Histone h4

Manufactured by Santa Cruz Biotechnology

Histone H4 is a nuclear protein that is a core component of the nucleosome, the basic unit of chromatin. Histone H4 plays a crucial role in the structural organization of chromosomes and the regulation of gene expression.

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Histone H4 (sc-25260) (3 citations) Histones (2 citations) Anti-acetyl-Histone H4 (2 citations) Goat anti-ac-Histone H4 Lys16 (sc-8662, (2 citations) Acetylated Histone-H4 (2 citations) Acetyl-Histone H4 (2 citations) Rabbit anti-Histone H4 1/100 (2 citations) Anti-Ac Histone H4 (2 citations)

4 protocols using histone h4

Protein Analysis of Tissue and Cell Lysates

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Total proteins from tissue or cells were obtained using RIPA buffer supplemented with protease and phosphatase inhibitor cocktails. A total of 30–50 μg of lysates was resolved on 10% or 15% SDS–PAGE gels, and proteins were transferred to PVDF membranes (BioRad, cat # 162–0177). Subsequent western analyses were performed using standard procedures. Antibodies against CBP (RRID: AB_2616020, 1:1000), GCN5 (RRID: AB_2128281, 1:3000), PCAF (RRID: AB_2128409, 1:3000), HDAC1 (RRID: AB_10612242, 1:2000), HDAC2 (RRID: AB_10624871, 1:3000), HDAC3 (RRID: AB_2118371, 1:3000), histone H3 (RRID: AB_10544537, 1:10000), H3K9ac (RRID: AB_823528, 1:50000), H3K14ac (RRID: AB_10839410, 1:5000), H3K18ac (RRID: AB_2783723, 1:30000), H3K27ac (RRID: AB_10949503, 1:15000), H3K56ac (RRID: AB_10548193, 1:1000), histone H4 (RRID: AB_1147658, 1:1000), H4K5ac (RRID: AB_11217428, 1:100000), H4 Antibodies against Gli1 (sc-515751, 1:1000), actin (RRID: AB_2223345, 1:3000) and tubulin (RRID: AB_1130901, 1:3000) were purchased from Santa Cruz. Antibodies against HAT1 (RRID: AB_2116435, 1:3000) were purchased from Proteintech. For Ptch;p53 SD-CSC tumors shown in figure 2, 4, and 5, same *ß-ACTIN loading control image is shown since same samples were loaded on multiple gels on the same day and membranes were cut into multiple pieces to probe different proteins shown.

George J., Chen Y., Abdelfattah N., Yamamoto K., Gallup T.D., Adamson S.I., Rybinski B., Srivastava A., Kumar P., Lee M.G., Baskin D.S., Jiang W., Choi J.M., Flavahan W., Chuang J.H., Kim B.Y., Xu J., Jung S.Y, & Yun K. (2022). Cancer Stem Cells, not Bulk Tumor Cells, Determine Mechanisms of Resistance to SMO Inhibitors. Cancer Research Communications, 2(6), 402-416.

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Antibody-based Protein Analysis in Adrenal Tissues

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Antibodies to PDH kinase-4 (PDK4), PGC-1α (for immunoprecipitation), and histone H4 were purchased from Santa Cruz Biotechnology (Dallas, TX). Antibodies to acetylated lysine, acetylated p53 (Lys³⁷⁹), phospho-AMPK-α (Thr¹⁷²), AMPK-α, conformation-specific anti-rabbit IgG, and GAPDH were from Cell Signaling Technology (Danvers, MA). Total PGC-1α and Sirt1 were measured using antibodies from Millipore (Billerica, MA). Antibodies against p53, COXIV, and ATP5F1 were purchased from Novus Biologicals (Littleton, CO). Standard immunoprecipitation procedures (Cell Signaling Technology) and Western blotting procedures (Invitrogen, Carlsbad, CA) were performed, with GAPDH used as a loading control for whole-tissue samples; histone H4 protein was used as the loading control for nuclear extracts. Quantitation by densitometry used Scion image software (Frederick, MD), with data expressed as the ratio of band intensity of the protein of interest to loading control. When immunoblotting procedures of protein samples from the AdrKO and AdrTG groups were performed in the same run; the data were expressed as a ratio of the WT in the AdrKO group. When the blotting procedures were performed separately, the WTs in relevant individual groups (AdrKO or AdrTG) were used as the control.

Gao S., McMillan R.P., Jacas J., Zhu Q., Li X., Kumar G.K., Casals N., Hegardt F.G., Robbins P.D., Lopaschuk G.D., Hulver M.W, & Butler A.A. (2014). Regulation of Substrate Oxidation Preferences in Muscle by the Peptide Hormone Adropin. Diabetes, 63(10), 3242-3252.

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Protein Extraction and Western Blotting

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Nuclear and cytoplasmic proteins were extracted according to the manufacturer's instructions (Sigma, #NXTRACT). Western blotting was performed as described in detail in a previous study [26 (link)]. Primary antibodies used in current study included anti-mouse Yap1 (Abcam, #ab56701), TAZ (Cell signaling, #4883), Histone H4 (Santa Cruz, #sc-25260), Hsp90 (Santa Cruz, #sc-8262), p-Smad2 (Santa Cruz, #sc-101801), Smad3 (Cell signaling, #9513), p-Smad3 (Santa Cruz, #sc-11769), Krt14 (Santa Cruz, #sc-43310), Krt18 (Santa Cruz, #sc-45406) and p63 (Abcam, #ab124762).

Sun J.G., Chen X.W., Zhang L.P., Wang J, & Diehn M. (2015). Yap1 promotes the survival and self-renewal of breast tumor initiating cells via inhibiting Smad3 signaling. Oncotarget, 7(9), 9692-9706.

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SARS-CoV-2 Protein Expression and Localization

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The primary antibodies for western blotting (WB) experiments: mAbs anti-GAPDH (sc-32233) and -Histone H4, were from Santa Cruz Biotechnology (Dallas, TX). pAbs anti–ACE2 (AB_2792286) was from Invitrogen (Waltham, MA). pAbs anti-TMPRSS2 (ab109131) was from Abcam (Cambridge, UK). Ab anti-acetyl-H3 (06599) was from Millipore (Merk, Kenilworth, NJ). Ab anti-acetyl-H4 (06866) was from Millipore (Merk, Kenilworth, NJ); control rabbit IgG (NB810-56910) was from Novus Bio, Minneapolis, MN.
Antibodies for Immunofluorescence: anti-ACE2 (Thermo Fisher Scientific, Waltham, MA, USA, AB_2792286). Cy3-conjugated anti-rat secondary antibodies (Jackson ImmunoResearch, 112-165-003). DRAQ5 staining solution (#130-117-343) was from Milteny. MS-275, MGCD0103, MC-2468, MC-4448, Tubastatin A, PCI34051, MC-2500 were from Prof. Mai laboratory. The VSV-spike-GFP construct was a kind gift from Sean Whelan, Washington University St. Louis, USA.

Trionfetti F., Alonzi T., Bontempi G., Terri M., Battistelli C., Montaldo C., Repele F., Rotili D., Valente S., Zwergel C., Matusali G., Maggi F., Goletti D., Tripodi M., Mai A, & Strippoli R. (2023). HDAC1-3 inhibition increases SARS-CoV-2 replication and productive infection in lung mesothelial and epithelial cells. Frontiers in Cellular and Infection Microbiology, 13, 1257683.

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