rnase h elution buffer Search Results


elution buffer  (Zymo Research)
96
Zymo Research elution buffer
Elution Buffer, supplied by Zymo Research, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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elution buffer  (Thermo Fisher)
99
Thermo Fisher elution buffer
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
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Average 99 stars, based on 1 article reviews
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rip elution buffer  (Thermo Fisher)
99
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, 2026-04
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tg1 bacterial cells  (Lucigen Corp)
90
Lucigen Corp tg1 bacterial cells
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.
Tg1 Bacterial Cells, supplied by Lucigen Corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/tg1 bacterial cells/product/Lucigen Corp
Average 90 stars, based on 1 article reviews
tg1 bacterial cells - by Bioz Stars, 2026-04
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rnase  (Qiagen)
96
Qiagen rnase
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.
Rnase, supplied by Qiagen, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rnase/product/Qiagen
Average 96 stars, based on 1 article reviews
rnase - by Bioz Stars, 2026-04
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elution buffer  (New England Biolabs)
98
New England Biolabs 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.
Elution Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/elution buffer/product/New England Biolabs
Average 98 stars, based on 1 article reviews
elution buffer - by Bioz Stars, 2026-04
98/100 stars
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elution buffer  (Qiagen)
96
Qiagen 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.
Elution Buffer, supplied by Qiagen, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/elution buffer/product/Qiagen
Average 96 stars, based on 1 article reviews
elution buffer - by Bioz Stars, 2026-04
96/100 stars
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rnase h elution buffer  (New England Biolabs)
98
New England Biolabs rnase h 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.
Rnase H Elution Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rnase h elution buffer/product/New England Biolabs
Average 98 stars, based on 1 article reviews
rnase h elution buffer - by Bioz Stars, 2026-04
98/100 stars
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concentrator plus 5301  (Eppendorf AG)
90
Eppendorf AG concentrator plus 5301
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.
Concentrator Plus 5301, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/concentrator plus 5301/product/Eppendorf AG
Average 90 stars, based on 1 article reviews
concentrator plus 5301 - by Bioz Stars, 2026-04
90/100 stars
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rnase free elution buffer  (Qiagen)
90
Qiagen rnase free 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.
Rnase Free Elution Buffer, supplied by Qiagen, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rnase free elution buffer/product/Qiagen
Average 90 stars, based on 1 article reviews
rnase free elution buffer - by Bioz Stars, 2026-04
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rnasin® ribonuclease inhibitor  (Promega)
90
Promega rnasin® ribonuclease inhibitor
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.
Rnasin® Ribonuclease Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rnasin® ribonuclease inhibitor/product/Promega
Average 90 stars, based on 1 article reviews
rnasin® ribonuclease inhibitor - by Bioz Stars, 2026-04
90/100 stars
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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