Histone 3 Antikörper (H3K27me)

Produktnummer ABIN3023269

Dieses Anti-Histone 3-Antikörper ist ein Kaninchen Polyklonal-Antikörper zur Detektion von Histone 3 in WB, IHC, IF, ChIP, IP und ChIP-seq. Geeignet für Human. Dieses Primary Antibody wurde in 14+ Publikationen zitiert.

Kurzübersicht für Histone 3 Antikörper (H3K27me) (ABIN3023269)

Target: Histone 3 (H3) (Histone H3 (H3))

Reaktivität: Human

Wirt: Kaninchen

Klonalität: Polyklonal

Konjugat: Dieser Histone 3 Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), Chromatin Immunoprecipitation (ChIP), Immunoprecipitation (IP), ChIP DNA-Sequencing (ChIP-seq)

Produktdetails anti-Histone 3 Antikörper

Bindungsspezifität: H3K27me

Kreuzreaktivität: Human, Maus, Ratte

Produktmerkmale: Methylated Antibodies

Aufreinigung: Affinity purification

Immunogen: A synthetic methylated peptide corresponding to residues surrounding K27 of human histone H3

Isotyp: IgG

Anwendungsinformationen

Applikationshinweise: WB,1:500 - 1:2000,IHC,1:50 - 1:200,IF,1:50 - 1:200,IP,1:50 - 1:200,ChIP,1:20 - 1:100,ChIP-seq,1:20 - 1:100

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Buffer: PBS with 0.02 % sodium azide,50 % glycerol, pH 7.3.

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Handhabung: Avoid freeze / thaw cycles

Lagerung: -20 °C

Informationen zur Lagerung: Store at -20°C. Avoid freeze / thaw cycles.

Referenzen für anti-Histone 3 Antikörper (ABIN3023269)

Wang, Wang, Lin, Ye, Li, Tu, Shen, Li, Yang, Zhang: "Evolutionary dynamics of 3D genome architecture following polyploidization in cotton." in: Nature plants, Vol. 4, Issue 2, pp. 90-97, (2018) (PubMed).

Cheng, Tan, Lu, Liu, Li, Yuan, Zhao, Zhou: "WOX11 recruits a histone H3K27me3 demethylase to promote gene expression during shoot development in rice." in: Nucleic acids research, Vol. 46, Issue 5, pp. 2356-2369, (2018) (PubMed).

Wu, Tian, Zhang, Tong, Huang, Li, Zhao, Tang, Yuan, Wang, Fang, Gao, Hu, Li, Qin, Yao, Chen, Chen, Zhang, Liu, Sun, Chen, Wong, Ge, Chen, Ji: "In vivo CRISPR screening unveils histone demethylase UTX as an important epigenetic regulator in lung tumorigenesis." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 115, Issue 17, pp. E3978-E3986, (2018) (PubMed).

Dumasia, Kumar, Deshpande, Balasinor: "Estrogen, through estrogen receptor 1, regulates histone modifications and chromatin remodeling during spermatogenesis in adult rats." in: Epigenetics, Vol. 12, Issue 11, pp. 953-963, (2018) (PubMed).

Yu, Liu, Liu, Wang, Liu, Miao, Du, Yang: "Ascorbic acid induces global epigenetic reprogramming to promote meiotic maturation and developmental competence of porcine oocytes." in: Scientific reports, Vol. 8, Issue 1, pp. 6132, (2018) (PubMed).

Song, Li, Wang, Du, Yang: "DMBA acts on cumulus cells to desynchronize nuclear and cytoplasmic maturation of pig oocytes." in: Scientific reports, Vol. 7, Issue 1, pp. 1687, (2018) (PubMed).

Tang, Guo, Zhu, Huang, Liu, Cai, Yu, Wang: "Metformin inhibits ovarian cancer via decreasing H3K27 trimethylation." in: International journal of oncology, Vol. 52, Issue 6, pp. 1899-1911, (2018) (PubMed).

Cao, Liu, Yue, Liu, Pei, Gu, Wang, Jia: "Iron chelation inhibits cancer cell growth and modulates global histone methylation status in colorectal cancer." in: Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, Vol. 31, Issue 5, pp. 797-805, (2018) (PubMed).

Wang, Tu, Lin, Lin, Wang, Yang, Ye, Shen, Li, Zhang, Zhou, Nie, Li, Guo, Ma, Huang, Jin, Zhu, Yang, Min, Yuan, Zhang, Lindsey, Zhang: "Asymmetric subgenome selection and cis-regulatory divergence during cotton domestication." in: Nature genetics, Vol. 49, Issue 4, pp. 579-587, (2017) (PubMed).

Zhou, Liu, Zhou, Zhou, Zhao, Li, Zhou: "Cooperation between the H3K27me3 Chromatin Mark and Non-CG Methylation in Epigenetic Regulation." in: Plant physiology, Vol. 172, Issue 2, pp. 1131-1141, (2017) (PubMed).

Kumar, Dumasia, Deshpande, Balasinor: "Direct regulation of genes involved in sperm release by estrogen and androgen through their receptors and coregulators." in: The Journal of steroid biochemistry and molecular biology, Vol. 171, pp. 66-74, (2017) (PubMed).

Su, Li, Lei, Wang, Zhao, Cai, Wang, Li, Wu: "The EZH1-SUZ12 complex positively regulates the transcription of NF-κB target genes through interaction with UXT." in: Journal of cell science, Vol. 129, Issue 12, pp. 2343-53, (2017) (PubMed).

Yi, Guo, Guo, Sun, Yang, Wang, Li, Xie, Cai, Wang: "EZH2-mediated epigenetic silencing of TIMP2 promotes ovarian cancer migration and invasion." in: Scientific reports, Vol. 7, Issue 1, pp. 3568, (2017) (PubMed).

Liu, Zhou, Wang, Ye, Zhao, Xu, Zhou, Tan, Cheng, Zhou: "Regulation of histone methylation and reprogramming of gene expression in the rice inflorescence meristem." in: The Plant cell, Vol. 27, Issue 5, pp. 1428-44, (2016) (PubMed).

Details zu Histone 3

Target: Histone 3 (H3) (Histone H3 (H3))

Andere Bezeichnung: Histone H3

Hintergrund: Actin is a key regulator of RNA polymerase (Pol) II-dependent transcription. Positive transcription elongation factor b (P-TEFb), a Cdk9/cyclin T1 heterodimer, has been reported to play a critical role in transcription elongation. However, the relationship between actin and P-TEFb is still not clear. In this study, actin was found to interact with Cdk9, a catalytic subunit of P-TEFb, in elongation complexes. Using immunofluorescence and immunoprecipitation assays, Cdk9 was found to bind to G-actin through the conserved Thr-186 in the T-loop. Overexpression and in vitro kinase assays showed that G-actin promotes P-TEFb-dependent phosphorylation of the Pol II C-terminal domain. An in vitro transcription experiment revealed that the interaction between G-actin and Cdk9 stimulated Pol II transcription elongation. ChIP and immobilized template assays indicated that actin recruited Cdk9 to a transcriptional template in vivo and in vitro. Using cytokine IL-6-inducible p21 gene expression system, we revealed that actin recruited Cdk9 to endogenous gene. Moreover, overexpression of actin and Cdk9 increased histone H3 acetylation and acetylized histone H3 binding to a transcriptional template through the interaction with histone acetyltransferase, p300. Taken together, our results suggested that actin participates in transcription elongation by recruiting Cdk9 for phosphorylation of the Pol II C-terminal domain, and the actin-Cdk9 interaction promotes chromatin remodeling.,H3.4,H3/g,H3FT,H3t,HIST3H3,Histone H3,HIST1H3A,Signal Transduction,MAPK-Erk Signaling Pathway,MAPK-P38 Signaling Pathway,Epigenetics & Nuclear Signaling,Epigenetic Modifications,Methylation,Histone H3

Molekulargewicht: 15 kDa

Gen-ID: 8290

UniProt: Q16695