hdac 1 Search Results


gene exp hdac1 mm02745760 g1  (Thermo Fisher)
93
Thermo Fisher gene exp hdac1 mm02745760 g1
Correlations in the thalamus region of 5mC and 5hmC with the expression levels of some genes involved in epigenetic regulation. 5hmC positively correlated with ( a ) Dnmt1 , ( b ) Dnmt3a , ( c ) Tet1 , ( d ) Tet2 , and ( e ) <t>Hdac1</t> in Tg338 mice, and 5mC ( f ) and 5hmC ( g ) negatively correlated with HDAC2 in sheep.
Gene Exp Hdac1 Mm02745760 G1, supplied by Thermo Fisher, 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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short hairpin sh ‑hdac1  (OriGene)
91
OriGene short hairpin sh ‑hdac1
Correlations in the thalamus region of 5mC and 5hmC with the expression levels of some genes involved in epigenetic regulation. 5hmC positively correlated with ( a ) Dnmt1 , ( b ) Dnmt3a , ( c ) Tet1 , ( d ) Tet2 , and ( e ) <t>Hdac1</t> in Tg338 mice, and 5mC ( f ) and 5hmC ( g ) negatively correlated with HDAC2 in sheep.
Short Hairpin Sh ‑Hdac1, supplied by OriGene, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hdac1  (Cell Signaling Technology Inc)
97
Cell Signaling Technology Inc hdac1
Figure 8. ARID1A interacts with <t>HDAC1</t> through its C-terminal domain. (A) Silver-stained gel shows differential bands between control and ARID1A-overexpressing samples. (B) HEK293T cells were transfected with ARID1A-Flag and HDAC1-HA, and their interaction is examined by co-IP. (C) Interaction between ARID1A and HDAC1 is examined by GST pull-down. (D) The interaction between endogenous ARID1A and HDAC1 is examined by co-IP with HDAC1 antibody in HEK293T and SNU-398 cells. (E) The semi-exogenous interaction between ARID1A and HDAC1 is examined by co-IP with Flag antibody or HDAC1 antibody in HEK293T cells transfected with ARID1A-Flag. (F) Localization of ARID1A and HDAC1 proteins in YY-8103 cells is examined by immunofluorescence assay. Scale bar: 25 mm. (G) The schematic diagram of full-length ARID1A and 5 truncated mutants. (H) Interactions between different ARID1A mutants with HDAC1 in HEK293T cells are examined by co-IP with HA antibody. The arrows indicate exogenous ARID1A with Flag tag. (I) Interactions between different mutants of ARID1A and HDAC1 in PVTT cells are examined by co-IP with Flag antibody. The arrows indicate exogenous Flag-tagged ARID1A. DEL,deletion; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.
Hdac1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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complex with hsp70  (BPS Bioscience)
95
BPS Bioscience complex with hsp70
Figure 8. ARID1A interacts with <t>HDAC1</t> through its C-terminal domain. (A) Silver-stained gel shows differential bands between control and ARID1A-overexpressing samples. (B) HEK293T cells were transfected with ARID1A-Flag and HDAC1-HA, and their interaction is examined by co-IP. (C) Interaction between ARID1A and HDAC1 is examined by GST pull-down. (D) The interaction between endogenous ARID1A and HDAC1 is examined by co-IP with HDAC1 antibody in HEK293T and SNU-398 cells. (E) The semi-exogenous interaction between ARID1A and HDAC1 is examined by co-IP with Flag antibody or HDAC1 antibody in HEK293T cells transfected with ARID1A-Flag. (F) Localization of ARID1A and HDAC1 proteins in YY-8103 cells is examined by immunofluorescence assay. Scale bar: 25 mm. (G) The schematic diagram of full-length ARID1A and 5 truncated mutants. (H) Interactions between different ARID1A mutants with HDAC1 in HEK293T cells are examined by co-IP with HA antibody. The arrows indicate exogenous ARID1A with Flag tag. (I) Interactions between different mutants of ARID1A and HDAC1 in PVTT cells are examined by co-IP with Flag antibody. The arrows indicate exogenous Flag-tagged ARID1A. DEL,deletion; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.
Complex With Hsp70, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hdac1  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Hdac1, supplied by Santa Cruz Biotechnology, 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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anti hdac1  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc anti hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Anti Hdac1, supplied by Cell Signaling Technology Inc, 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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pcdna3 1 hdac1  (Addgene inc)
93
Addgene inc pcdna3 1 hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Pcdna3 1 Hdac1, supplied by Addgene inc, 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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lactate dehydrogenase a  (Biorbyt)
93
Biorbyt lactate dehydrogenase a
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Lactate Dehydrogenase A, supplied by Biorbyt, 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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hdac1 sirna knockdown  (OriGene)
90
OriGene hdac1 sirna knockdown
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Hdac1 Sirna Knockdown, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti hdac1  (Bethyl)
93
Bethyl anti hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Anti Hdac1, supplied by Bethyl, 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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hdac1  (Proteintech)
96
Proteintech hdac1
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Hdac1, supplied by Proteintech, 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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kinetic hdac1 assay kit  (BPS Bioscience)
93
BPS Bioscience kinetic hdac1 assay kit
Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, <t>HDAC1,</t> HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005
Kinetic Hdac1 Assay Kit, supplied by BPS Bioscience, 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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Image Search Results


Correlations in the thalamus region of 5mC and 5hmC with the expression levels of some genes involved in epigenetic regulation. 5hmC positively correlated with ( a ) Dnmt1 , ( b ) Dnmt3a , ( c ) Tet1 , ( d ) Tet2 , and ( e ) Hdac1 in Tg338 mice, and 5mC ( f ) and 5hmC ( g ) negatively correlated with HDAC2 in sheep.

Journal: International Journal of Molecular Sciences

Article Title: 5-Methylcytosine and 5-Hydroxymethylcytosine in Scrapie-Infected Sheep and Mouse Brain Tissues

doi: 10.3390/ijms24021621

Figure Lengend Snippet: Correlations in the thalamus region of 5mC and 5hmC with the expression levels of some genes involved in epigenetic regulation. 5hmC positively correlated with ( a ) Dnmt1 , ( b ) Dnmt3a , ( c ) Tet1 , ( d ) Tet2 , and ( e ) Hdac1 in Tg338 mice, and 5mC ( f ) and 5hmC ( g ) negatively correlated with HDAC2 in sheep.

Article Snippet: Hdac1 , Mm02745760_g1.

Techniques: Expressing

References of the probes used for the RT-qPCR TaqMan amplification assay in Tg338 mice. ID = identification of the commercial company (Thermo Fisher Scientific, Waltham, MA, USA).

Journal: International Journal of Molecular Sciences

Article Title: 5-Methylcytosine and 5-Hydroxymethylcytosine in Scrapie-Infected Sheep and Mouse Brain Tissues

doi: 10.3390/ijms24021621

Figure Lengend Snippet: References of the probes used for the RT-qPCR TaqMan amplification assay in Tg338 mice. ID = identification of the commercial company (Thermo Fisher Scientific, Waltham, MA, USA).

Article Snippet: Hdac1 , Mm02745760_g1.

Techniques: Amplification

Sequences of primers used in the RT-qPCR assay in sheep. Fw = Forward primer and Rv = Reverse primer.

Journal: International Journal of Molecular Sciences

Article Title: 5-Methylcytosine and 5-Hydroxymethylcytosine in Scrapie-Infected Sheep and Mouse Brain Tissues

doi: 10.3390/ijms24021621

Figure Lengend Snippet: Sequences of primers used in the RT-qPCR assay in sheep. Fw = Forward primer and Rv = Reverse primer.

Article Snippet: Hdac1 , Mm02745760_g1.

Techniques:

Figure 8. ARID1A interacts with HDAC1 through its C-terminal domain. (A) Silver-stained gel shows differential bands between control and ARID1A-overexpressing samples. (B) HEK293T cells were transfected with ARID1A-Flag and HDAC1-HA, and their interaction is examined by co-IP. (C) Interaction between ARID1A and HDAC1 is examined by GST pull-down. (D) The interaction between endogenous ARID1A and HDAC1 is examined by co-IP with HDAC1 antibody in HEK293T and SNU-398 cells. (E) The semi-exogenous interaction between ARID1A and HDAC1 is examined by co-IP with Flag antibody or HDAC1 antibody in HEK293T cells transfected with ARID1A-Flag. (F) Localization of ARID1A and HDAC1 proteins in YY-8103 cells is examined by immunofluorescence assay. Scale bar: 25 mm. (G) The schematic diagram of full-length ARID1A and 5 truncated mutants. (H) Interactions between different ARID1A mutants with HDAC1 in HEK293T cells are examined by co-IP with HA antibody. The arrows indicate exogenous ARID1A with Flag tag. (I) Interactions between different mutants of ARID1A and HDAC1 in PVTT cells are examined by co-IP with Flag antibody. The arrows indicate exogenous Flag-tagged ARID1A. DEL,deletion; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

Journal: Cellular and molecular gastroenterology and hepatology

Article Title: Targeting USP9X-AMPK Axis in ARID1A-Deficient Hepatocellular Carcinoma.

doi: 10.1016/j.jcmgh.2022.03.009

Figure Lengend Snippet: Figure 8. ARID1A interacts with HDAC1 through its C-terminal domain. (A) Silver-stained gel shows differential bands between control and ARID1A-overexpressing samples. (B) HEK293T cells were transfected with ARID1A-Flag and HDAC1-HA, and their interaction is examined by co-IP. (C) Interaction between ARID1A and HDAC1 is examined by GST pull-down. (D) The interaction between endogenous ARID1A and HDAC1 is examined by co-IP with HDAC1 antibody in HEK293T and SNU-398 cells. (E) The semi-exogenous interaction between ARID1A and HDAC1 is examined by co-IP with Flag antibody or HDAC1 antibody in HEK293T cells transfected with ARID1A-Flag. (F) Localization of ARID1A and HDAC1 proteins in YY-8103 cells is examined by immunofluorescence assay. Scale bar: 25 mm. (G) The schematic diagram of full-length ARID1A and 5 truncated mutants. (H) Interactions between different ARID1A mutants with HDAC1 in HEK293T cells are examined by co-IP with HA antibody. The arrows indicate exogenous ARID1A with Flag tag. (I) Interactions between different mutants of ARID1A and HDAC1 in PVTT cells are examined by co-IP with Flag antibody. The arrows indicate exogenous Flag-tagged ARID1A. DEL,deletion; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

Article Snippet: Antibodies against acetyl–histone H3 (Lys9) (9649), acetyl–histone H3 (Lys9) (8173), ULK1 (8054), phospho-ULK1 (Ser317) (12753), phospho-ULK1 (Ser555) (5869), phospho-ULK1 (Ser757) (6888), acetyl-CoA carboxylase (3676), phospho-acetyl-CoA carboxylase (Ser79) (11818), AMPKa (2532), phosphoAMPKa (Thr172) (2535), LC3B (3868), and HDAC1 (34589) were purchased from Cell Signaling Technology (Danvers, MA); antibodies against PRKAA1 (10929), PRKAA2 (18167), USP9X (55054), glyceraldehyde-3-phosphate dehydrogenase (10494), and liver kinase B1 (10746) were purchased from Proteintech (Rosemont, IL); antibodies against ARID1A (sc-32761), a-tubulin (sc-32293), b-actin (sc-47778), ubiquitin (sc-8017), and c-myc (sc-764) were purchased from Santa Cruz Biotechnology (Dallas, Texas); and antibodies against Flag and HA were purchased from Sigma-Aldrich (St. Louis, MO).

Techniques: Staining, Control, Transfection, Co-Immunoprecipitation Assay, FLAG-tag

Figure 9. ARID1A regulates the promoter activity of USP9X via HDAC1. (A) Data from the Catalogue of Somatic Mutations in Cancer shows that 1989* is the most frequent mutation of ARID1A. (B) Interaction between ARID1A-WT or ARID1A-1989* mutation with HDAC1. (C) Influence of ARID1A-WT or ARID1A-1989* mutation on the ubiquitination of PRKAA2. (D) Influence of ARID1A-WT or ARID1A-1989* mutation on the promoter activity of USP9X. The promoter activity of USP9X in (E) HEK293T cells overexpressing ARID1A or HDAC1 (OE) or in (F) ARID1A knockout Huh7 and YY-8103 cells is examined by luciferase reporter assay. (G) Influence of ARID1A-WT or ARID1A-1989* mutation on the expression of USP9X and PRKAA2. CTRL, control; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. **P<0.01, ***P<0.001, ns, not significant.

Journal: Cellular and molecular gastroenterology and hepatology

Article Title: Targeting USP9X-AMPK Axis in ARID1A-Deficient Hepatocellular Carcinoma.

doi: 10.1016/j.jcmgh.2022.03.009

Figure Lengend Snippet: Figure 9. ARID1A regulates the promoter activity of USP9X via HDAC1. (A) Data from the Catalogue of Somatic Mutations in Cancer shows that 1989* is the most frequent mutation of ARID1A. (B) Interaction between ARID1A-WT or ARID1A-1989* mutation with HDAC1. (C) Influence of ARID1A-WT or ARID1A-1989* mutation on the ubiquitination of PRKAA2. (D) Influence of ARID1A-WT or ARID1A-1989* mutation on the promoter activity of USP9X. The promoter activity of USP9X in (E) HEK293T cells overexpressing ARID1A or HDAC1 (OE) or in (F) ARID1A knockout Huh7 and YY-8103 cells is examined by luciferase reporter assay. (G) Influence of ARID1A-WT or ARID1A-1989* mutation on the expression of USP9X and PRKAA2. CTRL, control; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. **P<0.01, ***P<0.001, ns, not significant.

Article Snippet: Antibodies against acetyl–histone H3 (Lys9) (9649), acetyl–histone H3 (Lys9) (8173), ULK1 (8054), phospho-ULK1 (Ser317) (12753), phospho-ULK1 (Ser555) (5869), phospho-ULK1 (Ser757) (6888), acetyl-CoA carboxylase (3676), phospho-acetyl-CoA carboxylase (Ser79) (11818), AMPKa (2532), phosphoAMPKa (Thr172) (2535), LC3B (3868), and HDAC1 (34589) were purchased from Cell Signaling Technology (Danvers, MA); antibodies against PRKAA1 (10929), PRKAA2 (18167), USP9X (55054), glyceraldehyde-3-phosphate dehydrogenase (10494), and liver kinase B1 (10746) were purchased from Proteintech (Rosemont, IL); antibodies against ARID1A (sc-32761), a-tubulin (sc-32293), b-actin (sc-47778), ubiquitin (sc-8017), and c-myc (sc-764) were purchased from Santa Cruz Biotechnology (Dallas, Texas); and antibodies against Flag and HA were purchased from Sigma-Aldrich (St. Louis, MO).

Techniques: Activity Assay, Mutagenesis, Ubiquitin Proteomics, Knock-Out, Luciferase, Reporter Assay, Expressing, Control

Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, HDAC1, HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005

Journal: PloS one

Article Title: Histone deacetylases and NF-kB signaling coordinate expression of CX3CL1 in epithelial cells in response to microbial challenge by suppressing miR-424 and miR-503.

doi: 10.1371/journal.pone.0065153

Figure Lengend Snippet: Figure 5. C. parvum infection increases recruitment of NF-kB p50 and HDAC complex and decreases H3 acetylation associated with the NF-kB promoter region of the mir-424-503 gene promoter. A, Two potential binding sites for NF-kB are identified in the promoter of the mir-424-503 gene. Increased promoter recruitment of p50, but not p65, and HDAC complex to the NF-kB associated site A region of mir-424-503 gene was found in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. Promoter recruitment of p65, p50, HDAC1, HDAC2 and Sirt1 to the mir-424-503 gene was assessed by ChIP analysis using primers covering the NF-kB-binding site A and site B regions within the promoter. The results were analyzed by real-time PCR and shown as the percentage of input. Data are averages of three independent experiments. The start of pri-miR-424-503 was indicated as +1. B, Representative PCR gels for p50 were shown as an example. C, Decrease of H3 acetylation in the NF-kB-associated region in the mir-424-503 gene promoter in cells following C. parvum infection. H69 cells were exposed to C. parvum infection for 8 h. H3 acetylation associated with the NF-kB promoter site A region was assessed by ChIP analysis, using an antibody to H3Ac and primers covering the NF-kB-binding site A region within its promoter. *, p,0.05 ANOVA vs. the non-infected control. doi:10.1371/journal.pone.0065153.g005

Article Snippet: In brief, 106 H69 cells were exposed to C. parvum infection for 8 h. The chromatin fraction was immunoprecipitated overnight at 4uC using antibodies to p65 (Upstate Biotechnologies), p50 (Santa Cruz), HDAC1 (Santa Cruz), HDAC2 (Santa Cruz), Sirt1 (Santa Cruz), C/EBPb (Abcam).

Techniques: Infection, Binding Assay, Real-time Polymerase Chain Reaction, Control