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rip elution buffer  (Thermo Fisher)


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    Thermo Fisher rip elution buffer
    a Diagram illustrating the locations <t>of</t> <t>RNA</t> probes (red lines) and primer pairs (blue bars) used in RNA-EMSA and <t>RIP</t> assays. b RNA-EMSA assay showing that CIS1 binds to the FLM Joint 3 probe but not FLM Joint 2 in vitro and that CIS1 shows the strongest binding affinity to short FLM Joint 3 ( FLM Joint 3 s) among the short probes (Intron 2 and FLM Joint 3 s). RNA probes are indicated in ( a ). c RIP-qPCR assay showing the binding affinity of CIS1 protein to FLM pre-mRNA in vivo. Col-0, cry1 cry2 , and cis1-1 (mock) seedlings were grown at 22 °C in LD condition for 7 days and pretreated with darkness (D) for 24 h, treated with MG132 for 2 h, and transferred to blue light (B, 30 μmol m −2 s −1 ) for 4 h. RNA fragments (200–400 nt) extracted from seedlings were immunoprecipitated with anti-CIS1 agarose beads (IP). The precipitated RNA was analyzed by RT-qPCR using different primer pairs of FLM pre-mRNA as indicated in ( a ). The FLM promoter and ACT7 served as negative controls. The level of binding was calculated as the ratio between IP and mock, normalized to that of IPP2 as an internal control; n.d., not detected. Error bars, s.d. of three biological replicates. d Co-localization of CIS1 and U2AF65A proteins in nuclear speckles in N. benthamiana . mCherry served as a negative control. Scale bar = 5 μm. e BiFC assay showing in vivo protein interactions between CIS1 and U2AF65A. CIS1(ΔN)-nYFP and cCFP-U2AF65B were used as negative controls. N. benthamiana leaf epidermal cells were co-infiltrated with the indicated constructs. Scale bar = 20 μm. In b , d , e , three independent experiments were performed with similar results.
    Rip Elution Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rip elution buffer/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    rip elution buffer - by Bioz Stars, 2026-06
    99/100 stars

    Images

    1) Product Images from "CRY2 interacts with CIS1 to regulate thermosensory flowering via FLM alternative splicing"

    Article Title: CRY2 interacts with CIS1 to regulate thermosensory flowering via FLM alternative splicing

    Journal: Nature Communications

    doi: 10.1038/s41467-022-34886-2

    a Diagram illustrating the locations of RNA probes (red lines) and primer pairs (blue bars) used in RNA-EMSA and RIP assays. b RNA-EMSA assay showing that CIS1 binds to the FLM Joint 3 probe but not FLM Joint 2 in vitro and that CIS1 shows the strongest binding affinity to short FLM Joint 3 ( FLM Joint 3 s) among the short probes (Intron 2 and FLM Joint 3 s). RNA probes are indicated in ( a ). c RIP-qPCR assay showing the binding affinity of CIS1 protein to FLM pre-mRNA in vivo. Col-0, cry1 cry2 , and cis1-1 (mock) seedlings were grown at 22 °C in LD condition for 7 days and pretreated with darkness (D) for 24 h, treated with MG132 for 2 h, and transferred to blue light (B, 30 μmol m −2 s −1 ) for 4 h. RNA fragments (200–400 nt) extracted from seedlings were immunoprecipitated with anti-CIS1 agarose beads (IP). The precipitated RNA was analyzed by RT-qPCR using different primer pairs of FLM pre-mRNA as indicated in ( a ). The FLM promoter and ACT7 served as negative controls. The level of binding was calculated as the ratio between IP and mock, normalized to that of IPP2 as an internal control; n.d., not detected. Error bars, s.d. of three biological replicates. d Co-localization of CIS1 and U2AF65A proteins in nuclear speckles in N. benthamiana . mCherry served as a negative control. Scale bar = 5 μm. e BiFC assay showing in vivo protein interactions between CIS1 and U2AF65A. CIS1(ΔN)-nYFP and cCFP-U2AF65B were used as negative controls. N. benthamiana leaf epidermal cells were co-infiltrated with the indicated constructs. Scale bar = 20 μm. In b , d , e , three independent experiments were performed with similar results.
    Figure Legend Snippet: a Diagram illustrating the locations of RNA probes (red lines) and primer pairs (blue bars) used in RNA-EMSA and RIP assays. b RNA-EMSA assay showing that CIS1 binds to the FLM Joint 3 probe but not FLM Joint 2 in vitro and that CIS1 shows the strongest binding affinity to short FLM Joint 3 ( FLM Joint 3 s) among the short probes (Intron 2 and FLM Joint 3 s). RNA probes are indicated in ( a ). c RIP-qPCR assay showing the binding affinity of CIS1 protein to FLM pre-mRNA in vivo. Col-0, cry1 cry2 , and cis1-1 (mock) seedlings were grown at 22 °C in LD condition for 7 days and pretreated with darkness (D) for 24 h, treated with MG132 for 2 h, and transferred to blue light (B, 30 μmol m −2 s −1 ) for 4 h. RNA fragments (200–400 nt) extracted from seedlings were immunoprecipitated with anti-CIS1 agarose beads (IP). The precipitated RNA was analyzed by RT-qPCR using different primer pairs of FLM pre-mRNA as indicated in ( a ). The FLM promoter and ACT7 served as negative controls. The level of binding was calculated as the ratio between IP and mock, normalized to that of IPP2 as an internal control; n.d., not detected. Error bars, s.d. of three biological replicates. d Co-localization of CIS1 and U2AF65A proteins in nuclear speckles in N. benthamiana . mCherry served as a negative control. Scale bar = 5 μm. e BiFC assay showing in vivo protein interactions between CIS1 and U2AF65A. CIS1(ΔN)-nYFP and cCFP-U2AF65B were used as negative controls. N. benthamiana leaf epidermal cells were co-infiltrated with the indicated constructs. Scale bar = 20 μm. In b , d , e , three independent experiments were performed with similar results.

    Techniques Used: In Vitro, Binding Assay, In Vivo, Immunoprecipitation, Quantitative RT-PCR, Control, Negative Control, Bimolecular Fluorescence Complementation Assay, Construct



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    rip elution buffer  (Thermo Fisher)
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    a Diagram illustrating the locations <t>of</t> <t>RNA</t> probes (red lines) and primer pairs (blue bars) used in RNA-EMSA and <t>RIP</t> assays. b RNA-EMSA assay showing that CIS1 binds to the FLM Joint 3 probe but not FLM Joint 2 in vitro and that CIS1 shows the strongest binding affinity to short FLM Joint 3 ( FLM Joint 3 s) among the short probes (Intron 2 and FLM Joint 3 s). RNA probes are indicated in ( a ). c RIP-qPCR assay showing the binding affinity of CIS1 protein to FLM pre-mRNA in vivo. Col-0, cry1 cry2 , and cis1-1 (mock) seedlings were grown at 22 °C in LD condition for 7 days and pretreated with darkness (D) for 24 h, treated with MG132 for 2 h, and transferred to blue light (B, 30 μmol m −2 s −1 ) for 4 h. RNA fragments (200–400 nt) extracted from seedlings were immunoprecipitated with anti-CIS1 agarose beads (IP). The precipitated RNA was analyzed by RT-qPCR using different primer pairs of FLM pre-mRNA as indicated in ( a ). The FLM promoter and ACT7 served as negative controls. The level of binding was calculated as the ratio between IP and mock, normalized to that of IPP2 as an internal control; n.d., not detected. Error bars, s.d. of three biological replicates. d Co-localization of CIS1 and U2AF65A proteins in nuclear speckles in N. benthamiana . mCherry served as a negative control. Scale bar = 5 μm. e BiFC assay showing in vivo protein interactions between CIS1 and U2AF65A. CIS1(ΔN)-nYFP and cCFP-U2AF65B were used as negative controls. N. benthamiana leaf epidermal cells were co-infiltrated with the indicated constructs. Scale bar = 20 μm. In b , d , e , three independent experiments were performed with similar results.
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    a Diagram illustrating the locations <t>of</t> <t>RNA</t> probes (red lines) and primer pairs (blue bars) used in RNA-EMSA and <t>RIP</t> assays. b RNA-EMSA assay showing that CIS1 binds to the FLM Joint 3 probe but not FLM Joint 2 in vitro and that CIS1 shows the strongest binding affinity to short FLM Joint 3 ( FLM Joint 3 s) among the short probes (Intron 2 and FLM Joint 3 s). RNA probes are indicated in ( a ). c RIP-qPCR assay showing the binding affinity of CIS1 protein to FLM pre-mRNA in vivo. Col-0, cry1 cry2 , and cis1-1 (mock) seedlings were grown at 22 °C in LD condition for 7 days and pretreated with darkness (D) for 24 h, treated with MG132 for 2 h, and transferred to blue light (B, 30 μmol m −2 s −1 ) for 4 h. RNA fragments (200–400 nt) extracted from seedlings were immunoprecipitated with anti-CIS1 agarose beads (IP). The precipitated RNA was analyzed by RT-qPCR using different primer pairs of FLM pre-mRNA as indicated in ( a ). The FLM promoter and ACT7 served as negative controls. The level of binding was calculated as the ratio between IP and mock, normalized to that of IPP2 as an internal control; n.d., not detected. Error bars, s.d. of three biological replicates. d Co-localization of CIS1 and U2AF65A proteins in nuclear speckles in N. benthamiana . mCherry served as a negative control. Scale bar = 5 μm. e BiFC assay showing in vivo protein interactions between CIS1 and U2AF65A. CIS1(ΔN)-nYFP and cCFP-U2AF65B were used as negative controls. N. benthamiana leaf epidermal cells were co-infiltrated with the indicated constructs. Scale bar = 20 μm. In b , d , e , three independent experiments were performed with similar results.
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    Image Search Results


    a Diagram illustrating the locations of RNA probes (red lines) and primer pairs (blue bars) used in RNA-EMSA and RIP assays. b RNA-EMSA assay showing that CIS1 binds to the FLM Joint 3 probe but not FLM Joint 2 in vitro and that CIS1 shows the strongest binding affinity to short FLM Joint 3 ( FLM Joint 3 s) among the short probes (Intron 2 and FLM Joint 3 s). RNA probes are indicated in ( a ). c RIP-qPCR assay showing the binding affinity of CIS1 protein to FLM pre-mRNA in vivo. Col-0, cry1 cry2 , and cis1-1 (mock) seedlings were grown at 22 °C in LD condition for 7 days and pretreated with darkness (D) for 24 h, treated with MG132 for 2 h, and transferred to blue light (B, 30 μmol m −2 s −1 ) for 4 h. RNA fragments (200–400 nt) extracted from seedlings were immunoprecipitated with anti-CIS1 agarose beads (IP). The precipitated RNA was analyzed by RT-qPCR using different primer pairs of FLM pre-mRNA as indicated in ( a ). The FLM promoter and ACT7 served as negative controls. The level of binding was calculated as the ratio between IP and mock, normalized to that of IPP2 as an internal control; n.d., not detected. Error bars, s.d. of three biological replicates. d Co-localization of CIS1 and U2AF65A proteins in nuclear speckles in N. benthamiana . mCherry served as a negative control. Scale bar = 5 μm. e BiFC assay showing in vivo protein interactions between CIS1 and U2AF65A. CIS1(ΔN)-nYFP and cCFP-U2AF65B were used as negative controls. N. benthamiana leaf epidermal cells were co-infiltrated with the indicated constructs. Scale bar = 20 μm. In b , d , e , three independent experiments were performed with similar results.

    Journal: Nature Communications

    Article Title: CRY2 interacts with CIS1 to regulate thermosensory flowering via FLM alternative splicing

    doi: 10.1038/s41467-022-34886-2

    Figure Lengend Snippet: a Diagram illustrating the locations of RNA probes (red lines) and primer pairs (blue bars) used in RNA-EMSA and RIP assays. b RNA-EMSA assay showing that CIS1 binds to the FLM Joint 3 probe but not FLM Joint 2 in vitro and that CIS1 shows the strongest binding affinity to short FLM Joint 3 ( FLM Joint 3 s) among the short probes (Intron 2 and FLM Joint 3 s). RNA probes are indicated in ( a ). c RIP-qPCR assay showing the binding affinity of CIS1 protein to FLM pre-mRNA in vivo. Col-0, cry1 cry2 , and cis1-1 (mock) seedlings were grown at 22 °C in LD condition for 7 days and pretreated with darkness (D) for 24 h, treated with MG132 for 2 h, and transferred to blue light (B, 30 μmol m −2 s −1 ) for 4 h. RNA fragments (200–400 nt) extracted from seedlings were immunoprecipitated with anti-CIS1 agarose beads (IP). The precipitated RNA was analyzed by RT-qPCR using different primer pairs of FLM pre-mRNA as indicated in ( a ). The FLM promoter and ACT7 served as negative controls. The level of binding was calculated as the ratio between IP and mock, normalized to that of IPP2 as an internal control; n.d., not detected. Error bars, s.d. of three biological replicates. d Co-localization of CIS1 and U2AF65A proteins in nuclear speckles in N. benthamiana . mCherry served as a negative control. Scale bar = 5 μm. e BiFC assay showing in vivo protein interactions between CIS1 and U2AF65A. CIS1(ΔN)-nYFP and cCFP-U2AF65B were used as negative controls. N. benthamiana leaf epidermal cells were co-infiltrated with the indicated constructs. Scale bar = 20 μm. In b , d , e , three independent experiments were performed with similar results.

    Article Snippet: The bound RNA fragments were eluted with RIP Elution Buffer [100 mM Tris–HCl pH 8.0, 10 mM EDTA, 1% SDS, and 100 U/mL RNase inhibitor] with 50 μg Proteinase-K (Thermo) for each sample, incubated 0.5 h at 55 °C.

    Techniques: In Vitro, Binding Assay, In Vivo, Immunoprecipitation, Quantitative RT-PCR, Control, Negative Control, Bimolecular Fluorescence Complementation Assay, Construct