| 別品名 |
HRP, TrueBlot, HRP TrueBlot ULTRA, Peroxidase TrueBlot, TrueBlot for IP/WB, TrueBlot for immunoprecipitation, TrueBlot for western blotting
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| 種由来 |
Mouse
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| 精製度 |
Affinity Purified
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| 適用 |
Western Blot
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| 免疫動物 |
Rat
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| 抗体クラス |
IgG
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| クローン |
eB144
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| 交差種 |
Mouse
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| 形状 |
滅菌済み液状品
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| 構成内容 |
ミニゲルで約20ブロット分の試薬が含まれます。
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| 参考文献 |
[Pub Med ID]33271062, 32751253, 31941780, 31519498, 31263146, 30837642, 24591630, 22492230, 18949366, 33493263, 33523111, 33411764, 33311540, 33240434, 32995755, 32934222, 32348780, 26503466, 22660415, 25659891+他100件以上
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| [注意事項] |
濃度はロットによって異なる可能性があります。メーカーDS及びCoAからご確認ください。
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※サムネイル画像をクリックすると拡大画像が表示されます。
IRE1α expression is regulated by p53. A.) Western blot analysis of the expression of endogenous IRE1α in 23 human cancer cell lines. Cell lines were grouped according to expression of wild type or mutant p53 as indicated. (A well between wt p53 and mutant p53 cell lines was cut, from the gel as indicated by a black line, due to the controversial p53 status of the cell line). Right panel: The intensities of the IRE1α bands (left panel) are expressed relative to those of B actin. Values shown are the mean + standard deviation (s.d.). The P value was calculated using two way ANOVA. B.) Downregulation of p53 expression induces increased expression of IRE1α. HCT116 p53+/+ and U2OS cells were transfected with shLuc, shp53 (753), or shp53 (814), and selected using puromycin. Whole cell lysates of a pool of transfectants were analyzed using western blotting with the indicated antibodies. C.) Overexpression of wild type p53 inhibits IRE1α expression in mutant p53 cell lines. Cell lysates, prepared 48 h after transfection with wild type p53, were analyzed for the expression of indicated proteins. D.) Mutant p53 proteins do not inhibit IRE1α expression. Cell lysates were prepared from cells transfected with p53 G245S, p53 R248W, p53 249S, and p53 R273H expression vectors or from cells that constitutively expressed wild type p53 and were analyzed for the expression of the indicated proteins. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
ER stress response in p53-deficient or knockdown cells. A.) HCT116 p53+/+ or HCT116 p53−/− cells, B. MEF p53+/+ or MEF p53−/− cells, and C. U2OS shLuc or U2OS shp53 cells were incubated with Tm (0.5 μg/mL) or BFA (1 μg/mL) for the times indicated. Cell lysates were analyzed using western blotting with the indicated antibodies. The blot was cut based on the size of proteins or stripped. Total RNAs were extracted and subjected to RT-PCR analysis using specific primer sets for XBP1(U) and XBP1(S). Cell lysates were analyzed using western blotting with indicated antibodies. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
ER stress response in p53-deficient or knockdown cells. A.) HCT116 p53+/+ or HCT116 p53−/− cells, B.) MEF p53+/+ or MEF p53−/− cells, and C.) U2OS shLuc or U2OS shp53 cells were incubated with Tm (0.5 μg/mL) or BFA (1 μg/mL) for the times indicated. Cell lysates were analyzed using western blotting with the indicated antibodies. The blot was cut based on the size of proteins or stripped. Total RNAs were extracted and subjected to RT-PCR analysis using specific primer sets for XBP1(U) and XBP1(S). Cell lysates were analyzed using western blotting with indicated antibodies. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
p53 deficiency increases secretory the function of the ER through the IRE1α/XBP1 pathway. A.) HCT116 p53+/+ or HCT116 p53−/− cells, MEF p53+/+ or MEF p53−/− cells, and U2OS shLuc or U2OS shp53 cells expressing secreted embryonic alkaline phosphatase (SEAP) were transduced with a pSEAP2 control vector and washed 24 h after transduction. The medium was then changed, and the cells were cultured for another 6 h. Culture media were analyzed for SEAP activity, and luminescence was normalized to cell number. The transfection efficiencies of HCT116 p53+/+ and HCT116 p53−/− cells were approximately 80% each (data not shown). B.) Overexpression of wild-type p53 inhibited SEAP activity. SEAP activities of cells that constitutively expressed the indicated p53 molecules were analyzed using the same procedure described in (A). C.) HCT116 p53−/− cells that expressed SEAP were transfected with siControl, siATF6, siPERK, or siIRE1α, cultured for 24 h, and following a change of medium, the cells were cultured for another 6 h. Whole cell lysates were analyzed using western blotting with the indicated antibodies, and culture supernatants were analyzed for SEAP activity. Values shown are the mean ± s.d. of three different experiments simultaneously measured. The P value was calculated using two-way ANOVA. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
ER stress response in p53-deficient or knockdown cells. A.) HCT116 p53+/+ or HCT116 p53−/− cells, B. MEF p53+/+ or MEF p53−/− cells, and C. U2OS shLuc or U2OS shp53 cells were incubated with Tm (0.5 μg/mL) or BFA (1 μg/mL) for the times indicated. Cell lysates were analyzed using western blotting with the indicated antibodies. The blot was cut based on the size of proteins or stripped. Total RNAs were extracted and subjected to RT-PCR analysis using specific primer sets for XBP1(U) and XBP1(S). Cell lysates were analyzed using western blotting with indicated antibodies. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
p53 deficiency increases secretory the function of the ER through the IRE1α/XBP1 pathway. A.) HCT116 p53+/+ or HCT116 p53−/− cells, MEF p53+/+ or MEF p53−/− cells, and U2OS shLuc or U2OS shp53 cells expressing secreted embryonic alkaline phosphatase (SEAP) were transduced with a pSEAP2 control vector and washed 24 h after transduction. The medium was then changed, and the cells were cultured for another 6 h. Culture media were analyzed for SEAP activity, and luminescence was normalized to cell number. The transfection efficiencies of HCT116 p53+/+ and HCT116 p53−/− cells were approximately 80% each (data not shown). B.) Overexpression of wild-type p53 inhibited SEAP activity. SEAP activities of cells that constitutively expressed the indicated p53 molecules were analyzed using the same procedure described in (A). C.) HCT116 p53−/− cells that expressed SEAP were transfected with siControl, siATF6, siPERK, or siIRE1α, cultured for 24 h, and following a change of medium, the cells were cultured for another 6 h. Whole cell lysates were analyzed using western blotting with the indicated antibodies, and culture supernatants were analyzed for SEAP activity. Values shown are the mean ± s.d. of three different experiments simultaneously measured. The P value was calculated using two-way ANOVA. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
Synoviolin promotes IRE1α degradation in a wild-type p53-dependent manner. A.) SYVN1 suppresses IRE1α protein expression in wild-type p53 cells. HCT116 p53+/+ or HCT116 p53−/− cells were transfected with siControl (−) or siSYVN1 (+) and cultured for 24 h. Cell lysates were analyzed using western blotting with indicated the antibodies (left panel). The intensities of the SYVN1 bands were quantified. The levels of SYVN1 are reported relative to those of β-actin (right panel). The blot was cut based on the size of proteins or stripped and reprobed. B.) IRE1α and SYVN1 interaction is suppressed in p53-deficient cells. Proteins were cross-linked with DSP before protein extraction. Coimmunoprecipitation was performed with cell lysate using an IRE1α or an SYVN1 antibody. C.) SYVN1 interacts with wild-type p53. H1299 cells transiently expressed wild-type p53, p53-R248S, or p53-R273H. Coimmunoprecipitation experiments were performed using the anti-p53 antibody. D.) p53-SYVN1-IRE1α complex is observed by treatment with proteasome inhibitor. H1299 cells transiently expressing wild-type p53 (left panel) or HCT116 p53+/+ (right panel) cells were treated with 50 μM MG132 for 3 h. Coimmunoprecipitation experiments were performed using the anti-p53 antibody. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
Synoviolin promotes IRE1α degradation in a wild-type p53-dependent manner. A.) SYVN1 suppresses IRE1α protein expression in wild-type p53 cells. HCT116 p53+/+ or HCT116 p53−/− cells were transfected with siControl (−) or siSYVN1 (+) and cultured for 24 h. Cell lysates were analyzed using western blotting with indicated the antibodies (left panel). The intensities of the SYVN1 bands were quantified. The levels of SYVN1 are reported relative to those of β-actin (right panel). The blot was cut based on the size of proteins or stripped and reprobed. B.) IRE1α and SYVN1 interaction is suppressed in p53-deficient cells. Proteins were cross-linked with DSP before protein extraction. Coimmunoprecipitation was performed with cell lysate using an IRE1α or an SYVN1 antibody. C.) SYVN1 interacts with wild-type p53. H1299 cells transiently expressed wild-type p53, p53-R248S, or p53-R273H. Coimmunoprecipitation experiments were performed using the anti-p53 antibody. D.) p53-SYVN1-IRE1α complex is observed by treatment with proteasome inhibitor. H1299 cells transiently expressing wild-type p53 (left panel) or HCT116 p53+/+ (right panel) cells were treated with 50 μM MG132 for 3 h. Coimmunoprecipitation experiments were performed using the anti-p53 antibody. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
p53 deficiency increases secretory the function of the ER through the IRE1α/XBP1 pathway. A.) HCT116 p53+/+ or HCT116 p53−/− cells, MEF p53+/+ or MEF p53−/− cells, and U2OS shLuc or U2OS shp53 cells expressing secreted embryonic alkaline phosphatase (SEAP) were transduced with a pSEAP2 control vector and washed 24 h after transduction. The medium was then changed, and the cells were cultured for another 6 h. Culture media were analyzed for SEAP activity, and luminescence was normalized to cell number. The transfection efficiencies of HCT116 p53+/+ and HCT116 p53−/− cells were approximately 80% each (data not shown). B.) Overexpression of wild-type p53 inhibited SEAP activity. SEAP activities of cells that constitutively expressed the indicated p53 molecules were analyzed using the same procedure described in (A). C.) HCT116 p53−/− cells that expressed SEAP were transfected with siControl, siATF6, siPERK, or siIRE1α, cultured for 24 h, and following a change of medium, the cells were cultured for another 6 h. Whole cell lysates were analyzed using western blotting with the indicated antibodies, and culture supernatants were analyzed for SEAP activity. Values shown are the mean ± s.d. of three different experiments simultaneously measured. The P value was calculated using two-way ANOVA. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
Synoviolin promotes IRE1α degradation in a wild-type p53-dependent manner. A.) SYVN1 suppresses IRE1α protein expression in wild-type p53 cells. HCT116 p53+/+ or HCT116 p53−/− cells were transfected with siControl (−) or siSYVN1 (+) and cultured for 24 h. Cell lysates were analyzed using western blotting with indicated the antibodies (left panel). The intensities of the SYVN1 bands were quantified. The levels of SYVN1 are reported relative to those of β-actin (right panel). The blot was cut based on the size of proteins or stripped and reprobed. B.) IRE1α and SYVN1 interaction is suppressed in p53-deficient cells. Proteins were cross-linked with DSP before protein extraction. Coimmunoprecipitation was performed with cell lysate using an IRE1α or an SYVN1 antibody. C.) SYVN1 interacts with wild-type p53. H1299 cells transiently expressed wild-type p53, p53-R248S, or p53-R273H. Coimmunoprecipitation experiments were performed using the anti-p53 antibody. D.) p53-SYVN1-IRE1α complex is observed by treatment with proteasome inhibitor. H1299 cells transiently expressing wild-type p53 (left panel) or HCT116 p53+/+ (right panel) cells were treated with 50 μM MG132 for 3 h. Coimmunoprecipitation experiments were performed using the anti-p53 antibody. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
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IRE1α expression is regulated by p53. A.) Western blot analysis of the expression of endogenous IRE1α in 23 human cancer cell lines. Cell lines were grouped according to expression of wild type or mutant p53 as indicated. (A well between wt p53 and mutant p53 cell lines was cut, from the gel as indicated by a black line, due to the controversial p53 status of the cell line). Right panel: The intensities of the IRE1α bands (left panel) are expressed relative to those of B actin. Values shown are the mean + standard deviation (s.d.). The P value was calculated using two way ANOVA. B.) Downregulation of p53 expression induces increased expression of IRE1α. HCT116 p53+/+ and U2OS cells were transfected with shLuc, shp53 (753), or shp53 (814), and selected using puromycin. Whole cell lysates of a pool of transfectants were analyzed using western blotting with the indicated antibodies. C.) Overexpression of wild type p53 inhibits IRE1α expression in mutant p53 cell lines. Cell lysates, prepared 48 h after transfection with wild type p53, were analyzed for the expression of indicated proteins. D.) Mutant p53 proteins do not inhibit IRE1α expression. Cell lysates were prepared from cells transfected with p53 G245S, p53 R248W, p53 249S, and p53 R273H expression vectors or from cells that constitutively expressed wild type p53 and were analyzed for the expression of the indicated proteins. Figure provided by CiteAb. Source: Oncotarget, PMID: 26254280.
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| メーカー |
品番 |
包装 |
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RKL
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18-8817-31
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50 UL
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※表示価格について
| 当社在庫 |
なし
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| 入荷予定 |
あり
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| 納期目安 |
発注済・入荷予定
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| 保存温度 |
-２０℃
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