Hdac2

Manufactured by Proteintech

Sourced in United States

HDAC2 is a lab equipment product that functions as a histone deacetylase enzyme. It is involved in the regulation of gene expression by deacetylating histones, which can lead to changes in chromatin structure and transcriptional activity.

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Lab products found in correlation

Hdac1, by Proteintech (3 mentions) Hdac3, by Proteintech (2 mentions) Hdac4, by Proteintech (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Ubiquitin, by Proteintech (1 mentions) Chloroquine, by MedChemExpress (1 mentions) Parkin, by Proteintech (1 mentions) Anti flag m2 affinity gel, by Merck Group (1 mentions) α tubulin, by Merck Group (1 mentions) Ep300, by Abcam (1 mentions) Flag tag (flag), by Sangon (1 mentions) Tim23, by Santa Cruz Biotechnology (1 mentions) Vdac1, by Proteintech (1 mentions) Trichostatin a, by MedChemExpress (1 mentions) Bafilomycin a1, by Merck Group (1 mentions) Gapdh, by Proteintech (1 mentions) β actin, by ABclonal (1 mentions) Bcl2 associated x (bax), by Proteintech (1 mentions) Hoechst, by Beyotime (1 mentions) Bcl 2, by Proteintech (1 mentions)

6 protocols using hdac2

Antibody-based Mitochondrial Protein Analysis

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The antibodies used in our experiments included: ACAT1 (CST, 44276), acetylated-lysine (CST, 9441), BAX (Proteintech, 50599-2-Ig), BCL-2 (Proteintech, 12789-1-AP), COXⅣ (CST, 11967), cleaved-PARP-1 (CST, 5625), cleaved-caspase3 (CST, 9661), EP300 (Abcam, ab14984), FLAG (Sangon Biotech, D191041), anti-FLAG® M2 Affinity Gel (MERCK, F2426), GAPDH (Proteintech, 600004-1-lg), HDAC1 (Proteintech, 10197-1-AP), HDAC2 (Proteintech, 12922-3-AP), HDAC3 (Proteintech, 10255-1-AP), HSP60 (CST, 12165), HA (Sangon Biotech, D110004), Ki67 (Proteintech, 27309-1-AP), LC3 (MERCK, L7543), MFN2 (Proteintech, 12186-1-AP), PINK1 (CST, 6946), Parkin (Proteintech, 14060-1-AP; CST, 4211), Parkin (phospho-Ser65, Biorbyt, orb312554), P62 (MERCK, P0067), TOMM20 (CST, 42406), TIM23 (Santa Cruz Biotechnology, sc-514463), ubiquitin (Proteintech, 10201-2-AP), ULK1 (CST, 8054), VDAC1 (Proteintech, 10866-1-AP), α-tubulin (Sigma, T6199), β-actin (ABclonal, AC004).
The chemicals used in our experiments were: bafilomycin A1 (Sigma, B1793), chloroquine (MedChemExpress, HY-17589A), Hoechst (Beyotime, 33342), suberoylanilide hydroxamic acid (SAHA; MedChemExpress, HY-10221), and trichostatin A (TSA, MedChemExpress, HY-15144).

Sun X., Shu Y., Ye G., Wu C., Xu M., Gao R., Huang D, & Zhang J. (2021). Histone deacetylase inhibitors inhibit cervical cancer growth through Parkin acetylation-mediated mitophagy. Acta Pharmaceutica Sinica. B, 12(2), 838-852.

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Protein Extraction and Western Blot Analysis

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We extracted protein from cells and tissues, and we quantified the concentration using the BCA protein detection kit (Beyotime, China). Separated proteins were transferred to polyvinylidene fluoride (PVDF) membranes by adding 10% or 12% SDS‒PAGE. The PVDF membrane was incubated with the primary antibody overnight at 4 °C, followed by 1 h of incubation with horseradish peroxidase-conjugated secondary antibodies. Target proteins were detected using an enhanced chemiluminescence system. Images were acquired using a multifunctional UVP ChemStudio/PLUS imager (Jena, Thuringia, Germany). The antibodies used were as follows: AZGP1, HDAC1, H3K27Ac from Abcam (Abcam, Cambridge, UK); smad3, p-smad3, and GAPDH from CST (CST, Beverly MA, USA); TGF-β1, E-cadherin, N-Cadherin, Vimentin, HDAC2, HDAC3, and HDAC7 from Proteintech (Proteintech, Chicago, USA).

Deng L., Bao W., Zhang B., Zhang S., Chen Z., Zhu X., He B., Wu L., Chen X., Deng T., Chen B., Yu Z., Wang Y, & Chen G. (2023). AZGP1 activation by lenvatinib suppresses intrahepatic cholangiocarcinoma epithelial-mesenchymal transition through the TGF-β1/Smad3 pathway. Cell Death & Disease, 14(9), 590.

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Combinatorial Anti-Cancer Drug Screening

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Sorafenib, quisinostat (JNJ-26481585), JNK inhibitor SP600125, AKT inhibitor MK2206 2HCL and Caspase inhibitor Z-VAD-FMK were from Selleckchem (Houston, Texas, USA). Dimethylsulfoxide was purchased from Sigma-Aldrich (St. Louis, MO, USA). Minimum Essential Medium Eagle (MEM), fetal bovine serum (FBS) were from Gibco Life Technologies (Grand Island, NY, USA). The Cell Counting Kit-8 was purchased from Dojindo (Kumamoto, Japan). The cell cycle staining kit was from MultiSciences (Hangzhou, China). The Annexin V-FITC apoptosis detection kit was obtained from KeyGen Biotech (Nanjing, China). The EdU Apollo567 In Vitro Imaging Kit was from Ribobio (Guangzhou, China). The BCA protein assay kit was from Thermo Fisher Scientific Inc (Waltham, Massachusetts, USA). The following antibodies were used: HDAC1, HDAC2, HDAC4 (Proteintech), p21Cip1, CyclinD1, CyclinE1, CyclinA2, cdk2, cdk4, cdk6, Cleaved-Caspase-3, Cleaved-Caspase-9, Caspase-3, Caspase-9, Cleaved-PARP, PARP, phospho-JNK, JNK, PI3K-p110, PI3K- p85, phospho-AKT⁴⁷³, phospho-c-jun, Bcl-xl, Bcl2, Bax, Survivin, Ki67, GAPDH (Cell Signaling Technology).

He B., Dai L., Zhang X., Chen D., Wu J., Feng X., Zhang Y., Xie H., Zhou L., Wu J, & Zheng S. (2018). The HDAC Inhibitor Quisinostat (JNJ-26481585) Supresses Hepatocellular Carcinoma alone and Synergistically in Combination with Sorafenib by G0/G1 phase arrest and Apoptosis induction. International Journal of Biological Sciences, 14(13), 1845-1858.

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Western Blot Analysis of Cell Signaling

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After transfection and/or treatment with chemicals, the cells were lysed for a Western blot assay as described previously 12. The blots were incubated with primary antibodies against PERK, p‐PERK (Thr981), ATF4 (CREB‐2), ATF3, Bcl‐2, BAX, poly (ADP‐ribose) polymerase (PARP), HDAC1 glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) (Santa Cruz Biotechnology, Dallas, TX, USA), cleaved caspase‐3 (Epitomics, Burlingame, CA, USA), mTOR and phospho‐mTOR (Ser2448), DJ‐1, GRP78, eIF2a, phospho‐eIF2a, AKT, phospho‐AKT (Ser473), HDAC5, HDAC6 (Cell Signaling Technology, Danvers, MA, USA), 4EBP1 (Abcam, Cambridge, MA, USA), HDAC2, HDAC4 and COX4 (Proteintech, Wuhan, China) overnight at 4°C, respectively, followed by appropriate peroxidase‐conjugated secondary antibodies. GAPDH or actin served as an internal control. The detection system visualization (Millipore) was followed by exposure to X‐ray film.

Xu Q., Liu X., Zhu S., Hu X., Niu H., Zhang X., Zhu D., Nesa E.U., Tian K, & Yuan H. (2018). Hyper‐acetylation contributes to the sensitivity of chemo‐resistant prostate cancer cells to histone deacetylase inhibitor Trichostatin A. Journal of Cellular and Molecular Medicine, 22(3), 1909-1922.

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Protein Expression Analysis in Tissue Lysates

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Tissue and cell lysates were prepared using RIPA buffer (20 mM Tris-Cl pH 7.5, 140 mM NaCl, 1 mM CaCl₂ and MgCl₂, 10 mM NaF, 1% NP-40, 10% glycerol, 2 mM Na-Vanadate, and 1 mM PMSF). Proteins were subjected to SDS-PAGE and were then transferred onto polyvinylidene difluoride (PVDF) membranes (Millipore). Immunoblotting was performed with the following primary antibodies, according to the manufacturer’s protocol: KLF9 (Invitrogen; Cat: 701888; Clone name: 5H16L7; Dilution: 1:1000), KLF9 (Abcam; Cat: ab227920; Dilution: 1:1000), PGC1α (Millipore; Cat: AB3242; Dilution: 1:1000), UCP1 (Abcam; Cat: ab10983; Dilution: 1:1000), SERCA2(ABclonal; Cat: A11692; Clone name: ARC0679; Dilution: 1:1000), β-Actin (ABclonal; Cat: AC026; Clone name: ARC5115-01; Dilution: 1:20,000), ARG1 (ABclonal; Cat: A4923; Clone name: ARC1164; Dilution: 1:1000), SREBP1 (ABclonal; Cat: A15586; Dilution: 1:1000), HDAC1 (ABclonal; Cat: A0238; Dilution: 1:1000), HDAC2 (ABclonal; Cat: A2084; Dilution: 1:1000), SIN3A (Proteintech; Cat: 14638-1-AP; Dilution: 1:1000), STAT3 (Santa Cruz Biotechnology; Cat: sc-8019; Dilution: 1:50), P-STAT3 (Santa Cruz Biotechnology; Cat: sc-8059; Dilution: 1:50), p65 (Cell Signaling Technology; Cat: #8242; Clone name: D14E12; Dilution: 1:1000), P-p65 (Cell Signaling Technology; Cat: #3033; Clone name: 93H1; Dilution: 1:1000).

Zhang Y., Du C., Wang W., Qiao W., Li Y., Zhang Y., Sheng S., Zhou X., Zhang L., Fan H., Yu Y., Chen Y., Liao Y., Chen S, & Chang Y. (2024). Glucocorticoids increase adiposity by stimulating Krüppel-like factor 9 expression in macrophages. Nature Communications, 15, 1190.

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Immunoblotting Protocol for Protein Analysis

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Tissue samples were solubilized with 4X Laemmli Sample Buffer (Bio-Rad) with β-mercaptoethanol , separated with 4–12% Bis–Tris gradient gel(Life Technologies), transferred to PVDF blotting paper, and developed as previously described^{71 (link)}. The immunoblotting antibodies were β-actin(Sigma#A5441), CCT5(Scbt#sc-377261), CCT8(Scbt#sc-376188), COXIV(CST#4,850), EIF1A(CST#2,538), HDAC2(ProteinTech#12,922–3), and SynGAP(Abcam#ab3344). The immunoblots were quantitated as previously described^{34 (link)}.

McClatchy D.B., Martínez-Bartolomé S., Gao Y., Lavallée-Adam M, & Yates JR I.I.I. (2020). Quantitative analysis of global protein stability rates in tissues. Scientific Reports, 10, 15983.

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