Rabbit anti histone h3

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Rabbit anti-Histone H3 is a primary antibody that specifically binds to the histone H3 protein, which is a core component of nucleosomes in eukaryotic cells. This antibody can be used in various applications, such as Western blotting, immunohistochemistry, and chromatin immunoprecipitation, to detect and study the presence and distribution of histone H3 in biological samples.

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Close spelling variants of this product

Histone H3 (74 citations) Anti-histone H3 (36 citations) Histones (2 citations) Rabbit anti-TM (2 citations)

5 protocols using rabbit anti histone h3

Protein Extraction and Western Blotting

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Protein extraction and Western Blotting were performed as described previously (Dutta and Baehrecke, 2008 (link)). Primary antibodies used were rabbit anti-GFP (1:1,000) (Novus Biologicals), chicken anti-GFP (1:20,000) (Abcam), mouse anti-Ecdysone Receptor (1:500) (Developmental Studies Hybridoma Bank), mouse anti-Broad Complex (1:100) (Developmental Studies Hybridoma Bank), Rabbit anti-Histone-H3 (1:2000) (Santa Cruz Biotechnology), and mouse anti-Beta-Tubulin (1:500) (Developmental Studies Hybridoma Bank). Western blots were imaged using a Bio-Rad Chemi-Doc XRS+ and quantified using Bio-Rad Image Lab software.

Nelson C., Ambros V, & Baehrecke E.H. (2014). miR-14 regulates autophagy during developmental cell death by targeting ip3-kinase 2. Molecular cell, 56(3), 376-388.

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Comprehensive Protein Analysis Protocol

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Nuclear and Cytoplasmic Protein Extraction Kit (Beyotime Biotech, China); Lipofectmin 2000 (Invitrogen, USA); Entranster™-in vivo transfection reagent (Engreen Biosystem, China); pifithrin-α (Sigma, USA); fluvastatin (Novartis Pharma, Switzerland); 3-methyadenine (Sigma, USA); Bafilomycin A1 (Santa Cruz, CA, USA), chloroquine (MedChemExpress, USA), denosumab (Prolia, Amgen Inc., USA); mouse-anti-AMPKα1/2 (sc-74461, Santa Cruz, USA); rabbit-anti-pAMPKα1/2 (Thr 172) (sc-33524, Santa Cruz, USA); rabbit-anti-ACCα (sc-30212, Santa Cruz); rabbit-anti-ACCα (sc-271965, Santa Cruz); mouse-anti-PTEN (sc-7974, Santa Cruz); rabbit-anti-AKT (sc-8312, Santa Cruz); rabbit-anti-pAKT (Ser 473) (sc-33437, Santa Cruz); rabbit-anti-Histone H3 (sc-10809, Santa Cruz); mouse-anti-p53 (sc-126, Santa Cruz); rabbit-anti-LC3 (sc-28266, Santa Cruz); rabbit-anti-mTOR (sc-8319, Santa Cruz); rabbit-anti-mTOR (Ser 2448) (sc-101738, Santa Cruz); mouse-anti-β-Actin (sc-47778, Santa Cruz).

Yang Z., Su Z., DeWitt J.P., Xie L., Chen Y., Li X., Han L., Li D., Xia J., Zhang Y., Yang Y., Jin C., Zhang J., Li S., Li K., Zhang Z., Qu X., He Z., Chen Y., Shen Y., Ren M, & Yuan Z. (2017). Fluvastatin Prevents Lung Adenocarcinoma Bone Metastasis by Triggering Autophagy. EBioMedicine, 19, 49-59.

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ChIP-qRT-PCR Protocol for PRDM16

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Chromatin immunoprecipitation assays were performed using the SimpleChIP Enzymatic Chromatin IP Kit (Magenetic Beads, Cell Signaling Technology, #9003). Briefly, K1 cells were cross-linked by 1% formaldehyde for 10 min at room temperature. The cross-link reaction was quenched by glycine, and cells were lysed in PBS buffer containing a protease inhibitor cocktail. Fragmented chromatin was treated with micrococcal nuclease and subjected to sonication to shear chromatin DNA into fragments with 200–500 base pairs in size. Chromatin immunoprecipitation was performed with rabbit antihistone H3 (a technical positive control; 1:50) (sc7160; Santa Cruz Biotechnology), goat anti-PRDM16 antibody (ABIN, 184809; 3 μg), and normal rabbit IgG (a negative control; 5 μg) (Cell Signaling Technology). After washing with a series of low and high salt concentration washing buffers, immunoprecipitated DNA fragments were de-crosslinked and purified. Immunoprecipitated DNA was quantified by qRT-PCR using SYBR Green Premix Ex Taq (Takara, Dalian, China) with primers for PRDM16 binding sites in PC promoter (listed in Supplementary Table 3). Fold enrichment was calculated based on the threshold cycle (CT) value of the Ig G control using the comparative CT method.

Liu W.L., Guan Q., Wen D., Ma B., Xu W.B., Hu J.Q., Wei W.J., Li D.S., Wang Y., Xiang J., Liao T, & Ji Q.H. (2021). PRDM16 Inhibits Cell Proliferation and Migration via Epithelial-to-Mesenchymal Transition by Directly Targeting Pyruvate Carboxylase in Papillary Thyroid Cancer. Frontiers in Cell and Developmental Biology, 9, 723777.

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Antibody Characterization for Cellular Analysis

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The following primary antibodies were used at indicated dilutions: mouse anti-APC/CC1 [immunohistochemistry (IHC) 1:20; Millipore OP80], mouse anti-CNP [western blotting (WB) 1:1000; Millipore C5922], rabbit anti-Dystrophin (WB 1 µg/ml, Abcam AB15277), mouse anti-beta-dystroglycan (WB 1:250; Developmental Studies Hybridoma Bank), rat anti-Ki67 (IHC: 1:100, Invitrogen 4-5698-82), rat anti-MBP (IHC 1:200; WB 1:1000; BioRad AA82-87), rabbit anti-Histone H3 (1:750; Santa Cruz), rabbit anti-MOG (WB: 1:1000; Abcam ab108505), rabbit anti-GFAP (1:1000; DAKO), rabbit anti-Olig2 (IHC 1:100; Millipore AB9610), goat anti-PDGFRα , (IHC 1:100; R&D Systems AF1062), mouse anti-SOX2 (IHC 1:100; R&D Systems MAB2018), mouse (IgG1) anti-β-Catenin [immunofluorescence (IF) Wholemount 1:500; BD Transduction Labs 610153], rabbit anti-γ-Tubulin (IF Wholemount 1:500; Sigma T5192). Olig2 was visualized using anti-rabbit CY5, Ki67 was visualized using anti-rat Alexa-Fluor 488, Sox2 was visualized using anti-mouse CY3, and PDGFRα was visualized using antigoat Alexa-Fluor 680. The following secondary antibodies were used at indicated dilutions: anti-mouse IgG1 (IF Wholemount 1:500; Fisher A-21240), anti-rabbit IRDye 800 Donkey (1:2500; Licor AB_2715510), anti-mouse IRDye 800 Donkey (1:2500; Licor AB_621847), anti-rat (IRDye 800 Goat) (1:4000; Licor AB_2721932).

Arreguin A.J., Shao Z, & Colognato H. (2024). Dmdmdx mice have defective oligodendrogenesis, delayed myelin compaction and persistent hypomyelination. Disease Models & Mechanisms, 17(4), dmm050115.

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Macrophage response to silica and rCC16

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THP-1 cells were seeded in 6-well plates, induced to a mature macrophage-like state by PMA. After treated with silica particles and/or rCC16, the macrophages were washed by PBS and then scraped into 1.5-mL EP tubes.
Total cell lysates, cytosolic or nuclear extracts were separated by sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) and then transferred onto polyvinylidene difluoride (PVDF) membranes. Nuclear and cytosolic extracts was extracted with a Nuclear and Cytoplasmic Protein Extraction kit (P0028, Beyotime Biotechnology, Shanghai, China) in accordance with the manufacturer's instructions. After blockade with 5% BSA, PVDF membranes were incubated overnight at 4°C with corresponding primary antibodies and followed by incubation with appropriate secondary antibodies. The primary antibodies used in this study included: rabbit anti-NF-κB p65, rabbit anti-NLRP3 (both from Cell Signaling Technology, Danvers, MA, USA), mouse anti-IL-1β (R&D Systems, Minneapolis, MN, USA), rabbit anti-caspase-1 p10, rabbit anti-β-actin and rabbit anti-Histone H3 antibodies (all from Santa Cruz Biotechnology, Santa Cruz, CA, USA). Secondary antibodies were horseradish peroxidase-conjugated anti-mouse and Santi-rabbit IgG (both from Santa Cruz Biotechnology).

Cui X., Xu R., Zhang H., Peng Z., Feng M., Yu B., Wang Y., Shi T., Zhou Y, & Liu Y. (2020). Exogenous Clara cell protein 16 attenuates silica particles-induced inflammation in THP-1 macrophages by down-regulating NF-κB and caspase-1 activation. The Journal of toxicological sciences, 45(10).

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