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arid1a  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc arid1a
    Arid1a, supplied by Cell Signaling Technology Inc, 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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    A, Alignment of the SIN3A PRISMA binding profile to <t>ARID1A</t> tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between <t>recombinant</t> <t>ARID1A-V5</t> and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.
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    A, Alignment of the SIN3A PRISMA binding profile to <t>ARID1A</t> tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between <t>recombinant</t> <t>ARID1A-V5</t> and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.
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    A, Alignment of the SIN3A PRISMA binding profile to <t>ARID1A</t> tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between <t>recombinant</t> <t>ARID1A-V5</t> and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.
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    A, Alignment of the SIN3A PRISMA binding profile to <t>ARID1A</t> tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between <t>recombinant</t> <t>ARID1A-V5</t> and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.
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    A, Alignment of the SIN3A PRISMA binding profile to <t>ARID1A</t> tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between <t>recombinant</t> <t>ARID1A-V5</t> and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.
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    A, Alignment of the SIN3A PRISMA binding profile to <t>ARID1A</t> tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between <t>recombinant</t> <t>ARID1A-V5</t> and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.
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    A, Alignment of the SIN3A PRISMA binding profile to <t>ARID1A</t> tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between <t>recombinant</t> <t>ARID1A-V5</t> and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.
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    Cell Signaling Technology Inc antibodies against arid1a
    miR-663a is induced in esophageal cancer cells upon <t>ARID1A</t> depletion. (A) Bioinformatics analysis showed 14 differentially expressed miRs between esophageal cancer and adjacent normal tissues based on GEO datasets ( GSE157805 and GSE145198 ). (B) The protein expression of ARID1A in esophageal cancer cells transfected with shCtrl or ARID1A-targeting shRNAs was measured by Western blot analysis. GAPDH was used as the loading control. (C) Measurement of miR-663a levels in esophageal cancer cells transfected with indicated shRNAs. ***, P<0.001 vs . shCtrl. (D) The expression level of miR-663a in 50 pairs of esophageal cancer and adjacent normal tissues measured by quantitative real-time PCR analysis. (E) The correlation between the miR-663a and ARID1A mRNA expression levels in the 50 cases of esophageal cancer tissues. (F) Overall survival analysis in esophageal cancer patients according to the miR-663a expression level using the data from Kaplan-Meier plotter. Data in parentheses are 95% confidence interval. GEO, Gene Expression Omnibus; HR, hazard ratio; miR, microRNA; PCR, polymerase chain reaction; shCtrl, control shRNA; shRNA, short hairpin RNA.
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    Image Search Results


    A, Alignment of the SIN3A PRISMA binding profile to ARID1A tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between recombinant ARID1A-V5 and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.

    Journal: bioRxiv

    Article Title: High resolution interaction surface mapping by PRISMA reveals novel ARID1A interactions

    doi: 10.64898/2026.03.15.711656

    Figure Lengend Snippet: A, Alignment of the SIN3A PRISMA binding profile to ARID1A tiled peptide array and the Sin3 SLiM ELM prediction on ARID1A . B, Bar graph representing levels of SIN3A on chromatin in ARID1A KO and parental RPE1 cells (n=3, mean ± SD, * p< 0.05, *** p< 0.00005). C, Co-immunoprecipitation of endogenous SIN3 complex (circled) by ARID1A C-terminal fragment GFP pulldown. D, Schematic of the in vitro binding experiment between recombinant ARID1A-V5 and SIN3A fragment (449-1086) containing the PAH3 domain tagged with StrepII tag. E, Co-immunoprecipitation of recombinant ARID1A-V5 and SIN3A_PAH3-StrepII. ARID1A-V5 was immunoprecipitated from insect cell lysates. IgG was used as a negative control. Beads were then incubated with cell lysate from insect cells expressing SIN3A_PAH3-StrepII. Co-immunoprecipitation was assessed with anti-V5 and anti-StrepII antibodies to detect ARID1A and SIN3A_PAH3 respectively. KDM5A-StrepII was used as a positive control. Lanes labelled with X are irrelevant for this work.

    Article Snippet: Codon-optimised human SIN3A (residues 449-1086) fused to StrepII tag and ARID1A-V5 (from Addgene plasmid #39311) cDNAs for insect cell expression were synthesised and subcloned into the pFastBac1 vector (GenScript).

    Techniques: Binding Assay, Peptide Microarray, Immunoprecipitation, In Vitro, Recombinant, Negative Control, Incubation, Expressing, Positive Control

    miR-663a is induced in esophageal cancer cells upon ARID1A depletion. (A) Bioinformatics analysis showed 14 differentially expressed miRs between esophageal cancer and adjacent normal tissues based on GEO datasets ( GSE157805 and GSE145198 ). (B) The protein expression of ARID1A in esophageal cancer cells transfected with shCtrl or ARID1A-targeting shRNAs was measured by Western blot analysis. GAPDH was used as the loading control. (C) Measurement of miR-663a levels in esophageal cancer cells transfected with indicated shRNAs. ***, P<0.001 vs . shCtrl. (D) The expression level of miR-663a in 50 pairs of esophageal cancer and adjacent normal tissues measured by quantitative real-time PCR analysis. (E) The correlation between the miR-663a and ARID1A mRNA expression levels in the 50 cases of esophageal cancer tissues. (F) Overall survival analysis in esophageal cancer patients according to the miR-663a expression level using the data from Kaplan-Meier plotter. Data in parentheses are 95% confidence interval. GEO, Gene Expression Omnibus; HR, hazard ratio; miR, microRNA; PCR, polymerase chain reaction; shCtrl, control shRNA; shRNA, short hairpin RNA.

    Journal: Translational Cancer Research

    Article Title: MicroRNA-663a upregulation upon ARID1A depletion promotes the growth and migration of esophageal cancer cells by targeting FKBP8

    doi: 10.21037/tcr-2025-1457

    Figure Lengend Snippet: miR-663a is induced in esophageal cancer cells upon ARID1A depletion. (A) Bioinformatics analysis showed 14 differentially expressed miRs between esophageal cancer and adjacent normal tissues based on GEO datasets ( GSE157805 and GSE145198 ). (B) The protein expression of ARID1A in esophageal cancer cells transfected with shCtrl or ARID1A-targeting shRNAs was measured by Western blot analysis. GAPDH was used as the loading control. (C) Measurement of miR-663a levels in esophageal cancer cells transfected with indicated shRNAs. ***, P<0.001 vs . shCtrl. (D) The expression level of miR-663a in 50 pairs of esophageal cancer and adjacent normal tissues measured by quantitative real-time PCR analysis. (E) The correlation between the miR-663a and ARID1A mRNA expression levels in the 50 cases of esophageal cancer tissues. (F) Overall survival analysis in esophageal cancer patients according to the miR-663a expression level using the data from Kaplan-Meier plotter. Data in parentheses are 95% confidence interval. GEO, Gene Expression Omnibus; HR, hazard ratio; miR, microRNA; PCR, polymerase chain reaction; shCtrl, control shRNA; shRNA, short hairpin RNA.

    Article Snippet: After blocking with 5% skimmed milk, the membranes were incubated with the primary antibodies against ARID1A (1:800; Cell Signaling Technology, Danvers, MA, USA), FKBP8 (1:800; Cell Signaling Technology), SIRT6 (1:800; Cell Signaling Technology), and GAPDH (1:5,000; Cell Signaling Technology) at 4 °C overnight.

    Techniques: Expressing, Transfection, Western Blot, Control, Real-time Polymerase Chain Reaction, Gene Expression, Polymerase Chain Reaction, shRNA