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FUBP3 binds the minimal NLRP3 promoter in neurons. (A) The indicated DNA fragments from the promoter region of NLRP3 were biotin-labeled and used to pull down bound proteins from Neuro2A cell nuclear extracts. The –21 to +217 fragment, which has no promoter activity, was used as a negative control. The precipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the gel was stained with Coomassie Blue. The ~ 70 kDa band was excised and analyzed by mass spectrometry. Transcription factors represented by high amounts of peptide in the mass spectrometry results are listed. (B) 5′ and 3’ biotin-labeled Del5, the minimal promoter, were used to pull down FUBP3 from Neuro2A nuclear extracts. A 5′ labeled irrelevant DNA (ir. DNA) was used as the control. Western blot analysis of FUBP3 in the precipitates, and equal loading of the bait DNAs, (input probes), as assessed by <t>EMSA.</t> (C) Neuro2A nuclear extracts were mixed with the 5′ labeled probe (Del5), and the mixtures were loaded onto native gels and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP3 antibody. (D) Neuro2A nuclear extracts were mixed with the 5′ labeled single-stranded probe. After incubation for 30 minutes at room temperature, the mixtures were loaded onto native gels, and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP1 antibody. (E) The listed components were mixed, and the mixtures were subjected to regular EMSA. a.s.: Antisense strand; ds: double strand probes; EMSA: electrophoretic mobility shift assay; FUBP1: far upstream binding protein 1; NLRP3: NOD-, LRR- and pyrin domain-containing protein 3; sen: sense strand; ss: single strand; WB: western blot.
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FUBP3 binds the minimal NLRP3 promoter in neurons. (A) The indicated DNA fragments from the promoter region of NLRP3 were biotin-labeled and used to pull down bound proteins from Neuro2A cell nuclear extracts. The –21 to +217 fragment, which has no promoter activity, was used as a negative control. The precipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the gel was stained with Coomassie Blue. The ~ 70 kDa band was excised and analyzed by mass spectrometry. Transcription factors represented by high amounts of peptide in the mass spectrometry results are listed. (B) 5′ and 3’ biotin-labeled Del5, the minimal promoter, were used to pull down FUBP3 from Neuro2A nuclear extracts. A 5′ labeled irrelevant DNA (ir. DNA) was used as the control. Western blot analysis of FUBP3 in the precipitates, and equal loading of the bait DNAs, (input probes), as assessed by <t>EMSA.</t> (C) Neuro2A nuclear extracts were mixed with the 5′ labeled probe (Del5), and the mixtures were loaded onto native gels and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP3 antibody. (D) Neuro2A nuclear extracts were mixed with the 5′ labeled single-stranded probe. After incubation for 30 minutes at room temperature, the mixtures were loaded onto native gels, and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP1 antibody. (E) The listed components were mixed, and the mixtures were subjected to regular EMSA. a.s.: Antisense strand; ds: double strand probes; EMSA: electrophoretic mobility shift assay; FUBP1: far upstream binding protein 1; NLRP3: NOD-, LRR- and pyrin domain-containing protein 3; sen: sense strand; ss: single strand; WB: western blot.
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FUBP3 binds the minimal NLRP3 promoter in neurons. (A) The indicated DNA fragments from the promoter region of NLRP3 were biotin-labeled and used to pull down bound proteins from Neuro2A cell nuclear extracts. The –21 to +217 fragment, which has no promoter activity, was used as a negative control. The precipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the gel was stained with Coomassie Blue. The ~ 70 kDa band was excised and analyzed by mass spectrometry. Transcription factors represented by high amounts of peptide in the mass spectrometry results are listed. (B) 5′ and 3’ biotin-labeled Del5, the minimal promoter, were used to pull down FUBP3 from Neuro2A nuclear extracts. A 5′ labeled irrelevant DNA (ir. DNA) was used as the control. Western blot analysis of FUBP3 in the precipitates, and equal loading of the bait DNAs, (input probes), as assessed by <t>EMSA.</t> (C) Neuro2A nuclear extracts were mixed with the 5′ labeled probe (Del5), and the mixtures were loaded onto native gels and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP3 antibody. (D) Neuro2A nuclear extracts were mixed with the 5′ labeled single-stranded probe. After incubation for 30 minutes at room temperature, the mixtures were loaded onto native gels, and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP1 antibody. (E) The listed components were mixed, and the mixtures were subjected to regular EMSA. a.s.: Antisense strand; ds: double strand probes; EMSA: electrophoretic mobility shift assay; FUBP1: far upstream binding protein 1; NLRP3: NOD-, LRR- and pyrin domain-containing protein 3; sen: sense strand; ss: single strand; WB: western blot.
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FUBP3 binds the minimal NLRP3 promoter in neurons. (A) The indicated DNA fragments from the promoter region of NLRP3 were biotin-labeled and used to pull down bound proteins from Neuro2A cell nuclear extracts. The –21 to +217 fragment, which has no promoter activity, was used as a negative control. The precipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the gel was stained with Coomassie Blue. The ~ 70 kDa band was excised and analyzed by mass spectrometry. Transcription factors represented by high amounts of peptide in the mass spectrometry results are listed. (B) 5′ and 3’ biotin-labeled Del5, the minimal promoter, were used to pull down FUBP3 from Neuro2A nuclear extracts. A 5′ labeled irrelevant DNA (ir. DNA) was used as the control. Western blot analysis of FUBP3 in the precipitates, and equal loading of the bait DNAs, (input probes), as assessed by <t>EMSA.</t> (C) Neuro2A nuclear extracts were mixed with the 5′ labeled probe (Del5), and the mixtures were loaded onto native gels and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP3 antibody. (D) Neuro2A nuclear extracts were mixed with the 5′ labeled single-stranded probe. After incubation for 30 minutes at room temperature, the mixtures were loaded onto native gels, and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP1 antibody. (E) The listed components were mixed, and the mixtures were subjected to regular EMSA. a.s.: Antisense strand; ds: double strand probes; EMSA: electrophoretic mobility shift assay; FUBP1: far upstream binding protein 1; NLRP3: NOD-, LRR- and pyrin domain-containing protein 3; sen: sense strand; ss: single strand; WB: western blot.
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FUBP3 binds the minimal NLRP3 promoter in neurons. (A) The indicated DNA fragments from the promoter region of NLRP3 were biotin-labeled and used to pull down bound proteins from Neuro2A cell nuclear extracts. The –21 to +217 fragment, which has no promoter activity, was used as a negative control. The precipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the gel was stained with Coomassie Blue. The ~ 70 kDa band was excised and analyzed by mass spectrometry. Transcription factors represented by high amounts of peptide in the mass spectrometry results are listed. (B) 5′ and 3’ biotin-labeled Del5, the minimal promoter, were used to pull down FUBP3 from Neuro2A nuclear extracts. A 5′ labeled irrelevant DNA (ir. DNA) was used as the control. Western blot analysis of FUBP3 in the precipitates, and equal loading of the bait DNAs, (input probes), as assessed by <t>EMSA.</t> (C) Neuro2A nuclear extracts were mixed with the 5′ labeled probe (Del5), and the mixtures were loaded onto native gels and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP3 antibody. (D) Neuro2A nuclear extracts were mixed with the 5′ labeled single-stranded probe. After incubation for 30 minutes at room temperature, the mixtures were loaded onto native gels, and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP1 antibody. (E) The listed components were mixed, and the mixtures were subjected to regular EMSA. a.s.: Antisense strand; ds: double strand probes; EMSA: electrophoretic mobility shift assay; FUBP1: far upstream binding protein 1; NLRP3: NOD-, LRR- and pyrin domain-containing protein 3; sen: sense strand; ss: single strand; WB: western blot.
Chemiluminescent Emsa Kit, supplied by Beyotime, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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FUBP3 binds the minimal NLRP3 promoter in neurons. (A) The indicated DNA fragments from the promoter region of NLRP3 were biotin-labeled and used to pull down bound proteins from Neuro2A cell nuclear extracts. The –21 to +217 fragment, which has no promoter activity, was used as a negative control. The precipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the gel was stained with Coomassie Blue. The ~ 70 kDa band was excised and analyzed by mass spectrometry. Transcription factors represented by high amounts of peptide in the mass spectrometry results are listed. (B) 5′ and 3’ biotin-labeled Del5, the minimal promoter, were used to pull down FUBP3 from Neuro2A nuclear extracts. A 5′ labeled irrelevant DNA (ir. DNA) was used as the control. Western blot analysis of FUBP3 in the precipitates, and equal loading of the bait DNAs, (input probes), as assessed by <t>EMSA.</t> (C) Neuro2A nuclear extracts were mixed with the 5′ labeled probe (Del5), and the mixtures were loaded onto native gels and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP3 antibody. (D) Neuro2A nuclear extracts were mixed with the 5′ labeled single-stranded probe. After incubation for 30 minutes at room temperature, the mixtures were loaded onto native gels, and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP1 antibody. (E) The listed components were mixed, and the mixtures were subjected to regular EMSA. a.s.: Antisense strand; ds: double strand probes; EMSA: electrophoretic mobility shift assay; FUBP1: far upstream binding protein 1; NLRP3: NOD-, LRR- and pyrin domain-containing protein 3; sen: sense strand; ss: single strand; WB: western blot.
Lightshift Chemiluminescent Emsa Kit, supplied by Beyotime, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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FUBP3 binds the minimal NLRP3 promoter in neurons. (A) The indicated DNA fragments from the promoter region of NLRP3 were biotin-labeled and used to pull down bound proteins from Neuro2A cell nuclear extracts. The –21 to +217 fragment, which has no promoter activity, was used as a negative control. The precipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the gel was stained with Coomassie Blue. The ~ 70 kDa band was excised and analyzed by mass spectrometry. Transcription factors represented by high amounts of peptide in the mass spectrometry results are listed. (B) 5′ and 3’ biotin-labeled Del5, the minimal promoter, were used to pull down FUBP3 from Neuro2A nuclear extracts. A 5′ labeled irrelevant DNA (ir. DNA) was used as the control. Western blot analysis of FUBP3 in the precipitates, and equal loading of the bait DNAs, (input probes), as assessed by EMSA. (C) Neuro2A nuclear extracts were mixed with the 5′ labeled probe (Del5), and the mixtures were loaded onto native gels and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP3 antibody. (D) Neuro2A nuclear extracts were mixed with the 5′ labeled single-stranded probe. After incubation for 30 minutes at room temperature, the mixtures were loaded onto native gels, and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP1 antibody. (E) The listed components were mixed, and the mixtures were subjected to regular EMSA. a.s.: Antisense strand; ds: double strand probes; EMSA: electrophoretic mobility shift assay; FUBP1: far upstream binding protein 1; NLRP3: NOD-, LRR- and pyrin domain-containing protein 3; sen: sense strand; ss: single strand; WB: western blot.

Journal: Neural Regeneration Research

Article Title: FUBP3 mediates the amyloid-β-induced neuronal NLRP3 expression

doi: 10.4103/NRR.NRR-D-23-01799

Figure Lengend Snippet: FUBP3 binds the minimal NLRP3 promoter in neurons. (A) The indicated DNA fragments from the promoter region of NLRP3 were biotin-labeled and used to pull down bound proteins from Neuro2A cell nuclear extracts. The –21 to +217 fragment, which has no promoter activity, was used as a negative control. The precipitated proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the gel was stained with Coomassie Blue. The ~ 70 kDa band was excised and analyzed by mass spectrometry. Transcription factors represented by high amounts of peptide in the mass spectrometry results are listed. (B) 5′ and 3’ biotin-labeled Del5, the minimal promoter, were used to pull down FUBP3 from Neuro2A nuclear extracts. A 5′ labeled irrelevant DNA (ir. DNA) was used as the control. Western blot analysis of FUBP3 in the precipitates, and equal loading of the bait DNAs, (input probes), as assessed by EMSA. (C) Neuro2A nuclear extracts were mixed with the 5′ labeled probe (Del5), and the mixtures were loaded onto native gels and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP3 antibody. (D) Neuro2A nuclear extracts were mixed with the 5′ labeled single-stranded probe. After incubation for 30 minutes at room temperature, the mixtures were loaded onto native gels, and transferred to nylon membranes for regular EMSA or to nitrocellulose membranes for EMSA–western blot using an anti-FUBP1 antibody. (E) The listed components were mixed, and the mixtures were subjected to regular EMSA. a.s.: Antisense strand; ds: double strand probes; EMSA: electrophoretic mobility shift assay; FUBP1: far upstream binding protein 1; NLRP3: NOD-, LRR- and pyrin domain-containing protein 3; sen: sense strand; ss: single strand; WB: western blot.

Article Snippet: An electrophoretic mobility shift assay (EMSA) for FUBP3 was conducted using a Lightshift Chemiluminescent EMSA kit (Pierce, Rockford, IL, USA), following the manufacturer’s instructions.

Techniques: Labeling, Activity Assay, Negative Control, Polyacrylamide Gel Electrophoresis, Staining, Mass Spectrometry, Control, Western Blot, Incubation, Electrophoretic Mobility Shift Assay, Binding Assay