immunoprecipitation Search Results


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  • 93
    Millipore protein immune precipitation kit
    AhSLF-S 2 Interacts with ASK1- and CUL1-Like Proteins. (A) Extracts of styles of S 1 S 4 or S 2 S 5 lines (50 μg each) and pollen of an S 2 S 5 line (50 μg) were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL) (lanes 1 and 3) or control preimmune serum (3 μL) (lanes 2 and 4), respectively. As additional controls, the extracts of styles of S 1 S 4 (lane 5) and S 2 S 5 (lane 6) lines or pollen of S 1 S 4 (lane 7) and S 2 S 5 (lane 8) lines also were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL). After <t>immunoprecipitation,</t> the proteins were subjected to 12% SDS-PAGE followed by protein gel blotting with specific antibodies against AtASK1 of Arabidopsis (top panel). Total proteins of Antirrhinum pollen (lane 9) and Arabidopsis leaf (lane 10) also were used as positive controls. The bottom panel represents the Coomassie blue–stained gel before protein gel blotting for equal loading of proteins. (B) Immunoblot detection of CUL1-like protein from total pollen proteins of Antirrhinum pollen (lane 1) and Arabidopsis (lane 2). (C) A pull-down assay for an interaction between AhSLF-S 2 and CUL1-like proteins. His-NAT resin or the purified fusion proteins of His-AhSLF-S 2 -C were incubated with the extracts of Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 (lanes 5 and 10), respectively. The extracts of the Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 were incubated without His-AhSLF-S 2 -C as negative controls (lanes 4 and 9), and style and pollen extracts were used as positive controls (lanes 1 and 6). As additional controls, the extracts of the styles of S 2 S 5 (lane 2) and S 1 S 4 (lane 7) lines or pollen of S 2 S 5 (lane 3) and S 1 S 4 (lane 8) lines were incubated with anti-AhSLF-S 2 -C antibody (3 μL). Proteins bound were pulled down with His-NAT resin, eluted with lysis buffer, separated by 12% SDS-PAGE, transferred to membranes, and analyzed by immunoblotting with Arabidopsis anti-CUL1 antibody.
    Protein Immune Precipitation Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Keygen Biotech immune precipitation assay buffer
    AhSLF-S 2 Interacts with ASK1- and CUL1-Like Proteins. (A) Extracts of styles of S 1 S 4 or S 2 S 5 lines (50 μg each) and pollen of an S 2 S 5 line (50 μg) were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL) (lanes 1 and 3) or control preimmune serum (3 μL) (lanes 2 and 4), respectively. As additional controls, the extracts of styles of S 1 S 4 (lane 5) and S 2 S 5 (lane 6) lines or pollen of S 1 S 4 (lane 7) and S 2 S 5 (lane 8) lines also were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL). After <t>immunoprecipitation,</t> the proteins were subjected to 12% SDS-PAGE followed by protein gel blotting with specific antibodies against AtASK1 of Arabidopsis (top panel). Total proteins of Antirrhinum pollen (lane 9) and Arabidopsis leaf (lane 10) also were used as positive controls. The bottom panel represents the Coomassie blue–stained gel before protein gel blotting for equal loading of proteins. (B) Immunoblot detection of CUL1-like protein from total pollen proteins of Antirrhinum pollen (lane 1) and Arabidopsis (lane 2). (C) A pull-down assay for an interaction between AhSLF-S 2 and CUL1-like proteins. His-NAT resin or the purified fusion proteins of His-AhSLF-S 2 -C were incubated with the extracts of Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 (lanes 5 and 10), respectively. The extracts of the Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 were incubated without His-AhSLF-S 2 -C as negative controls (lanes 4 and 9), and style and pollen extracts were used as positive controls (lanes 1 and 6). As additional controls, the extracts of the styles of S 2 S 5 (lane 2) and S 1 S 4 (lane 7) lines or pollen of S 2 S 5 (lane 3) and S 1 S 4 (lane 8) lines were incubated with anti-AhSLF-S 2 -C antibody (3 μL). Proteins bound were pulled down with His-NAT resin, eluted with lysis buffer, separated by 12% SDS-PAGE, transferred to membranes, and analyzed by immunoblotting with Arabidopsis anti-CUL1 antibody.
    Immune Precipitation Assay Buffer, supplied by Keygen Biotech, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Beyotime radio immune precipitation buffer
    AhSLF-S 2 Interacts with ASK1- and CUL1-Like Proteins. (A) Extracts of styles of S 1 S 4 or S 2 S 5 lines (50 μg each) and pollen of an S 2 S 5 line (50 μg) were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL) (lanes 1 and 3) or control preimmune serum (3 μL) (lanes 2 and 4), respectively. As additional controls, the extracts of styles of S 1 S 4 (lane 5) and S 2 S 5 (lane 6) lines or pollen of S 1 S 4 (lane 7) and S 2 S 5 (lane 8) lines also were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL). After <t>immunoprecipitation,</t> the proteins were subjected to 12% SDS-PAGE followed by protein gel blotting with specific antibodies against AtASK1 of Arabidopsis (top panel). Total proteins of Antirrhinum pollen (lane 9) and Arabidopsis leaf (lane 10) also were used as positive controls. The bottom panel represents the Coomassie blue–stained gel before protein gel blotting for equal loading of proteins. (B) Immunoblot detection of CUL1-like protein from total pollen proteins of Antirrhinum pollen (lane 1) and Arabidopsis (lane 2). (C) A pull-down assay for an interaction between AhSLF-S 2 and CUL1-like proteins. His-NAT resin or the purified fusion proteins of His-AhSLF-S 2 -C were incubated with the extracts of Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 (lanes 5 and 10), respectively. The extracts of the Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 were incubated without His-AhSLF-S 2 -C as negative controls (lanes 4 and 9), and style and pollen extracts were used as positive controls (lanes 1 and 6). As additional controls, the extracts of the styles of S 2 S 5 (lane 2) and S 1 S 4 (lane 7) lines or pollen of S 2 S 5 (lane 3) and S 1 S 4 (lane 8) lines were incubated with anti-AhSLF-S 2 -C antibody (3 μL). Proteins bound were pulled down with His-NAT resin, eluted with lysis buffer, separated by 12% SDS-PAGE, transferred to membranes, and analyzed by immunoblotting with Arabidopsis anti-CUL1 antibody.
    Radio Immune Precipitation Buffer, supplied by Beyotime, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore anti flt1 immune precipitation
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Anti Flt1 Immune Precipitation, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher radio immune precipitation ripa buffer
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Radio Immune Precipitation Ripa Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Beyotime radio immunoprecipitation assay ripa buffer
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Radio Immunoprecipitation Assay Ripa Buffer, supplied by Beyotime, used in various techniques. Bioz Stars score: 93/100, based on 541 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega radio immune precipitation assay ripa buffer
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Radio Immune Precipitation Assay Ripa Buffer, supplied by Promega, used in various techniques. Bioz Stars score: 91/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc radio immunoprecipitation assay ripa buffer
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Radio Immunoprecipitation Assay Ripa Buffer, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 142 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Beyotime radio immune precipitation lysis buffer
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Radio Immune Precipitation Lysis Buffer, supplied by Beyotime, used in various techniques. Bioz Stars score: 91/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology radio immunoprecipitation assay ripa buffer
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Radio Immunoprecipitation Assay Ripa Buffer, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 86 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Upstate Biotechnology Inc acetyl histone h3 immune precipitation assay kit
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Acetyl Histone H3 Immune Precipitation Assay Kit, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc radio immune precipitation assay
    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor <t>1/FLT1</t> . (A) HUVECs transfected with the indicated siRNAs were serum starved
    Radio Immune Precipitation Assay, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore co immunoprecipitation
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Co Immunoprecipitation, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 2208 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher crosslink immune precipitation kit protocol
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Crosslink Immune Precipitation Kit Protocol, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Nissen chromatin immune precipitation technique
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Chromatin Immune Precipitation Technique, supplied by Nissen, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore radio immunoprecipitation assay buffer ripa
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Radio Immunoprecipitation Assay Buffer Ripa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 97 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Beyotime radio immune precipitation ripa lysis buffer
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Radio Immune Precipitation Ripa Lysis Buffer, supplied by Beyotime, used in various techniques. Bioz Stars score: 92/100, based on 158 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore chromatin immune precipitation kit
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Chromatin Immune Precipitation Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher dna immune precipitation ip
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Dna Immune Precipitation Ip, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Cell Signaling Technology Inc radio immunoprecipitation assay buffer
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Radio Immunoprecipitation Assay Buffer, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 163 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Beyotime radio immunoprecipitation assay ripa
    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an <t>immunoprecipitation</t> input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.
    Radio Immunoprecipitation Assay Ripa, supplied by Beyotime, used in various techniques. Bioz Stars score: 94/100, based on 113 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Roche radio immunoprecipitation assay buffer
    <t>Immunoprecipitation</t> with anti-P2X 1 antibody. Antibodies to P2X 1 were immobilized onto resin beads and then incubated with mouse bladder lysates to IP the antigen and co-IP interacting proteins. Proteins that were bound (IP: 2.5 µg protein/lane) or did not bind (FT: 25 µg protein/lane) to the beads were resolved by SDS-PAGE, and Western blots were probed with A) P2X 1, B) P2X 4 or C) Nt5e antibodies. ( A ) Left and right panels show P2X 1 immunoblots on IP and FT lysates from wild type and P2X 4 −/− mice. Monomeric P2X 1 can be seen highly concentrated in the pulldown fraction at 50 kDa. Little P2X 1 appears in FT. ( B ) P2X 4 antibody detects P2X 4 as a band at 70 kDa in wild type, but is completely absent in P2X 4 −/− mice. The antibody shows minor cross-reactivity to possibly P2X 1 . Note, there is no evidence of the 70 kDa band in the IP lane. ( C ) An antibody to 5′-nucleotidase (Nt5e) demonstrates that pulldown with anti-P2X 1 is ‘clean’ with no non-specific protein binding evident in the IP lanes.
    Radio Immunoprecipitation Assay Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 94/100, based on 422 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/radio immunoprecipitation assay buffer/product/Roche
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    Image Search Results


    AhSLF-S 2 Interacts with ASK1- and CUL1-Like Proteins. (A) Extracts of styles of S 1 S 4 or S 2 S 5 lines (50 μg each) and pollen of an S 2 S 5 line (50 μg) were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL) (lanes 1 and 3) or control preimmune serum (3 μL) (lanes 2 and 4), respectively. As additional controls, the extracts of styles of S 1 S 4 (lane 5) and S 2 S 5 (lane 6) lines or pollen of S 1 S 4 (lane 7) and S 2 S 5 (lane 8) lines also were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL). After immunoprecipitation, the proteins were subjected to 12% SDS-PAGE followed by protein gel blotting with specific antibodies against AtASK1 of Arabidopsis (top panel). Total proteins of Antirrhinum pollen (lane 9) and Arabidopsis leaf (lane 10) also were used as positive controls. The bottom panel represents the Coomassie blue–stained gel before protein gel blotting for equal loading of proteins. (B) Immunoblot detection of CUL1-like protein from total pollen proteins of Antirrhinum pollen (lane 1) and Arabidopsis (lane 2). (C) A pull-down assay for an interaction between AhSLF-S 2 and CUL1-like proteins. His-NAT resin or the purified fusion proteins of His-AhSLF-S 2 -C were incubated with the extracts of Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 (lanes 5 and 10), respectively. The extracts of the Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 were incubated without His-AhSLF-S 2 -C as negative controls (lanes 4 and 9), and style and pollen extracts were used as positive controls (lanes 1 and 6). As additional controls, the extracts of the styles of S 2 S 5 (lane 2) and S 1 S 4 (lane 7) lines or pollen of S 2 S 5 (lane 3) and S 1 S 4 (lane 8) lines were incubated with anti-AhSLF-S 2 -C antibody (3 μL). Proteins bound were pulled down with His-NAT resin, eluted with lysis buffer, separated by 12% SDS-PAGE, transferred to membranes, and analyzed by immunoblotting with Arabidopsis anti-CUL1 antibody.

    Journal: The Plant Cell

    Article Title: The F-Box Protein AhSLF-S2 Physically Interacts with S-RNases That May Be Inhibited by the Ubiquitin/26S Proteasome Pathway of Protein Degradation during Compatible Pollination in Antirrhinum

    doi: 10.1105/tpc.017673

    Figure Lengend Snippet: AhSLF-S 2 Interacts with ASK1- and CUL1-Like Proteins. (A) Extracts of styles of S 1 S 4 or S 2 S 5 lines (50 μg each) and pollen of an S 2 S 5 line (50 μg) were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL) (lanes 1 and 3) or control preimmune serum (3 μL) (lanes 2 and 4), respectively. As additional controls, the extracts of styles of S 1 S 4 (lane 5) and S 2 S 5 (lane 6) lines or pollen of S 1 S 4 (lane 7) and S 2 S 5 (lane 8) lines also were coimmunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL). After immunoprecipitation, the proteins were subjected to 12% SDS-PAGE followed by protein gel blotting with specific antibodies against AtASK1 of Arabidopsis (top panel). Total proteins of Antirrhinum pollen (lane 9) and Arabidopsis leaf (lane 10) also were used as positive controls. The bottom panel represents the Coomassie blue–stained gel before protein gel blotting for equal loading of proteins. (B) Immunoblot detection of CUL1-like protein from total pollen proteins of Antirrhinum pollen (lane 1) and Arabidopsis (lane 2). (C) A pull-down assay for an interaction between AhSLF-S 2 and CUL1-like proteins. His-NAT resin or the purified fusion proteins of His-AhSLF-S 2 -C were incubated with the extracts of Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 (lanes 5 and 10), respectively. The extracts of the Antirrhinum styles from S 2 S 5 and pollen of S 2 S 5 or S 1 S 4 were incubated without His-AhSLF-S 2 -C as negative controls (lanes 4 and 9), and style and pollen extracts were used as positive controls (lanes 1 and 6). As additional controls, the extracts of the styles of S 2 S 5 (lane 2) and S 1 S 4 (lane 7) lines or pollen of S 2 S 5 (lane 3) and S 1 S 4 (lane 8) lines were incubated with anti-AhSLF-S 2 -C antibody (3 μL). Proteins bound were pulled down with His-NAT resin, eluted with lysis buffer, separated by 12% SDS-PAGE, transferred to membranes, and analyzed by immunoblotting with Arabidopsis anti-CUL1 antibody.

    Article Snippet: Immunoprecipitation was performed following the manufacturer's recommendation of an immunoprecipitation kit (IP-50; Sigma-Aldrich).

    Techniques: Immunoprecipitation, SDS Page, Staining, Pull Down Assay, Purification, Incubation, Lysis

    Coimmunoprecipitation of AhSLF-S 2 and S-RNases. (A) Detection of AhSLF-S 2 in several tissues and E. coli expressing AhSLF-S 2 C by a polyclonal antibody against the C-terminal region of AhSLF-S 2 . Bottom panel: Coomassie blue–stained gel before protein gel blot analysis showing control loading of proteins. Lanes 1 to 4 represent protein extracts from sepal (Sp), petal (Pe), style (St), and anther (An) from an S 2 S 5 line. AhSLF-S 2 C indicates the detection of AhSLF-S 2 C in E. coli expressing AhSLF-S 2 C . (B) Immunoblot analysis of style proteins from several lines of an S -allele–segregating family using allele-specific antibodies against peptides derived from S 2 - and S 4 -RNases. Genotypes are indicated at the top. (C) Extracts of pollinated styles of S 1 S 4 (lane 1) or S 2 S 5 (lane 3) lines (50 μg) and pollen of an S 2 S 5 line (50 μg) were immunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL) (lanes 1 and 3) or control preimmune serum (3 μL) (lanes 2 and 4), respectively. After immunoprecipitation, the proteins were subjected to 12% SDS-PAGE followed by protein gel blotting with specific antibodies against S 2 - and S 4 -RNases, respectively (top panels). S-RNases detected are indicated. Bottom panels: Coomassie blue–stained gels before protein gel blot analysis showing equal loading of proteins. The strongest bands represent immunoglobulin heavy chains. Molecular mass markers are indicated in kilodaltons.

    Journal: The Plant Cell

    Article Title: The F-Box Protein AhSLF-S2 Physically Interacts with S-RNases That May Be Inhibited by the Ubiquitin/26S Proteasome Pathway of Protein Degradation during Compatible Pollination in Antirrhinum

    doi: 10.1105/tpc.017673

    Figure Lengend Snippet: Coimmunoprecipitation of AhSLF-S 2 and S-RNases. (A) Detection of AhSLF-S 2 in several tissues and E. coli expressing AhSLF-S 2 C by a polyclonal antibody against the C-terminal region of AhSLF-S 2 . Bottom panel: Coomassie blue–stained gel before protein gel blot analysis showing control loading of proteins. Lanes 1 to 4 represent protein extracts from sepal (Sp), petal (Pe), style (St), and anther (An) from an S 2 S 5 line. AhSLF-S 2 C indicates the detection of AhSLF-S 2 C in E. coli expressing AhSLF-S 2 C . (B) Immunoblot analysis of style proteins from several lines of an S -allele–segregating family using allele-specific antibodies against peptides derived from S 2 - and S 4 -RNases. Genotypes are indicated at the top. (C) Extracts of pollinated styles of S 1 S 4 (lane 1) or S 2 S 5 (lane 3) lines (50 μg) and pollen of an S 2 S 5 line (50 μg) were immunoprecipitated with anti-AhSLF-S 2 -C antibody (3 μL) (lanes 1 and 3) or control preimmune serum (3 μL) (lanes 2 and 4), respectively. After immunoprecipitation, the proteins were subjected to 12% SDS-PAGE followed by protein gel blotting with specific antibodies against S 2 - and S 4 -RNases, respectively (top panels). S-RNases detected are indicated. Bottom panels: Coomassie blue–stained gels before protein gel blot analysis showing equal loading of proteins. The strongest bands represent immunoglobulin heavy chains. Molecular mass markers are indicated in kilodaltons.

    Article Snippet: Immunoprecipitation was performed following the manufacturer's recommendation of an immunoprecipitation kit (IP-50; Sigma-Aldrich).

    Techniques: Expressing, Staining, Western Blot, Derivative Assay, Immunoprecipitation, SDS Page

    Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor 1/FLT1 . (A) HUVECs transfected with the indicated siRNAs were serum starved

    Journal: Blood

    Article Title: Endothelial cell-specific chemotaxis receptor (ecscr) promotes angioblast migration during vasculogenesis and enhances VEGF receptor sensitivity

    doi: 10.1182/blood-2009-10-248856

    Figure Lengend Snippet: Knockdown of ECSCR in HUVECs results in reduced VEGF-induced phosphorylation of VEGF receptor 2/KDR and downstream PLCβ3, but not tyrosine phosphorylation of VEGF receptor 1/FLT1 . (A) HUVECs transfected with the indicated siRNAs were serum starved

    Article Snippet: KDR and phosphoantigens were assayed by Western blot of total lysates; phospho-FLT1 was assayed by anti-FLT1 immune precipitation followed by phosphotyrosine immunoblot (4G10; Millipore/Upstate).

    Techniques: Transfection

    Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an immunoprecipitation input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.

    Journal: Psychopharmacology

    Article Title: RGS4 over-expression in the rat dorsal striatum modulates mGluR5- and amphetamine-mediated behavior and signaling

    doi: 10.1007/s00213-011-2606-8

    Figure Lengend Snippet: Infusion of HSV-RGS4 into the dSTR results in over-expression of RGS4 protein as well as binding of recombinant RGS4 to mGluR5 receptors Animals received bilateral intra-dSTR infusion of HSV-RGS4- FLAG or a control vector HSV-LacZ (2μl/side) and brains were analyzed 3 days later. A , Upper panel: Outline of the rat brain coronal section depicting a representative placement of HSV infusions; adapted from Paxinos and Watson (2005). Lower panels: Immunohistochemical detection of RGS4 and β-galactosidase over-expression in the dSTR near the infusion site (black box represents a tip of the injector). Representative image of Nissl-stained striatal section showing no necrosis or abnormal cytoarchitecture in the proximity of the infusion site. B , Protein levels of β-galactosidase, RGS4, RGS4- FLAG and calnexin as measured by immunoblotting in tissue lysates prepared from the dSTR. C , FLAG -tagged RGS4 co-immunoprecipitates with mGluR5, but not with, dopamine D1 or D2 receptors in the dSTR ( D ). Immunoprecipitates (IP) were analyzed by immunoblotting (IB) using antibodies against FLAG -tag, mGluR5 or D1 and D2 receptors. T - total lysate used as an immunoprecipitation input. co-IP analysis included negative controls in which lysate, FLAG IP beads or RGS4- FLAG over-expression was omitted.

    Article Snippet: Co-immunoprecipitation experiments included a positive control (immunoprecipitation of FLAG -BAP fusion protein; Sigma-Aldrich) as well as negative controls (omission of lysate, FLAG M2 beads or no over-expression of FLAG -tagged RGS4).

    Techniques: Over Expression, Binding Assay, Recombinant, Plasmid Preparation, Immunohistochemistry, Staining, FLAG-tag, Immunoprecipitation, Co-Immunoprecipitation Assay

    Immunoprecipitation with anti-P2X 1 antibody. Antibodies to P2X 1 were immobilized onto resin beads and then incubated with mouse bladder lysates to IP the antigen and co-IP interacting proteins. Proteins that were bound (IP: 2.5 µg protein/lane) or did not bind (FT: 25 µg protein/lane) to the beads were resolved by SDS-PAGE, and Western blots were probed with A) P2X 1, B) P2X 4 or C) Nt5e antibodies. ( A ) Left and right panels show P2X 1 immunoblots on IP and FT lysates from wild type and P2X 4 −/− mice. Monomeric P2X 1 can be seen highly concentrated in the pulldown fraction at 50 kDa. Little P2X 1 appears in FT. ( B ) P2X 4 antibody detects P2X 4 as a band at 70 kDa in wild type, but is completely absent in P2X 4 −/− mice. The antibody shows minor cross-reactivity to possibly P2X 1 . Note, there is no evidence of the 70 kDa band in the IP lane. ( C ) An antibody to 5′-nucleotidase (Nt5e) demonstrates that pulldown with anti-P2X 1 is ‘clean’ with no non-specific protein binding evident in the IP lanes.

    Journal: Scientific Reports

    Article Title: Role of P2X4 Receptor in Mouse Voiding Function

    doi: 10.1038/s41598-018-20216-4

    Figure Lengend Snippet: Immunoprecipitation with anti-P2X 1 antibody. Antibodies to P2X 1 were immobilized onto resin beads and then incubated with mouse bladder lysates to IP the antigen and co-IP interacting proteins. Proteins that were bound (IP: 2.5 µg protein/lane) or did not bind (FT: 25 µg protein/lane) to the beads were resolved by SDS-PAGE, and Western blots were probed with A) P2X 1, B) P2X 4 or C) Nt5e antibodies. ( A ) Left and right panels show P2X 1 immunoblots on IP and FT lysates from wild type and P2X 4 −/− mice. Monomeric P2X 1 can be seen highly concentrated in the pulldown fraction at 50 kDa. Little P2X 1 appears in FT. ( B ) P2X 4 antibody detects P2X 4 as a band at 70 kDa in wild type, but is completely absent in P2X 4 −/− mice. The antibody shows minor cross-reactivity to possibly P2X 1 . Note, there is no evidence of the 70 kDa band in the IP lane. ( C ) An antibody to 5′-nucleotidase (Nt5e) demonstrates that pulldown with anti-P2X 1 is ‘clean’ with no non-specific protein binding evident in the IP lanes.

    Article Snippet: Excised whole bladders were put in 0.5 ml ice-cold radio immunoprecipitation assay buffer (RIPA; 50 mM Tris pH 8.0, 150 mM NaCl, 1% v/v NP-40, 0.5% w/v deoxycholic acid, 0.1% w/v SDS) containing Complete Mini Protease Inhibitor Cocktail tablets (Roche, Germany).

    Techniques: Immunoprecipitation, Incubation, Co-Immunoprecipitation Assay, SDS Page, Western Blot, Mouse Assay, Protein Binding

    Immunoprecipitation with anti-P2X 4 antibody. Antibodies to P2X 4 were immobilized onto resin beads and then incubated with mouse bladder lysates to IP the antigen and co-IP interacting proteins. Proteins that were bound (IP: 2.5 µg protein/lane) or did not bind (FT: 25 µg protein/lane) to the beads, were resolved by SDS-PAGE, and Western blots were probed with A ) P2X 1, B) P2X 4 or C ) Nt5e antibodies. ( A ) Left and right panels show P2X 1 immunoblots on IP and FT lysates from wild type and P2X 4 −/− mice. P2X 1 is highly concentrated in the FT fractions. Minor potential P2X 1 staining appears in the IP lane, however this is due to P2X 4 antibody cross-reacting and pulling down some P2X 1 . ( B ) P2X 4 antibody detects P2X 4 as a band at 70 kDa in wild type IP lane, but is absent in P2X 4 −/− mice. The antibody shows minor cross-reactivity to P2X 1 (50 kDa band). ( C ) An antibody to 5′-nucleotidase (Nt5e) demonstrates that pulldown with anti-P2X 4 is ‘clean’ with no non-specific protein binding evident in the IP lanes.

    Journal: Scientific Reports

    Article Title: Role of P2X4 Receptor in Mouse Voiding Function

    doi: 10.1038/s41598-018-20216-4

    Figure Lengend Snippet: Immunoprecipitation with anti-P2X 4 antibody. Antibodies to P2X 4 were immobilized onto resin beads and then incubated with mouse bladder lysates to IP the antigen and co-IP interacting proteins. Proteins that were bound (IP: 2.5 µg protein/lane) or did not bind (FT: 25 µg protein/lane) to the beads, were resolved by SDS-PAGE, and Western blots were probed with A ) P2X 1, B) P2X 4 or C ) Nt5e antibodies. ( A ) Left and right panels show P2X 1 immunoblots on IP and FT lysates from wild type and P2X 4 −/− mice. P2X 1 is highly concentrated in the FT fractions. Minor potential P2X 1 staining appears in the IP lane, however this is due to P2X 4 antibody cross-reacting and pulling down some P2X 1 . ( B ) P2X 4 antibody detects P2X 4 as a band at 70 kDa in wild type IP lane, but is absent in P2X 4 −/− mice. The antibody shows minor cross-reactivity to P2X 1 (50 kDa band). ( C ) An antibody to 5′-nucleotidase (Nt5e) demonstrates that pulldown with anti-P2X 4 is ‘clean’ with no non-specific protein binding evident in the IP lanes.

    Article Snippet: Excised whole bladders were put in 0.5 ml ice-cold radio immunoprecipitation assay buffer (RIPA; 50 mM Tris pH 8.0, 150 mM NaCl, 1% v/v NP-40, 0.5% w/v deoxycholic acid, 0.1% w/v SDS) containing Complete Mini Protease Inhibitor Cocktail tablets (Roche, Germany).

    Techniques: Immunoprecipitation, Incubation, Co-Immunoprecipitation Assay, SDS Page, Western Blot, Mouse Assay, Staining, Protein Binding