anti tnfr1  (ProSci Incorporated)


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    ProSci Incorporated anti tnfr1
    RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or <t>anti-TNFR1</t> antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : <t>TNFR1</t> complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments
    Anti Tnfr1, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti tnfr1/product/ProSci Incorporated
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti tnfr1 - by Bioz Stars, 2023-03
    86/100 stars

    Images

    1) Product Images from "The cytoplasmic nuclear receptor RARγ controls RIP1 initiated cell death when cIAP activity is inhibited"

    Article Title: The cytoplasmic nuclear receptor RARγ controls RIP1 initiated cell death when cIAP activity is inhibited

    Journal: Nature Communications

    doi: 10.1038/s41467-017-00496-6

    RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or anti-TNFR1 antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : TNFR1 complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments
    Figure Legend Snippet: RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or anti-TNFR1 antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : TNFR1 complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments

    Techniques Used: Western Blot, shRNA, Immunoprecipitation, Marker

    RARγ initiates the formation of death complexes by dissociating RIP1 from TNFR1. a Immunoprecipitation of HT-29 cont-shRNA, TRADD-shRNA or RIP1-shRNA treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-TNFR1 antibody and immunoblotted with the indicated antibodies. b Sequential immunoprecipitation of HEK293T cells co-transfected with FLAG-TNFR1, DsRed-RIP1 and increasing amounts of V5-RARγ-NLSmut plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-FLAG (TNFR1) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-V5 (RARγ) antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. c Sequential immunoprecipitation of HEK293T cells co-transfected with V5-RARγ-NLSmut, RIP1-Myc, and increasing amounts of DsRed-RIP3 plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-V5 (RARγ) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-DsRed (RIP3) antibody. The immunoprecipitated complexes were analyzed with the indicated antibodies. d WT and RIP3−/− MEFs treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-Caspase-8 antibody and immunoblotted with the indicated antibodies. All blots above are representative of one of three experiments
    Figure Legend Snippet: RARγ initiates the formation of death complexes by dissociating RIP1 from TNFR1. a Immunoprecipitation of HT-29 cont-shRNA, TRADD-shRNA or RIP1-shRNA treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-TNFR1 antibody and immunoblotted with the indicated antibodies. b Sequential immunoprecipitation of HEK293T cells co-transfected with FLAG-TNFR1, DsRed-RIP1 and increasing amounts of V5-RARγ-NLSmut plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-FLAG (TNFR1) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-V5 (RARγ) antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. c Sequential immunoprecipitation of HEK293T cells co-transfected with V5-RARγ-NLSmut, RIP1-Myc, and increasing amounts of DsRed-RIP3 plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-V5 (RARγ) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-DsRed (RIP3) antibody. The immunoprecipitated complexes were analyzed with the indicated antibodies. d WT and RIP3−/− MEFs treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-Caspase-8 antibody and immunoblotted with the indicated antibodies. All blots above are representative of one of three experiments

    Techniques Used: Immunoprecipitation, shRNA, Transfection

    RARγ modulates TNF-induced RIP-initiated cell death. a TRADD is responsible for initiated TC or TCZ-induced cell death. b RARγ is essential for the transition from inflammatory signaling to death pathways in TNF-induced RIP1-initiated cell death. When RARγ is released from the nucleus in response to TNF under the conditions of cIAP inhibition, it initiates the formation of death complex IIa by dissociating RIP1 from TNFR1. When RIP1 recruits RIP3 to necrosome/complex IIb, RARγ is replaced from the complex
    Figure Legend Snippet: RARγ modulates TNF-induced RIP-initiated cell death. a TRADD is responsible for initiated TC or TCZ-induced cell death. b RARγ is essential for the transition from inflammatory signaling to death pathways in TNF-induced RIP1-initiated cell death. When RARγ is released from the nucleus in response to TNF under the conditions of cIAP inhibition, it initiates the formation of death complex IIa by dissociating RIP1 from TNFR1. When RIP1 recruits RIP3 to necrosome/complex IIb, RARγ is replaced from the complex

    Techniques Used: Inhibition

    anti tnfr1  (ProSci Incorporated)


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    ProSci Incorporated anti tnfr1
    RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or <t>anti-TNFR1</t> antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : <t>TNFR1</t> complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments
    Anti Tnfr1, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti tnfr1/product/ProSci Incorporated
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti tnfr1 - by Bioz Stars, 2023-03
    86/100 stars

    Images

    1) Product Images from "The cytoplasmic nuclear receptor RARγ controls RIP1 initiated cell death when cIAP activity is inhibited"

    Article Title: The cytoplasmic nuclear receptor RARγ controls RIP1 initiated cell death when cIAP activity is inhibited

    Journal: Nature Communications

    doi: 10.1038/s41467-017-00496-6

    RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or anti-TNFR1 antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : TNFR1 complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments
    Figure Legend Snippet: RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or anti-TNFR1 antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : TNFR1 complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments

    Techniques Used: Western Blot, shRNA, Immunoprecipitation, Marker

    RARγ initiates the formation of death complexes by dissociating RIP1 from TNFR1. a Immunoprecipitation of HT-29 cont-shRNA, TRADD-shRNA or RIP1-shRNA treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-TNFR1 antibody and immunoblotted with the indicated antibodies. b Sequential immunoprecipitation of HEK293T cells co-transfected with FLAG-TNFR1, DsRed-RIP1 and increasing amounts of V5-RARγ-NLSmut plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-FLAG (TNFR1) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-V5 (RARγ) antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. c Sequential immunoprecipitation of HEK293T cells co-transfected with V5-RARγ-NLSmut, RIP1-Myc, and increasing amounts of DsRed-RIP3 plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-V5 (RARγ) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-DsRed (RIP3) antibody. The immunoprecipitated complexes were analyzed with the indicated antibodies. d WT and RIP3−/− MEFs treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-Caspase-8 antibody and immunoblotted with the indicated antibodies. All blots above are representative of one of three experiments
    Figure Legend Snippet: RARγ initiates the formation of death complexes by dissociating RIP1 from TNFR1. a Immunoprecipitation of HT-29 cont-shRNA, TRADD-shRNA or RIP1-shRNA treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-TNFR1 antibody and immunoblotted with the indicated antibodies. b Sequential immunoprecipitation of HEK293T cells co-transfected with FLAG-TNFR1, DsRed-RIP1 and increasing amounts of V5-RARγ-NLSmut plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-FLAG (TNFR1) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-V5 (RARγ) antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. c Sequential immunoprecipitation of HEK293T cells co-transfected with V5-RARγ-NLSmut, RIP1-Myc, and increasing amounts of DsRed-RIP3 plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-V5 (RARγ) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-DsRed (RIP3) antibody. The immunoprecipitated complexes were analyzed with the indicated antibodies. d WT and RIP3−/− MEFs treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-Caspase-8 antibody and immunoblotted with the indicated antibodies. All blots above are representative of one of three experiments

    Techniques Used: Immunoprecipitation, shRNA, Transfection

    RARγ modulates TNF-induced RIP-initiated cell death. a TRADD is responsible for initiated TC or TCZ-induced cell death. b RARγ is essential for the transition from inflammatory signaling to death pathways in TNF-induced RIP1-initiated cell death. When RARγ is released from the nucleus in response to TNF under the conditions of cIAP inhibition, it initiates the formation of death complex IIa by dissociating RIP1 from TNFR1. When RIP1 recruits RIP3 to necrosome/complex IIb, RARγ is replaced from the complex
    Figure Legend Snippet: RARγ modulates TNF-induced RIP-initiated cell death. a TRADD is responsible for initiated TC or TCZ-induced cell death. b RARγ is essential for the transition from inflammatory signaling to death pathways in TNF-induced RIP1-initiated cell death. When RARγ is released from the nucleus in response to TNF under the conditions of cIAP inhibition, it initiates the formation of death complex IIa by dissociating RIP1 from TNFR1. When RIP1 recruits RIP3 to necrosome/complex IIb, RARγ is replaced from the complex

    Techniques Used: Inhibition

    anti tnfr1 in rabbit  (ProSci Incorporated)


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    ProSci Incorporated anti tnfr1 in rabbit
    Rats were implanted in the striatum with CNS-1 tumors and 9 days later brains were processed for immunocytochemistry. Confocal microphotographs show detection of therapeutic targets (green) using specific antibodies against the death receptors <t>TNFR1,</t> TRAILR2, Fas, while proliferating cells, the target for TK+GCV, were stained with an anti-Ki67 antibody. Tumor cells were labeled with anti-vimentin antibodies (red), neurons were stained with anti-NeuN (red) and astrocytes with anti-GFAP antibodies (red). Nuclei were stained with DAPI (blue). T: tumor area. N: necrotic patch. Arrows indicate cells expressing the therapeutic target indicated. Dashed line represents tumor border. Scale bars: 10 μm.
    Anti Tnfr1 In Rabbit, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti tnfr1 in rabbit/product/ProSci Incorporated
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti tnfr1 in rabbit - by Bioz Stars, 2023-03
    86/100 stars

    Images

    1) Product Images from "Release of HMGB1 in response to pro-apoptotic glioma killing strategies: efficacy and neurotoxicity"

    Article Title: Release of HMGB1 in response to pro-apoptotic glioma killing strategies: efficacy and neurotoxicity

    Journal:

    doi: 10.1158/1078-0432.CCR-09-0155

    Rats were implanted in the striatum with CNS-1 tumors and 9 days later brains were processed for immunocytochemistry. Confocal microphotographs show detection of therapeutic targets (green) using specific antibodies against the death receptors TNFR1, TRAILR2, Fas, while proliferating cells, the target for TK+GCV, were stained with an anti-Ki67 antibody. Tumor cells were labeled with anti-vimentin antibodies (red), neurons were stained with anti-NeuN (red) and astrocytes with anti-GFAP antibodies (red). Nuclei were stained with DAPI (blue). T: tumor area. N: necrotic patch. Arrows indicate cells expressing the therapeutic target indicated. Dashed line represents tumor border. Scale bars: 10 μm.
    Figure Legend Snippet: Rats were implanted in the striatum with CNS-1 tumors and 9 days later brains were processed for immunocytochemistry. Confocal microphotographs show detection of therapeutic targets (green) using specific antibodies against the death receptors TNFR1, TRAILR2, Fas, while proliferating cells, the target for TK+GCV, were stained with an anti-Ki67 antibody. Tumor cells were labeled with anti-vimentin antibodies (red), neurons were stained with anti-NeuN (red) and astrocytes with anti-GFAP antibodies (red). Nuclei were stained with DAPI (blue). T: tumor area. N: necrotic patch. Arrows indicate cells expressing the therapeutic target indicated. Dashed line represents tumor border. Scale bars: 10 μm.

    Techniques Used: Immunocytochemistry, Staining, Labeling, Expressing