Figure Legend Snippet: Expression of ADAM9 in ARPE-19 cells cultured for 24 h in standard medium (CTR) and in presence of high glucose (HG), silencing (INHIB), and upregulating (MIM) miR-126 under control conditions. ( A , E ) ADAM9 gene expression normalized vs. housekeeping genes. ( B , F ) Representative Western blot of ADAM9 protein expression with quantification of densitometries of both precursor ( C , G ) and active form ( D , H ). Data are expressed as mean ± SD of fold induction relative to β-actin of three independent experiments ( n = 3). ** p < 0.01 and *** p < 0.001 vs. CTR; § p < 0.05 HG + INHIB vs. HG; §§ p < 0.01 and §§§ p < 0.001 HG + MIM vs. HG.

    Techniques Used: Expressing, Cell Culture, Inhibition, Western Blot

    anti adam9 antibodies  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti adam9 antibodies
    Effect of comp 27 on the Expression of ADAM family. (A) Western blot analysis of <t>ADAM9,</t> 10 and 17 after comp 27 treatment. (B) Comp 27 dose-dependently increased the levels of precursor and active ADAM9. (C) Comp 27 dose-dependently increased the levels of precursor and active ADAM10. (D) Comp 27 did not change the levels of both precursor and active ADAM17. * p <0.05, ** p <0.01, and *** p <0.001 compared to the control group.
    Anti Adam9 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    Images

    1) Product Images from "3’-O-Acetyl-24-Epi-7,8-Didehydrocimigenol-3-O-β-D-Xylopryranoside Decreases Amyloid Beta Production in Amyloid Precursor Protein-Transfected HeLa Cells"

    Article Title: 3’-O-Acetyl-24-Epi-7,8-Didehydrocimigenol-3-O-β-D-Xylopryranoside Decreases Amyloid Beta Production in Amyloid Precursor Protein-Transfected HeLa Cells

    Journal: Biomolecules & Therapeutics

    doi: 10.4062/biomolther.2020.195

    Effect of comp 27 on the Expression of ADAM family. (A) Western blot analysis of ADAM9, 10 and 17 after comp 27 treatment. (B) Comp 27 dose-dependently increased the levels of precursor and active ADAM9. (C) Comp 27 dose-dependently increased the levels of precursor and active ADAM10. (D) Comp 27 did not change the levels of both precursor and active ADAM17. * p <0.05, ** p <0.01, and *** p <0.001 compared to the control group.
    Figure Legend Snippet: Effect of comp 27 on the Expression of ADAM family. (A) Western blot analysis of ADAM9, 10 and 17 after comp 27 treatment. (B) Comp 27 dose-dependently increased the levels of precursor and active ADAM9. (C) Comp 27 dose-dependently increased the levels of precursor and active ADAM10. (D) Comp 27 did not change the levels of both precursor and active ADAM17. * p <0.05, ** p <0.01, and *** p <0.001 compared to the control group.

    Techniques Used: Expressing, Western Blot

    anti adam9 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti adam9 antibody
    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or <t>ADAM9</t> knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Anti Adam9 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti adam9 antibody/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti adam9 antibody - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy"

    Article Title: Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy

    Journal: American Journal of Cancer Research

    doi:

    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Figure Legend Snippet: RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.

    Techniques Used: MTT Assay, Concentration Assay

    RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.
    Figure Legend Snippet: RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.

    Techniques Used: Western Blot, Quantitative RT-PCR, Expressing

    RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.
    Figure Legend Snippet: RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.

    Techniques Used: Immunoprecipitation, Western Blot, Expressing

    The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.
    Figure Legend Snippet: The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.

    Techniques Used:

    adam9  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc adam9
    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or <t>ADAM9</t> knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Adam9, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adam9/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adam9 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy"

    Article Title: Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy

    Journal: American Journal of Cancer Research

    doi:

    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Figure Legend Snippet: RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.

    Techniques Used: MTT Assay, Concentration Assay

    RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.
    Figure Legend Snippet: RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.

    Techniques Used: Western Blot, Quantitative RT-PCR, Expressing

    RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.
    Figure Legend Snippet: RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.

    Techniques Used: Immunoprecipitation, Western Blot, Expressing

    The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.
    Figure Legend Snippet: The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.

    Techniques Used:

    adam9  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc adam9
    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or <t>ADAM9</t> knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Adam9, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adam9/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adam9 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy"

    Article Title: Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy

    Journal: American Journal of Cancer Research

    doi:

    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Figure Legend Snippet: RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.

    Techniques Used: MTT Assay, Concentration Assay

    RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.
    Figure Legend Snippet: RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.

    Techniques Used: Western Blot, Quantitative RT-PCR, Expressing

    RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.
    Figure Legend Snippet: RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.

    Techniques Used: Immunoprecipitation, Western Blot, Expressing

    The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.
    Figure Legend Snippet: The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.

    Techniques Used:

    anti adam9 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti adam9 antibody
    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or <t>ADAM9</t> knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Anti Adam9 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti adam9 antibody/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti adam9 antibody - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy"

    Article Title: Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy

    Journal: American Journal of Cancer Research

    doi:

    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Figure Legend Snippet: RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.

    Techniques Used: MTT Assay, Concentration Assay

    RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.
    Figure Legend Snippet: RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.

    Techniques Used: Western Blot, Quantitative RT-PCR, Expressing

    RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.
    Figure Legend Snippet: RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.

    Techniques Used: Immunoprecipitation, Western Blot, Expressing

    The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.
    Figure Legend Snippet: The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.

    Techniques Used:

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    Cell Signaling Technology Inc rabbit polyclonal anti adam9 antibody
    Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection
    Rabbit Polyclonal Anti Adam9 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti adam9 antibody/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc adam9
    (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of <t>ADAM9</t> (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.
    Adam9, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc mmp 9 g657
    (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and <t>MMP9</t> and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.
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    Cell Signaling Technology Inc anti adam9 antibodies
    Effect of comp 27 on the Expression of ADAM family. (A) Western blot analysis of <t>ADAM9,</t> 10 and 17 after comp 27 treatment. (B) Comp 27 dose-dependently increased the levels of precursor and active ADAM9. (C) Comp 27 dose-dependently increased the levels of precursor and active ADAM10. (D) Comp 27 did not change the levels of both precursor and active ADAM17. * p <0.05, ** p <0.01, and *** p <0.001 compared to the control group.
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    Cell Signaling Technology Inc anti adam9 antibody
    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or <t>ADAM9</t> knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.
    Anti Adam9 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti adam9 antibody/product/Cell Signaling Technology Inc
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    Image Search Results


    Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection

    Journal: BMC Microbiology

    Article Title: Global secretome characterization of A549 human alveolar epithelial carcinoma cells during Mycoplasma pneumoniae infection

    doi: 10.1186/1471-2180-14-27

    Figure Lengend Snippet: Immune response and stress related proteins that were up-regulated by Mycoplasma pneumoniae infection

    Article Snippet: The primary antibodies utilized included rabbit polyclonal anti-ADAM9 antibody (Cell Signaling Technolgoy, Beverly, MA, USA, diluted 1:1000), rabbit polyclonal anti-Gal1 antibody (Proteintech, Chicago, IL, diluted 1:1500), rabbit polyclonal anti-MIF antibody (Proteintech, diluted 1:2000), rabbit polyclonal anti-IL33 antibody (Proteintech, diluted 1:600), rabbit polyclonal anti-SERPINE1 antibody (Proteintech, diluted 1:800), rabbit polyclonal anti-IGFBP4 antibody (Millipore, diluted 1:1000), mouse monoclonal anti-β-actin antibody (Upstate, Lake Placid, NY, diluted 1:3000).

    Techniques: Migration

    (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Journal: PLoS ONE

    Article Title: Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling

    doi: 10.1371/journal.pone.0087014

    Figure Lengend Snippet: (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Article Snippet: Following antibodies were purchased: CK2 α (H-286) from Santa Cruz, MMP-9 (G657) and ADAM9 (2099) from Cell Signaling, ADAM17 (T5442) and β-Actin (A5441) from Sigma-Aldrich.

    Techniques: Transfection, Expressing, Western Blot

    (A) and (B) SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4 and combinations of 3 nM siRNA for knock-down of ADAM9 (A9) and ADAM10 (A10), ADAM9 (A9) and ADAM17 (A17), ADAM10 (A10) and ADAM17 (A17) in (A) or ADAM9, 10 and 17 or ADAM9, 10, 17 and MMP9 in (B), were treated with 1 µM prucalopride (5-HT 4 receptor agonist) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) (B) and secretion of sAPPα was analyzed via measuring SEAP. (C) Cell lysates of experiments in (A) and (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Journal: PLoS ONE

    Article Title: Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling

    doi: 10.1371/journal.pone.0087014

    Figure Lengend Snippet: (A) and (B) SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4 and combinations of 3 nM siRNA for knock-down of ADAM9 (A9) and ADAM10 (A10), ADAM9 (A9) and ADAM17 (A17), ADAM10 (A10) and ADAM17 (A17) in (A) or ADAM9, 10 and 17 or ADAM9, 10, 17 and MMP9 in (B), were treated with 1 µM prucalopride (5-HT 4 receptor agonist) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) (B) and secretion of sAPPα was analyzed via measuring SEAP. (C) Cell lysates of experiments in (A) and (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Article Snippet: Following antibodies were purchased: CK2 α (H-286) from Santa Cruz, MMP-9 (G657) and ADAM9 (2099) from Cell Signaling, ADAM17 (T5442) and β-Actin (A5441) from Sigma-Aldrich.

    Techniques: Transfection, Expressing, Western Blot

    (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Journal: PLoS ONE

    Article Title: Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling

    doi: 10.1371/journal.pone.0087014

    Figure Lengend Snippet: (A) SH-SY5Y cells, transfected with pEAK12-AP-APP and pcDNA3.1-5-HT 4d , were treated with 1 µM prucalopride or 5-HT (5-HT 4 receptor agonists) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) and secretion of sAPPα was analyzed via measuring SEAP. (B) SEAP levels were measured in supernatants of SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4d and 3 nM siRNA for knock-down of ADAM9 (A9), ADAM10 (A10), ADAM17 (A17) and MMP9 and treated with 1 µM prucalopride. (C) Cell lysates of (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. The ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. * P <0.05, ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Article Snippet: Following antibodies were purchased: CK2 α (H-286) from Santa Cruz, MMP-9 (G657) and ADAM9 (2099) from Cell Signaling, ADAM17 (T5442) and β-Actin (A5441) from Sigma-Aldrich.

    Techniques: Transfection, Expressing, Western Blot

    (A) and (B) SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4 and combinations of 3 nM siRNA for knock-down of ADAM9 (A9) and ADAM10 (A10), ADAM9 (A9) and ADAM17 (A17), ADAM10 (A10) and ADAM17 (A17) in (A) or ADAM9, 10 and 17 or ADAM9, 10, 17 and MMP9 in (B), were treated with 1 µM prucalopride (5-HT 4 receptor agonist) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) (B) and secretion of sAPPα was analyzed via measuring SEAP. (C) Cell lysates of experiments in (A) and (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Journal: PLoS ONE

    Article Title: Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling

    doi: 10.1371/journal.pone.0087014

    Figure Lengend Snippet: (A) and (B) SH-SY5Y cells, co-transfected with pEAK12-AP-APP, pcDNA3.1-5-HT 4 and combinations of 3 nM siRNA for knock-down of ADAM9 (A9) and ADAM10 (A10), ADAM9 (A9) and ADAM17 (A17), ADAM10 (A10) and ADAM17 (A17) in (A) or ADAM9, 10 and 17 or ADAM9, 10, 17 and MMP9 in (B), were treated with 1 µM prucalopride (5-HT 4 receptor agonist) in the absence or presence of 80 µM GM6001 (metalloproteinases inhibitor) (B) and secretion of sAPPα was analyzed via measuring SEAP. (C) Cell lysates of experiments in (A) and (B) were analyzed for protein expression of ADAM9, 10, 17 and MMP9 by western blotting. ADAM10 and ADAM17 immature precursor proteins are indicated by an x, whereas the mature catalytically active forms are indicated by an xx for ADAM9, 17 and MMP9. The immature ADAM9 and the mature ADAM10 proteins were not visible. (D) Quantification of experiments in (C). Values shown are mean ± SEM of 6 individual wells and were normalized to vehicle control. ** P <0.01, *** P <0.001, one-way ANOVA with Tukey-Kramer's post-hoc test.

    Article Snippet: Following antibodies were purchased: CK2 α (H-286) from Santa Cruz, MMP-9 (G657) and ADAM9 (2099) from Cell Signaling, ADAM17 (T5442) and β-Actin (A5441) from Sigma-Aldrich.

    Techniques: Transfection, Expressing, Western Blot

    Effect of comp 27 on the Expression of ADAM family. (A) Western blot analysis of ADAM9, 10 and 17 after comp 27 treatment. (B) Comp 27 dose-dependently increased the levels of precursor and active ADAM9. (C) Comp 27 dose-dependently increased the levels of precursor and active ADAM10. (D) Comp 27 did not change the levels of both precursor and active ADAM17. * p <0.05, ** p <0.01, and *** p <0.001 compared to the control group.

    Journal: Biomolecules & Therapeutics

    Article Title: 3’-O-Acetyl-24-Epi-7,8-Didehydrocimigenol-3-O-β-D-Xylopryranoside Decreases Amyloid Beta Production in Amyloid Precursor Protein-Transfected HeLa Cells

    doi: 10.4062/biomolther.2020.195

    Figure Lengend Snippet: Effect of comp 27 on the Expression of ADAM family. (A) Western blot analysis of ADAM9, 10 and 17 after comp 27 treatment. (B) Comp 27 dose-dependently increased the levels of precursor and active ADAM9. (C) Comp 27 dose-dependently increased the levels of precursor and active ADAM10. (D) Comp 27 did not change the levels of both precursor and active ADAM17. * p <0.05, ** p <0.01, and *** p <0.001 compared to the control group.

    Article Snippet: Rabbit anti-GAPDH, anti-rabbit horseradish peroxidase linked IgG, anti-ADAM9 antibodies and lysis buffer were obtained from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Expressing, Western Blot

    RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.

    Journal: American Journal of Cancer Research

    Article Title: Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy

    doi:

    Figure Lengend Snippet: RSV decreases proliferation of ESCC cells. Cell viability was determined by MTT assay in control (shGFP) or ADAM9 knockdown (shADAM9) CE-146T cells (A), KYSE170 (B), Bm7 (C), and A549 (D) with resveratrol treatment for 72 h. Values are means ± SDs for triplicate at each concentration. The IC50 concentrations of RSV in cancer treatment were shown.

    Article Snippet: Cell lysates (1.5 mg) were mixed with anti-ADAM9 antibody (4 μl, Cell Signaling, Danvers, MA) for each reaction at 4°C overnight in a rotating wheel, and then 50 μL of protein A/G-coated beads was added and rotated 4°C for 1 hour.

    Techniques: MTT Assay, Concentration Assay

    RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.

    Journal: American Journal of Cancer Research

    Article Title: Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy

    doi:

    Figure Lengend Snippet: RSV promotes ADAM9 protein degradation. (A, B) Western blot analysis of the indicated proteins in lung cancer cells (A) and ESCC cells (B) after RSV treatment for 24 hours. EF1α served as the internal control. (C) RT-qPCR analysis of ADAM9 mRNA expression in cancer cells after RSV treatment for 24 hours. Data represent mean ± SD. (D) Western blot analysis of the indicated proteins in cancer cells after RSV (100 μM) and MG132 (5 μM) treatment. The numbers below the blots indicate the relative protein expression.

    Article Snippet: Cell lysates (1.5 mg) were mixed with anti-ADAM9 antibody (4 μl, Cell Signaling, Danvers, MA) for each reaction at 4°C overnight in a rotating wheel, and then 50 μL of protein A/G-coated beads was added and rotated 4°C for 1 hour.

    Techniques: Western Blot, Quantitative RT-PCR, Expressing

    RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.

    Journal: American Journal of Cancer Research

    Article Title: Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy

    doi:

    Figure Lengend Snippet: RSV-induced ADAM9 protein degradation is mediated by the ubiquitin-proteasome pathway. (A, B) HA-Ub was overexpressed in F4 (A) and Bm7 (B) cells treated with RSV (100 μM) and MG132 (5 μM) for 24 hours. Input (left), 10% of the total protein lysate for immunoprecipitation (IP). IP was performed with anti-ADAM9 antibodies, followed by Western blotting with the anti-HA antibody. EF1α, loading control. The numbers below the blots indicate the relative protein expression.

    Article Snippet: Cell lysates (1.5 mg) were mixed with anti-ADAM9 antibody (4 μl, Cell Signaling, Danvers, MA) for each reaction at 4°C overnight in a rotating wheel, and then 50 μL of protein A/G-coated beads was added and rotated 4°C for 1 hour.

    Techniques: Immunoprecipitation, Western Blot, Expressing

    The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.

    Journal: American Journal of Cancer Research

    Article Title: Resveratrol-mediated ADAM9 degradation decreases cancer progression and provides synergistic effects in combination with chemotherapy

    doi:

    Figure Lengend Snippet: The mechanism of RSV-mediated anticancer effects through promoting ADAM9 protein degradation. Combined RSV with clinical chemotherapeutics can provide synergistic anti-cancer effects.

    Article Snippet: Cell lysates (1.5 mg) were mixed with anti-ADAM9 antibody (4 μl, Cell Signaling, Danvers, MA) for each reaction at 4°C overnight in a rotating wheel, and then 50 μL of protein A/G-coated beads was added and rotated 4°C for 1 hour.

    Techniques: