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Hdac1

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HDAC1 is a histone deacetylase enzyme that removes acetyl groups from lysine residues on histone proteins, leading to transcriptional repression. It is involved in the regulation of gene expression and chromatin remodeling.

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Lab products found in correlation

Hdac2, by Cell Signaling Technology (39 mentions) Hdac3, by Cell Signaling Technology (25 mentions) Hdac4, by Cell Signaling Technology (16 mentions) β actin, by Merck Group (12 mentions) Hdac5, by Cell Signaling Technology (12 mentions) β actin, by Cell Signaling Technology (11 mentions) Gapdh, by Cell Signaling Technology (11 mentions) Hdac6, by Cell Signaling Technology (10 mentions) Cleaved caspase 3, by Cell Signaling Technology (7 mentions) Hdac7, by Cell Signaling Technology (6 mentions) P akt ser473, by Cell Signaling Technology (5 mentions) Acetyl histone h3, by Cell Signaling Technology (5 mentions) Hdac8, by Cell Signaling Technology (5 mentions) Histone h3, by Cell Signaling Technology (5 mentions) Erk1 2, by Cell Signaling Technology (5 mentions) Flag tag (flag), by Merck Group (4 mentions) Vimentin, by Cell Signaling Technology (4 mentions) Bcl 2, by Cell Signaling Technology (4 mentions) Survivin, by Cell Signaling Technology (4 mentions) Caspase 3, by Cell Signaling Technology (4 mentions)

Close spelling variants of this product

Anti-HDAC1 (52 citations) Anti-HDAC1 antibody (6 citations) HDAC1 antibody (4 citations) HDAC1 (10E2) (4 citations) Anti-HDAC1 (10E2, (3 citations) HDAC1/2 antibodies (3 citations) Mouse anti-HDAC1 (2 citations) Mouse monoclonal anti-HDAC1 antibody (10E2, (2 citations) Rabbit monoclonal anti-HDAC1 (2 citations) Rabbit anti-HDAC1 (2 citations)

114 protocols using hdac1

1

Isolation and Identification of FC from Ferula assafoetida

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FC (Figure 1A) was isolated and identified from Ferula assafoetida as previously described [12 (link)]. 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), Bcl-2, and β-actin were purchased from Sigma-Aldrich (Sigma-Aldrich, St. Louis, MO, USA). Also, specific antibodies for Cyclin D1, Cyclin E, Cyclin B1 were bought from Santa Cruz Biotechnology (Santa Cruz Biotechnology, Dallas, TX, USA). PARP, HDAC1, and HDAC2 were purchased from Cell Signaling (Cell signaling Technology, Danvers, MA, USA) for Western blot analysis.
Jung J.H., Park J.E., Sim D.Y., Im E., Park W.Y., Lee D., Shim B.S, & Kim S.H. (2019). Farnesiferol C Induces Apoptosis in Chronic Myelogenous Leukemia Cells as an Imatinib Sensitizer via Caspase Activation and HDAC (Histone Deacetylase) Inactivation. International Journal of Molecular Sciences, 20(22), 5535.
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2

Western Blot Analysis of Protein Signaling

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Total cellular protein was isolated from the cells after various treatments. For Western blots, a previously described procedure was applied [54 (link)]. The following primary antibodies were used: Acetyl Histone H3, HDAC1, HDAC8, PPARγ, cyclin D1, CDK6, p-Ser473 Akt, Akt, p-Ser2448 mTOR, mTOR, p-Ser139 H2AX, H2AX, Bax, Mcl-1, PARP, procaspase-8, cleaved caspase-9, LC3B, and Atg5 were purchased from Cell Signaling Technologies (Beverly, MA, USA); β-actin, Sigma-Aldrich (St. Louis, MO, USA). The secondary antibodies were purchased from Santa Cruz Biotechnology. The enhanced chemiluminescence (ECL) system for detection of immunoblotted proteins was from GE Healthcare Bioscience (Piscataway, NJ, USA). Then, the protein was visualized by FUSION SOLO S (VILBER, Deutschland, Germany).
Chiu C.F., Chin H.K., Huang W.J., Bai L.Y., Huang H.Y, & Weng J.R. (2019). Induction of Apoptosis and Autophagy in Breast Cancer Cells by a Novel HDAC8 Inhibitor. Biomolecules, 9(12), 824.
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3

Histone Acetylation and HDAC Profiling

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Histone preparations were made from young and aged mice BMSCs. Equal amounts of core histones were resolved by 15% SDS-PAGE, transferred onto PVDF membranes and probed with the following antibodies: acetylated H3K9/K14 (#9677, Cell Signaling Technology, Danvers, MA, USA), acetylated H4K12 (#13944, Cell Signaling Technology, Danvers, MA, USA), HDAC1 (#34589, Cell Signaling Technology, Danvers, MA, USA), HDAC3 (#85057, Cell Signaling Technology, Danvers, MA, USA), HDAC4 (MA5-15580, ThermoFisher scientific), HDAC5 (#98329, Cell Signaling Technology, Danvers, MA, USA), HDAC6 (PA1-41056, ThermoFisher scientific), total H3 (#4499, Cell Signaling Technology, Danvers, MA, USA), total H4 (#13919, Cell Signaling Technology, Danvers, MA, USA) and β-actin (#4970, Cell Signaling Technology, Danvers, MA, USA).
Ma C., Gao J., Liang J., Dai W., Wang Z., Xia M., Chen T., Huang S., Na J., Xu L., Feng S., Dai K, & Liu G. (2021). HDAC6 inactivates Runx2 promoter to block osteogenesis of bone marrow stromal cells in age-related bone loss of mice. Stem Cell Research & Therapy, 12, 484.
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4

Western Blot Analysis of Protein Complexes

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Western blot was performed according to the manufacturer’s protocol. Equal amounts of protein were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE) gels followed by transfer to PVDF membranes. Membranes were probed with primary antibodies overnight and then washed and incubated with horseradish peroxidase (HRP)-conjugated-secondary antibodies. Detection was performed by the enhanced chemical luminescence (ECL) method. The primary antibodies of NCOR2 (ab24551; 1:1000) was purchased from Abcam. CRBN (NBP1-91810; 1:1,000) antibody was purchased from Novus Biologicals. c-Myc (#5605; 1:1,000), IKAROS (#9034; 1:1,000), MTA1 (#5647; 1:1,000), MBD3 (#14540; 1:1,000), HDAC1 (#5356; 1:1,000), and HDAC2 (#5113; 1:1,000), antibodies were purchased from Cell Signaling Technology, Inc.
Mori T., Verma R., Nakamoto-Matsubara R., Siu K.T., Panaroni C., Fulzele K.S., Mukaihara K., Onyewadume C., Maebius A., Kato H., Wong L.P., Sadreyev R.I., Scadden D.T, & Raje N.S. (2021). Low NCOR2 levels in multiple myeloma patients drive multidrug resistance via MYC upregulation. Blood Cancer Journal, 11(12), 194.
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5

EVI1 Immunoprecipitation in Cultured Cortical Neurons

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Two-week-old cultured cortical neurons were incubated with TTX/APV for 1–2 h and harvested in ice-cold lysis buffer (PBS supplemented with 1% Triton X-100, 0.5% deoxycholate, 0.1% SDS and 1:300 protease inhibitor cocktail containing AEBSF, Aprotinin, Bedysyin, E-64, Leupeptin and Pepstatin A, Sigma) and rotated at 4 °C for 1 h. Following centrifugation of the lysates at 14,000g for 15 min, supernatants were incubated overnight on rotation at 4 °C with anti-EVI1 antibodies, (1 μg, Abcam) followed by the addition of 40 μl of 50% slurry of protein A-Sepharose beads (Santa Cruz Biotechnology). Immunoprecipitates were washed three times with lysis buffer and resuspended in 30 μl of 2 × Laemmli buffer and denatured on a 95 °C heat block for 10 min. Immunoprecipitates were analysed by western blotting. The full western blots are shown as Supplementary Figs 13–16.
The following antibodies were used for western blot: GFP (Mouse, 1:500, Abcam); GluA1C (Rabbit, 1:1,000; homemade) and GluA1N (Mouse, 1:1,000; Millipore), EV1 (Rabbit, 1:1,000, Abcam); PSD-95 (Mouse, 1:1,000; Thermo Fisher); HDAC1 (Rabbit, 1:1,000, Cell Signaling).
Hou Q., Ruan H., Gilbert J., Wang G., Ma Q., Yao W.D, & Man H.Y. (2015). MicroRNA miR124 is required for the expression of homeostatic synaptic plasticity. Nature Communications, 6, 10045.
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6

Nuclear and Cytosolic Fractionation of Rat Striatal Tissue

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The Nuclei Pure Prep Nuclei Isolation Kit (Sigma, St. Louis, MO) was used to prepare nuclear and cytosolic fractions from the rat tissue. The intact and lesioned striatal from rats injected with either GFP or GRK6 lentivirus and chronically treated with L-DOPA as described above were dissected and homogenized in 8 ml of Lysis buffer and the nuclei were separated from the cytosolic structured by differential centrifugation according to the manufacturer’s instructions. Final nuclei preparations were dissolved in 200 ml of Nuclei Storage buffer from the kit. Protein concentration in the samples was measured with Bradford reagent (Bio-Rad, Hercules, CA). Proteins from the nuclear and cytosolic fractions were precipitated with methanol and dissolved in in sodium dodecyl sulfate sample buffer at the final concentration of 0.5 mg/ml. ΔFosB was detected with rabbit polyclonal antibody (Cell Signaling Technology, cat.#9890, 1:1000) as described above. Lentivirally-delivered GFP and GFP-tagged GRK6 were detected with mouse monoclonal anti-GFP antibody (JL-8 Clontech, 1:500). Caspase-3 detected with rabbit polyclonal antibody (Cell Signaling Technology, cat.#9662, 1:1000) and histone deacetylase 1 (HDAC1, Cell Signaling Technology, cat.#2062, 1:1000) were used as markers of the cytosolic and nuclear fractions, respectively.
Ahmed M.R., Bychkov E., Kook S., Zurkovsky L., Dalby K.N, & Gurevich E.V. (2015). Overexpression of GRK6 rescues L-DOPA-induced signaling abnormalities in the dopamine-depleted striatum of hemiparkinsonian rats. Experimental neurology, 266, 42-54.
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7

Immunoblotting of HDAC Isoforms

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Immunoblotting was performed as previously described(16 (link)). Briefly, pediatric human and neonatal rat RV homogenates were prepared and concentrations quantified as above for HDAC catalytic activity assay. Proteins were resolved by SDS-PAGE, transferred to nitrocellulose membranes (BioRad) and probed with antibodies for HDAC1 (Cell Signaling Technology, 5356), HDAC2 (Cell Signaling Technology, 5113), HDAC3 (Cell Signaling Technology, 3949), HDAC4 (Cell Signaling Technology, 5392), HDAC5 (Cell Signaling Technology, 2082), HDAC6 (Santa Cruz Biotechnology, 11420), HDAC7 (Cell Signaling Technology, 2882), calnexin (Santa Cruz Biotechnology, 11397).
Blakeslee W.W., Demos-Davies K.M., Lemon D.D., Lutter K.M., Cavasin M.A., Payne S., Nunley K., Long C.S., McKinsey T.A, & Miyamoto S.D. (2017). Histone Deacetylase Adaptation in Single Ventricle Heart Disease and a Young Animal Model of Right Ventricular Hypertrophy. Pediatric research, 82(4), 642-649.
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8

Western Blot Antibody Catalog

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PDE3A (catalog number A302-740A, 1:1000 [Bethyl Laboratory]; catalog number Sc-293446, 1:20 [Santa Cruz Biotechnology]), Flag (catalog number F7425, 1:2000; Sigma), GAPDH (catalog number 60004-1-1g, 1:5000; ProteinTech), Anti-phospho-PKA substrate antibody (catalog number 9621S or 9624, 1:1000; Cell Signaling), SMAD4 (catalog number 46535, GTX01674; Cell Signaling) GATA4 (GATA4 binding protein 4; catalog number 36966, 1:1000; Cell Signaling), HDAC-1 (catalog number 34589, 1:1000; Cell Signaling), lamin B (catalog number 12586, 1:1000; Cell Signaling), lamin A/C (catalog number 4777S, 1:1000; Cell Signaling), actin-1 alpha (catalog number 17521-1-AP; Proteintech), RFP (catalog number ab62341, 1:2000; Abcam), GFP (catalog number ab6556, 1:1000; Abcam), horseradish peroxidase–conjugated goat anti-mouse (catalog number sc2005, 1:5000 [SCBT]; catalog number 705-035-151 [Jackson ImmunoResearch Labs]) or anti-rabbit secondary antibodies (catalog number sc2030, 1:5000 [Santa Cruz Biotechnology]; catalog number 705-035-152 [Jackson ImmunoResearch Labs]), antibodies conjugated with Alexa-Fluor 647 (catalog number A-21235, 1:250; Thermo Fisher Scientific), Alexa-Fluor 488 (catalog number A-11008, 1:250; Thermo Fisher Scientific), and wheat germ agglutinin conjugated with Alexa 488 (catalog number W11261; Invitrogen).
Subramaniam G., Schleicher K., Kovanich D., Zerio A., Folkmanaite M., Chao Y.C., Surdo N.C., Koschinski A., Hu J., Scholten A., Heck A.J., Ercu M., Sholokh A., Park K.C., Klussmann E., Meraviglia V., Bellin M., Zanivan S., Hester S., Mohammed S, & Zaccolo M. (2023). Integrated Proteomics Unveils Nuclear PDE3A2 as a Regulator of Cardiac Myocyte Hypertrophy. Circulation Research, 132(7), 828-848.
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9

Western Blot Analysis of Cell Signaling Proteins

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The western blot steps were described previously [20 (link)]. The blots were cut prior to hybridisation with antibodies during blotting. The original images of all blots are presented in the Supplementary Information. The proteins were detected using the following primary antibodies: anti-E-cadherin, HDAC1, Flag, vimentin and fibronectin (Cell Signaling Technology, Danvers, MA, USA). Anti-β-actin, TGIF2, ERK and p-ERK (Santa Cruz Biotechnology, Dallas, TX, USA).
Du R., Wang C., Liu J., Wang K., Dai L, & Shen W. (2023). Phosphorylation of TGIF2 represents a therapeutic target that drives EMT and metastasis of lung adenocarcinoma. BMC Cancer, 23, 52.
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10

Coimmunoprecipitation of SLC14A1 Interactome

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Coimmunoprecipitation was performed using the Pierce™ Co-Immunoprecipitation Kit (ThermoFisher). Protein lysates were incubated with anti-human SLC14A1 antibody and subsequently, magnetic beads. The protein complexes were eluted from antibody/beads after washing and subjected to immunoblot analysis by probing anti-SIN3A (Proteintech, USA), -HDAC1 (Cell Signalling, USA), -ARID4B (Proteintech) or -SUDS3 (Novus Biologicals, USA) antibody.
Chan T.C., Wu W.J., Li W.M., Shiao M.S., Shiue Y.L, & Li C.F. (2020). SLC14A1 prevents oncometabolite accumulation and recruits HDAC1 to transrepress oncometabolite genes in urothelial carcinoma. Theranostics, 10(25), 11775-11793.
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