hdac 7 33418 Search Results


hdac7  (Cell Signaling Technology Inc)
94
Cell Signaling Technology Inc hdac7
a HADC7 overexpression reduced ALKBH5 acetylation at K235. HeLa cells were transfected with the indicated plasmids together with the ALKBH5-HA vector; ALKBH5-HA was IPed using anti-HA antibody, and K235 acetylation in the IPed ALKBH5-HA was determined using the anti-pan acetylated lysine antibody. b , c ALKBH5 interacted with <t>HDAC7.</t> The ALKBH5-HA and HDAC7-FLAG plasmids were cotransfected into HeLa cells, and the HDAC7-FLAG ( b ) and ALKBH5-HA ( c ) complexes were co-IPed using anti-FLAG and anti-HA antibodies, respectively. ALKBH5-HA and HDAC7-FLAG were detected. d Silencing of HDAC7 increased the endogenous K235 acetylation of ALKBH5. HeLa cells were transfected with anti-HDAC7 siRNAs, and K235 acetylation was determined. e HDAC7 overexpression decreased the endogenous K235 acetylation of ALKBH5. HeLa cells were transfected with the indicated dose of HDAC7 plasmid, and K235 acetylation was determined. f HDAC7 directly deacetylated ALKBH5 at K235 in a dose-dependent manner in the in vitro deacetylation reaction. Immunopurified wild-type ALKBH5 containing K235-acetylated ALKBH5 stimulated by KAT8 overexpression was incubated with the indicated dose of immunopurified HADC7, and ALKBH5 acetylation at K235 was determined using anti-Ac K235 and anti-pan acetylated lysine antibodies. Source data are provided as a Source Data file.
Hdac7, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/hdac7/product/Cell Signaling Technology Inc
Average 94 stars, based on 1 article reviews
hdac7 - by Bioz Stars, 2026-02
94/100 stars
  Buy from Supplier

Image Search Results


a HADC7 overexpression reduced ALKBH5 acetylation at K235. HeLa cells were transfected with the indicated plasmids together with the ALKBH5-HA vector; ALKBH5-HA was IPed using anti-HA antibody, and K235 acetylation in the IPed ALKBH5-HA was determined using the anti-pan acetylated lysine antibody. b , c ALKBH5 interacted with HDAC7. The ALKBH5-HA and HDAC7-FLAG plasmids were cotransfected into HeLa cells, and the HDAC7-FLAG ( b ) and ALKBH5-HA ( c ) complexes were co-IPed using anti-FLAG and anti-HA antibodies, respectively. ALKBH5-HA and HDAC7-FLAG were detected. d Silencing of HDAC7 increased the endogenous K235 acetylation of ALKBH5. HeLa cells were transfected with anti-HDAC7 siRNAs, and K235 acetylation was determined. e HDAC7 overexpression decreased the endogenous K235 acetylation of ALKBH5. HeLa cells were transfected with the indicated dose of HDAC7 plasmid, and K235 acetylation was determined. f HDAC7 directly deacetylated ALKBH5 at K235 in a dose-dependent manner in the in vitro deacetylation reaction. Immunopurified wild-type ALKBH5 containing K235-acetylated ALKBH5 stimulated by KAT8 overexpression was incubated with the indicated dose of immunopurified HADC7, and ALKBH5 acetylation at K235 was determined using anti-Ac K235 and anti-pan acetylated lysine antibodies. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: K235 acetylation couples with PSPC1 to regulate the m 6 A demethylation activity of ALKBH5 and tumorigenesis

doi: 10.1038/s41467-023-39414-4

Figure Lengend Snippet: a HADC7 overexpression reduced ALKBH5 acetylation at K235. HeLa cells were transfected with the indicated plasmids together with the ALKBH5-HA vector; ALKBH5-HA was IPed using anti-HA antibody, and K235 acetylation in the IPed ALKBH5-HA was determined using the anti-pan acetylated lysine antibody. b , c ALKBH5 interacted with HDAC7. The ALKBH5-HA and HDAC7-FLAG plasmids were cotransfected into HeLa cells, and the HDAC7-FLAG ( b ) and ALKBH5-HA ( c ) complexes were co-IPed using anti-FLAG and anti-HA antibodies, respectively. ALKBH5-HA and HDAC7-FLAG were detected. d Silencing of HDAC7 increased the endogenous K235 acetylation of ALKBH5. HeLa cells were transfected with anti-HDAC7 siRNAs, and K235 acetylation was determined. e HDAC7 overexpression decreased the endogenous K235 acetylation of ALKBH5. HeLa cells were transfected with the indicated dose of HDAC7 plasmid, and K235 acetylation was determined. f HDAC7 directly deacetylated ALKBH5 at K235 in a dose-dependent manner in the in vitro deacetylation reaction. Immunopurified wild-type ALKBH5 containing K235-acetylated ALKBH5 stimulated by KAT8 overexpression was incubated with the indicated dose of immunopurified HADC7, and ALKBH5 acetylation at K235 was determined using anti-Ac K235 and anti-pan acetylated lysine antibodies. Source data are provided as a Source Data file.

Article Snippet: The indicated proteins were detected using the following antibodies: anti-Ac-K235 (developed in our lab, 1:500), acetylated lysine (Pan-Ac) (9814, CST, RRID:AB_10544700, 1:1000), ALKBH5 (703570, Thermo Fisher Scientific, RRID: AB_2762417, 1:1000), FLAG (M185-3 L, MBL, RRID: AB_11123930, 1:2000), HA (561, MBL, RRID: AB_591839, 1:2000), V5 (66007-1-Ig, Proteintech, RRID: AB_2734694, 1:1000), KAT8 (ab200660, Abcam, 1:1000), HDAC7 (33418, CST, RRID: AB_2716756, 1:1000), PSPC1 (16714-1-AP, Proteintech, RRID: AB_2878302, 1:1000), m 6 A (for dot blotting, ABE572, Merck Millipore, 1:1000), m 6 A (for m 6 A-seq, 202003, Synaptic systems, PRID: AB_2279214, 1:500), GST (2625 S, CST, RRID: AB_490796, 1:1000), NONO (11058-1-AP, Proteintech, RRID: AB_2152167, 1:1000), SFPQ (15585-1-AP, Proteintech, RRID: AB_10697653, 1:1000), FOXM1 (13147-1-AP, Proteintech, RRID:AB_2106213, 1:1000), SMAD7 (25840-1-AP, Proteintech, RRID:AB_2848137, 1:1000), TACC3 (25697-1-AP, Proteintech, RRID:AB_2880199, 1:1000), c-myc (13987 S, CST, RRID:AB_2631168, 1:1000) and β-actin (60008-1-Ig, Proteintech, RRID: AB_2289225, 1:5000).

Techniques: Over Expression, Transfection, Plasmid Preparation, In Vitro, Incubation

a , b K235 acetylation of ALKBH5 decreased the cellular mRNA m 6 A levels. The wild-type ALKBH5 and its mutant K235R and K235Q plasmids were transfected into ALKBH5 KO HeLa cells, and the cellular mRNA m 6 A level was determined by dot blotting ( a ) and quantified by LC‒MS/MS analysis ( b ) (n = 3, two-tailed unpaired Student’s t test, mean ± SD). c , d Wild-type ALKBH5, but not the K235R mutant, directly demethylated m 6 A in the m 6 A-RNA oligos in the in vitro demethylation reaction. Immunopurified wild-type ALKBH5 and its mutant K235R ( c ) or recombinant wild-type ALKBH5 and its mutant K235R ( d ) were incubated with m 6 A RNA oligos; the m 6 A level was determined by dot blotting or LC‒MS/MS assays. e Cumulative distribution curve for the m 6 A peak abundance in NC, WT and K235R cells. f Distribution of m 6 A peaks in the 5′ UTR, CDS, stop codon and 3′ UTR in NC, WT and K235R cells. g Top consensus motif identified by HOMER with m 6 A peaks in NC, WT and K235R cells. h The indicated ALKBH5 vectors together with the KAT8 plasmid were cotransfected into ALKBH5 KO HeLa cells, and the cellular RNA m 6 A level was determined. i , j Recombinant wild-type ALKBH5 or its K235R mutant was incubated with m 6 A RNA oligos after recombinant wild-type ALKBH5 or its K235R mutant was treated with immunopurified KAT8 ( i ) or immunopurified HDAC7 ( j ), and the m 6 A level was determined. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: K235 acetylation couples with PSPC1 to regulate the m 6 A demethylation activity of ALKBH5 and tumorigenesis

doi: 10.1038/s41467-023-39414-4

Figure Lengend Snippet: a , b K235 acetylation of ALKBH5 decreased the cellular mRNA m 6 A levels. The wild-type ALKBH5 and its mutant K235R and K235Q plasmids were transfected into ALKBH5 KO HeLa cells, and the cellular mRNA m 6 A level was determined by dot blotting ( a ) and quantified by LC‒MS/MS analysis ( b ) (n = 3, two-tailed unpaired Student’s t test, mean ± SD). c , d Wild-type ALKBH5, but not the K235R mutant, directly demethylated m 6 A in the m 6 A-RNA oligos in the in vitro demethylation reaction. Immunopurified wild-type ALKBH5 and its mutant K235R ( c ) or recombinant wild-type ALKBH5 and its mutant K235R ( d ) were incubated with m 6 A RNA oligos; the m 6 A level was determined by dot blotting or LC‒MS/MS assays. e Cumulative distribution curve for the m 6 A peak abundance in NC, WT and K235R cells. f Distribution of m 6 A peaks in the 5′ UTR, CDS, stop codon and 3′ UTR in NC, WT and K235R cells. g Top consensus motif identified by HOMER with m 6 A peaks in NC, WT and K235R cells. h The indicated ALKBH5 vectors together with the KAT8 plasmid were cotransfected into ALKBH5 KO HeLa cells, and the cellular RNA m 6 A level was determined. i , j Recombinant wild-type ALKBH5 or its K235R mutant was incubated with m 6 A RNA oligos after recombinant wild-type ALKBH5 or its K235R mutant was treated with immunopurified KAT8 ( i ) or immunopurified HDAC7 ( j ), and the m 6 A level was determined. Source data are provided as a Source Data file.

Article Snippet: The indicated proteins were detected using the following antibodies: anti-Ac-K235 (developed in our lab, 1:500), acetylated lysine (Pan-Ac) (9814, CST, RRID:AB_10544700, 1:1000), ALKBH5 (703570, Thermo Fisher Scientific, RRID: AB_2762417, 1:1000), FLAG (M185-3 L, MBL, RRID: AB_11123930, 1:2000), HA (561, MBL, RRID: AB_591839, 1:2000), V5 (66007-1-Ig, Proteintech, RRID: AB_2734694, 1:1000), KAT8 (ab200660, Abcam, 1:1000), HDAC7 (33418, CST, RRID: AB_2716756, 1:1000), PSPC1 (16714-1-AP, Proteintech, RRID: AB_2878302, 1:1000), m 6 A (for dot blotting, ABE572, Merck Millipore, 1:1000), m 6 A (for m 6 A-seq, 202003, Synaptic systems, PRID: AB_2279214, 1:500), GST (2625 S, CST, RRID: AB_490796, 1:1000), NONO (11058-1-AP, Proteintech, RRID: AB_2152167, 1:1000), SFPQ (15585-1-AP, Proteintech, RRID: AB_10697653, 1:1000), FOXM1 (13147-1-AP, Proteintech, RRID:AB_2106213, 1:1000), SMAD7 (25840-1-AP, Proteintech, RRID:AB_2848137, 1:1000), TACC3 (25697-1-AP, Proteintech, RRID:AB_2880199, 1:1000), c-myc (13987 S, CST, RRID:AB_2631168, 1:1000) and β-actin (60008-1-Ig, Proteintech, RRID: AB_2289225, 1:5000).

Techniques: Mutagenesis, Transfection, Two Tailed Test, In Vitro, Recombinant, Incubation, Plasmid Preparation

a The in vitro binding of wild-type ALKBH5 and its mutant K235R to m 6 A-unmethylated or methylated RNA oligos was investigated in ALKBH5 KO HeLa cells stably re-expressing wild-type ALKBH5 or its mutant K235R using RNA pulldown assays. b The in vitro binding of recombinant wild-type ALKBH5 and its mutant K235R to m 6 A-unmethylated or methylated RNA oligos was investigated. c , d The in vitro binding of recombinant wild-type ALKBH5 and its mutant K235R to m 6 A-unmethylated or methylated RNA oligos was investigated after the recombinant wild-type ALKBH5 or its mutant K235R were treated by immunopurified KAT8 ( c ) or by immunopurified HDAC7 ( d ). Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: K235 acetylation couples with PSPC1 to regulate the m 6 A demethylation activity of ALKBH5 and tumorigenesis

doi: 10.1038/s41467-023-39414-4

Figure Lengend Snippet: a The in vitro binding of wild-type ALKBH5 and its mutant K235R to m 6 A-unmethylated or methylated RNA oligos was investigated in ALKBH5 KO HeLa cells stably re-expressing wild-type ALKBH5 or its mutant K235R using RNA pulldown assays. b The in vitro binding of recombinant wild-type ALKBH5 and its mutant K235R to m 6 A-unmethylated or methylated RNA oligos was investigated. c , d The in vitro binding of recombinant wild-type ALKBH5 and its mutant K235R to m 6 A-unmethylated or methylated RNA oligos was investigated after the recombinant wild-type ALKBH5 or its mutant K235R were treated by immunopurified KAT8 ( c ) or by immunopurified HDAC7 ( d ). Source data are provided as a Source Data file.

Article Snippet: The indicated proteins were detected using the following antibodies: anti-Ac-K235 (developed in our lab, 1:500), acetylated lysine (Pan-Ac) (9814, CST, RRID:AB_10544700, 1:1000), ALKBH5 (703570, Thermo Fisher Scientific, RRID: AB_2762417, 1:1000), FLAG (M185-3 L, MBL, RRID: AB_11123930, 1:2000), HA (561, MBL, RRID: AB_591839, 1:2000), V5 (66007-1-Ig, Proteintech, RRID: AB_2734694, 1:1000), KAT8 (ab200660, Abcam, 1:1000), HDAC7 (33418, CST, RRID: AB_2716756, 1:1000), PSPC1 (16714-1-AP, Proteintech, RRID: AB_2878302, 1:1000), m 6 A (for dot blotting, ABE572, Merck Millipore, 1:1000), m 6 A (for m 6 A-seq, 202003, Synaptic systems, PRID: AB_2279214, 1:500), GST (2625 S, CST, RRID: AB_490796, 1:1000), NONO (11058-1-AP, Proteintech, RRID: AB_2152167, 1:1000), SFPQ (15585-1-AP, Proteintech, RRID: AB_10697653, 1:1000), FOXM1 (13147-1-AP, Proteintech, RRID:AB_2106213, 1:1000), SMAD7 (25840-1-AP, Proteintech, RRID:AB_2848137, 1:1000), TACC3 (25697-1-AP, Proteintech, RRID:AB_2880199, 1:1000), c-myc (13987 S, CST, RRID:AB_2631168, 1:1000) and β-actin (60008-1-Ig, Proteintech, RRID: AB_2289225, 1:5000).

Techniques: In Vitro, Binding Assay, Mutagenesis, Methylation, Stable Transfection, Expressing, Recombinant

a – d The ALKBH5 protein level ( a ); cell proliferation ( b ) ( n = 3); and migration, invasion ( c ) ( n = 5), and colony formation ( d ) ( n = 3) were determined in ALKBH5 KO HeLa cells stably re-expressing wild-type ALKBH5 or its mutants K235R or K235Q. e The in vivo tumorigenesis of the indicated ALKBH5 KO HeLa cells stably re-expressing wild-type ALKBH5 or its mutant K235R was examined, and the weights of the xenograft tumors were analyzed (n = 10 mice per group). f The levels of the indicated proteins were determined in ALKBH5 KO HeLa cells stably reexpressing wild-type ALKBH5 or its mutant K235R. g K235 acetylation and ALKBH5, KAT8, and HDAC7 levels were determined in ten pairs of fresh liver and gastric cancer tissues and their corresponding nontumor tissues. h A regulatory model of ALKBH5 m 6 A demethylation activity is elucidated in which K235-acetylated ALKBH5 primarily functions as the catalytic core, and PSPC1 serves as an RNA-binding platform to recruit and facilitate the recognition of RNA m 6 A by ALKBH5 by interacting with K235-acetylated ALKBH5, thereby promoting RNA m 6 A erasure. Two-tailed unpaired Student’s t test in c – e and two-way ANOVA in ( b ). The data are represented as the mean ± SD. ** p < 0.01, *** p < 0.001, ns indicates no significance. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: K235 acetylation couples with PSPC1 to regulate the m 6 A demethylation activity of ALKBH5 and tumorigenesis

doi: 10.1038/s41467-023-39414-4

Figure Lengend Snippet: a – d The ALKBH5 protein level ( a ); cell proliferation ( b ) ( n = 3); and migration, invasion ( c ) ( n = 5), and colony formation ( d ) ( n = 3) were determined in ALKBH5 KO HeLa cells stably re-expressing wild-type ALKBH5 or its mutants K235R or K235Q. e The in vivo tumorigenesis of the indicated ALKBH5 KO HeLa cells stably re-expressing wild-type ALKBH5 or its mutant K235R was examined, and the weights of the xenograft tumors were analyzed (n = 10 mice per group). f The levels of the indicated proteins were determined in ALKBH5 KO HeLa cells stably reexpressing wild-type ALKBH5 or its mutant K235R. g K235 acetylation and ALKBH5, KAT8, and HDAC7 levels were determined in ten pairs of fresh liver and gastric cancer tissues and their corresponding nontumor tissues. h A regulatory model of ALKBH5 m 6 A demethylation activity is elucidated in which K235-acetylated ALKBH5 primarily functions as the catalytic core, and PSPC1 serves as an RNA-binding platform to recruit and facilitate the recognition of RNA m 6 A by ALKBH5 by interacting with K235-acetylated ALKBH5, thereby promoting RNA m 6 A erasure. Two-tailed unpaired Student’s t test in c – e and two-way ANOVA in ( b ). The data are represented as the mean ± SD. ** p < 0.01, *** p < 0.001, ns indicates no significance. Source data are provided as a Source Data file.

Article Snippet: The indicated proteins were detected using the following antibodies: anti-Ac-K235 (developed in our lab, 1:500), acetylated lysine (Pan-Ac) (9814, CST, RRID:AB_10544700, 1:1000), ALKBH5 (703570, Thermo Fisher Scientific, RRID: AB_2762417, 1:1000), FLAG (M185-3 L, MBL, RRID: AB_11123930, 1:2000), HA (561, MBL, RRID: AB_591839, 1:2000), V5 (66007-1-Ig, Proteintech, RRID: AB_2734694, 1:1000), KAT8 (ab200660, Abcam, 1:1000), HDAC7 (33418, CST, RRID: AB_2716756, 1:1000), PSPC1 (16714-1-AP, Proteintech, RRID: AB_2878302, 1:1000), m 6 A (for dot blotting, ABE572, Merck Millipore, 1:1000), m 6 A (for m 6 A-seq, 202003, Synaptic systems, PRID: AB_2279214, 1:500), GST (2625 S, CST, RRID: AB_490796, 1:1000), NONO (11058-1-AP, Proteintech, RRID: AB_2152167, 1:1000), SFPQ (15585-1-AP, Proteintech, RRID: AB_10697653, 1:1000), FOXM1 (13147-1-AP, Proteintech, RRID:AB_2106213, 1:1000), SMAD7 (25840-1-AP, Proteintech, RRID:AB_2848137, 1:1000), TACC3 (25697-1-AP, Proteintech, RRID:AB_2880199, 1:1000), c-myc (13987 S, CST, RRID:AB_2631168, 1:1000) and β-actin (60008-1-Ig, Proteintech, RRID: AB_2289225, 1:5000).

Techniques: Migration, Stable Transfection, Expressing, In Vivo, Mutagenesis, Activity Assay, RNA Binding Assay, Two Tailed Test