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trf1  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology trf1
Figure 1. Effect of compound 2c on the binding of <t>TRF1</t> with telomeric DNA. (A) Structure of 2c. (B) Electrophoretic mobility shift (EMSA) assay for effect of 2c on disrupting the binding between TRF1 and oligonucleotide T-21GC. Lane 1, 1 μM T-21GC. Lane 2, 3 μM TRF1. Lanes 3–10, DMSO or 2c (0.39, 0.78, 1.56, 3.125, 6.25, 12.5 and 25.0 μM) was added into the mixture of TRF1 with T-21GC. TRF1-DNA complex is the binding combination of TRF1 and T-21GC, while free DNA is T-21GC only. (C) Enzyme-linked immunosorbent assay (ELISA) for the effect of 2c on the binding of TRF1 or TRF2 to oligonucleotide T-21GC. The data were derived from three experiments and were shown as the means ± S.E.M. (D) Filter-binding assay result for the effect of 2c on the binding of TRF1 to oligonucleotide T-21GC.
Trf1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Figure 1. Effect of compound 2c on the binding of TRF1 with telomeric DNA. (A) Structure of 2c. (B) Electrophoretic mobility shift (EMSA) assay for effect of 2c on disrupting the binding between TRF1 and oligonucleotide T-21GC. Lane 1, 1 μM T-21GC. Lane 2, 3 μM TRF1. Lanes 3–10, DMSO or 2c (0.39, 0.78, 1.56, 3.125, 6.25, 12.5 and 25.0 μM) was added into the mixture of TRF1 with T-21GC. TRF1-DNA complex is the binding combination of TRF1 and T-21GC, while free DNA is T-21GC only. (C) Enzyme-linked immunosorbent assay (ELISA) for the effect of 2c on the binding of TRF1 or TRF2 to oligonucleotide T-21GC. The data were derived from three experiments and were shown as the means ± S.E.M. (D) Filter-binding assay result for the effect of 2c on the binding of TRF1 to oligonucleotide T-21GC.

Journal: RNA biology

Article Title: Transcriptional regulation of telomeric repeat-containing RNA by acridine derivatives.

doi: 10.1080/15476286.2021.1899652

Figure Lengend Snippet: Figure 1. Effect of compound 2c on the binding of TRF1 with telomeric DNA. (A) Structure of 2c. (B) Electrophoretic mobility shift (EMSA) assay for effect of 2c on disrupting the binding between TRF1 and oligonucleotide T-21GC. Lane 1, 1 μM T-21GC. Lane 2, 3 μM TRF1. Lanes 3–10, DMSO or 2c (0.39, 0.78, 1.56, 3.125, 6.25, 12.5 and 25.0 μM) was added into the mixture of TRF1 with T-21GC. TRF1-DNA complex is the binding combination of TRF1 and T-21GC, while free DNA is T-21GC only. (C) Enzyme-linked immunosorbent assay (ELISA) for the effect of 2c on the binding of TRF1 or TRF2 to oligonucleotide T-21GC. The data were derived from three experiments and were shown as the means ± S.E.M. (D) Filter-binding assay result for the effect of 2c on the binding of TRF1 to oligonucleotide T-21GC.

Article Snippet: For immunolabeling experiments, cells were incubated with the following primary antibodies: γH2AX antibody (#9718, Cell Signaling Technology), TRF1 (#sc-271,485, Santa Cruz) and TRF2 antibody (#ab23579, Abcam) at 4°C overnight.

Techniques: Binding Assay, Electrophoretic Mobility Shift Assay, Enzyme-linked Immunosorbent Assay, Derivative Assay, Filter-binding Assay

Figure 2. Further studies for effect and selectivity of compound 2c. (A) MST experimental result for the binding of fluorescently labelled TRF1 to 2c. The data of MST were evaluated using NT Analysis 1.4.23. (B) MST experimental result for the binding of fluorescently labelled T-21GC to 2c. (C) MST experimental result for the binding of fluorescently labelled TRF2 to 2c. (D) ChIP experiment was used to evaluate the effect of 2c on disruption of the binding between TRF1 and telomeric DNA inside A549 cells. Normal rabbit IgG was used as a negative control for mock immunoprecipitation. Immunoprecipitated DNA samples were PCR-amplified to show TRF1 occupancy of the oligonucleotide of telomere, and the amplified products were separated on 2.0% agarose gel.

Journal: RNA biology

Article Title: Transcriptional regulation of telomeric repeat-containing RNA by acridine derivatives.

doi: 10.1080/15476286.2021.1899652

Figure Lengend Snippet: Figure 2. Further studies for effect and selectivity of compound 2c. (A) MST experimental result for the binding of fluorescently labelled TRF1 to 2c. The data of MST were evaluated using NT Analysis 1.4.23. (B) MST experimental result for the binding of fluorescently labelled T-21GC to 2c. (C) MST experimental result for the binding of fluorescently labelled TRF2 to 2c. (D) ChIP experiment was used to evaluate the effect of 2c on disruption of the binding between TRF1 and telomeric DNA inside A549 cells. Normal rabbit IgG was used as a negative control for mock immunoprecipitation. Immunoprecipitated DNA samples were PCR-amplified to show TRF1 occupancy of the oligonucleotide of telomere, and the amplified products were separated on 2.0% agarose gel.

Article Snippet: For immunolabeling experiments, cells were incubated with the following primary antibodies: γH2AX antibody (#9718, Cell Signaling Technology), TRF1 (#sc-271,485, Santa Cruz) and TRF2 antibody (#ab23579, Abcam) at 4°C overnight.

Techniques: Binding Assay, Disruption, Negative Control, Immunoprecipitation, Amplification, Agarose Gel Electrophoresis

Figure 4. In-depth study for regulation and effect of TERRA. (A) Compound DI26 down-regulated TERRA transcription in A549 cells upon 24 h incubation. (B) Compound 2c up-regulated TERRA transcription in A549 cells upon 24 h incubation. (C) TRF1 could tightly bind to TERRA, which was analysed by using ELISA. (D) Addition of compound 2c had no effect on binding affinity between TRF1 and TERRA, indicating that TRF1 bound to TERRA possibly with its allosteric site. (E) TRF1 could tightly bind to telomeric duplex DNA, and the binding affinity was significantly reduced upon addition of TERRA, indicating that TERRA could be an allosteric inhibitor of TRF1.

Journal: RNA biology

Article Title: Transcriptional regulation of telomeric repeat-containing RNA by acridine derivatives.

doi: 10.1080/15476286.2021.1899652

Figure Lengend Snippet: Figure 4. In-depth study for regulation and effect of TERRA. (A) Compound DI26 down-regulated TERRA transcription in A549 cells upon 24 h incubation. (B) Compound 2c up-regulated TERRA transcription in A549 cells upon 24 h incubation. (C) TRF1 could tightly bind to TERRA, which was analysed by using ELISA. (D) Addition of compound 2c had no effect on binding affinity between TRF1 and TERRA, indicating that TRF1 bound to TERRA possibly with its allosteric site. (E) TRF1 could tightly bind to telomeric duplex DNA, and the binding affinity was significantly reduced upon addition of TERRA, indicating that TERRA could be an allosteric inhibitor of TRF1.

Article Snippet: For immunolabeling experiments, cells were incubated with the following primary antibodies: γH2AX antibody (#9718, Cell Signaling Technology), TRF1 (#sc-271,485, Santa Cruz) and TRF2 antibody (#ab23579, Abcam) at 4°C overnight.

Techniques: Incubation, Enzyme-linked Immunosorbent Assay, Binding Assay