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Histone 3 Antikörper (H3K4me2)

Dieser Kaninchen Polyklonal Antikörper detektiert spezifisch Histone 3 in WB, ChIP, DB, ChIP-seq und CUT&Tag. Es zeigt Reaktivität gegenüber Proben von Human und Maus. Es wurde in 15+ Publikationen zitiert.
Produktnummer ABIN2668425
752,31 €
Zzgl. Versandkosten 20,00 € und MwSt
Lieferung nach: Deutschland
Lieferung in 2 bis 4 Werktagen

Kurzübersicht für Histone 3 Antikörper (H3K4me2) (ABIN2668425)

Target

Alle Histone 3 (H3) Antikörper anzeigen
Histone 3 (H3) (Histone H3 (H3))

Reaktivität

  • 1805
  • 1169
  • 1021
  • 48
  • 40
  • 37
  • 36
  • 33
  • 31
  • 23
  • 23
  • 19
  • 9
  • 8
  • 6
  • 6
  • 5
  • 5
  • 4
  • 4
  • 3
  • 3
  • 3
  • 2
  • 2
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Human, Maus

Wirt

  • 1538
  • 294
  • 13
  • 5
  • 1
Kaninchen

Klonalität

  • 1144
  • 706
  • 1
Polyklonal

Konjugat

  • 979
  • 103
  • 70
  • 69
  • 67
  • 67
  • 67
  • 67
  • 42
  • 29
  • 28
  • 24
  • 24
  • 18
  • 18
  • 18
  • 17
  • 17
  • 17
  • 17
  • 17
  • 17
  • 17
  • 17
  • 17
  • 7
  • 1
Dieser Histone 3 Antikörper ist unkonjugiert

Applikation

  • 1450
  • 623
  • 519
  • 425
  • 372
  • 355
  • 251
  • 210
  • 204
  • 188
  • 177
  • 157
  • 121
  • 49
  • 48
  • 41
  • 37
  • 26
  • 25
  • 19
  • 19
  • 7
  • 7
  • 7
  • 4
  • 3
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Western Blotting (WB), Chromatin Immunoprecipitation (ChIP), Dot Blot (DB), ChIP DNA-Sequencing (ChIP-seq), Cleavage Under Targets and Tagmentation (CUT&Tag)
  • Bindungsspezifität

    • 72
    • 59
    • 54
    • 54
    • 53
    • 50
    • 50
    • 49
    • 45
    • 42
    • 40
    • 39
    • 39
    • 36
    • 32
    • 32
    • 32
    • 31
    • 31
    • 31
    • 29
    • 27
    • 27
    • 26
    • 24
    • 23
    • 22
    • 22
    • 21
    • 21
    • 20
    • 19
    • 18
    • 17
    • 16
    • 15
    • 15
    • 14
    • 14
    • 13
    • 13
    • 12
    • 11
    • 11
    • 11
    • 11
    • 10
    • 10
    • 10
    • 10
    H3K4me2

    Verwendungszweck

    Histone H3K4me2 antibody (pAb)

    Aufreinigung

    Unpurified

    Immunogen

    This Histone H3 dimethyl Lys4 antibody was raised against a peptide including dimethyl-lysine 4 of histone H3.
  • Applikationshinweise

    ChIP: 5 - 10 µL per ChIP ChIP-Seq: 3 µL each WB*: 1:1,000 - 1:5,000 dilution CUT&Tag: 1 µL per 50 µL reaction *Note: many chromatin-bound proteins are not soluble in a low salt nuclear extract and fractionate to the pellet. Therefore, we recommend a High Salt / Sonication Protocol when preparing nuclear extracts for Western Blot. For Histone H3K4me2, we also offer AbFlex Histone H3K4me2 Recombinant Antibody (rAb). For details, see Catalog No. 91321.

    Beschränkungen

    Nur für Forschungszwecke einsetzbar
  • Format

    Liquid

    Buffer

    Rabbit serum containing 30 % glycerol and 0.035 % sodium azide.

    Konservierungsmittel

    Sodium azide

    Vorsichtsmaßnahmen

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

    Handhabung

    Avoid repeated freeze/thaw cycles by aliquoting items into single-use fractions,Keep all reagents on ice when not in storage

    Lagerung

    -20 °C

    Informationen zur Lagerung

    Some products may be shipped at room temperature. This will not affect their stability or performance. Avoid repeated freeze/thaw cycles by aliquoting items into single-use fractions for storage at -20°C for up to 2 years. Keep all reagents on ice when not in storage.

    Haltbarkeit

    24 months
  • Dheekollu, Wiedmer, Sentana-Lledo, Cassel, Messick, Lieberman: "HCF1 and OCT2 Cooperate with EBNA1 To Enhance OriP-Dependent Transcription and Episome Maintenance of Latent Epstein-Barr Virus." in: Journal of virology, Vol. 90, Issue 11, pp. 5353-67, (2016) (PubMed).

    Zhan, Kost-Alimova, Shi, Leo, Bardenhagen, Shepard, Appikonda, Vangamudi, Zhao, Tieu, Jiang, Heffernan, Marszalek, Toniatti, Draetta, Tyler, Barton, Jones, Palmer, Geck Do, Andersen: "Development of novel cellular histone-binding and chromatin-displacement assays for bromodomain drug discovery." in: Epigenetics & chromatin, Vol. 8, pp. 37, (2015) (PubMed).

    Mohan, Dialynas, Weake, Liu, Martin-Brown, Florens, Washburn, Workman, Abmayr: "Loss of Drosophila Ataxin-7, a SAGA subunit, reduces H2B ubiquitination and leads to neural and retinal degeneration." in: Genes & development, Vol. 28, Issue 3, pp. 259-72, (2014) (PubMed).

    Walter, Matter, Fahrenkrog: "Loss of histone H3 methylation at lysine 4 triggers apoptosis in Saccharomyces cerevisiae." in: PLoS genetics, Vol. 10, Issue 1, pp. e1004095, (2014) (PubMed).

    Konovalov, Garcia-Bassets: "Analysis of the levels of lysine-specific demethylase 1 (LSD1) mRNA in human ovarian tumors and the effects of chemical LSD1 inhibitors in ovarian cancer cell lines." in: Journal of ovarian research, Vol. 6, Issue 1, pp. 75, (2014) (PubMed).

    Rafehi, Balcerczyk, Lunke, Kaspi, Ziemann, Kn, Okabe, Khurana, Ooi, Khan, Du, Chang, Haviv, Keating, Karagiannis, El-Osta: "Vascular histone deacetylation by pharmacological HDAC inhibition." in: Genome research, Vol. 24, Issue 8, pp. 1271-84, (2014) (PubMed).

    Kallestad, Woods, Christensen, Gefroh, Balakrishnan, Milavetz: "Transcription and replication result in distinct epigenetic marks following repression of early gene expression." in: Frontiers in genetics, Vol. 4, pp. 140, (2013) (PubMed).

    Cannuyer, Loriot, Parvizi, De Smet: "Epigenetic hierarchy within the MAGEA1 cancer-germline gene: promoter DNA methylation dictates local histone modifications." in: PLoS ONE, Vol. 8, Issue 3, pp. e58743, (2013) (PubMed).

    Cie?lik, Hoang, Baranova, Chodaparambil, Kumar, Allison, Xu, Wamsley, Gray, Jones, Mayo, Bekiranov: "Epigenetic coordination of signaling pathways during the epithelial-mesenchymal transition." in: Epigenetics & chromatin, Vol. 6, Issue 1, pp. 28, (2013) (PubMed).

    Jamieson, Rountree, Lewis, Stajich, Selker: "Regional control of histone H3 lysine 27 methylation in Neurospora." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 110, Issue 15, pp. 6027-32, (2013) (PubMed).

    Subrahmanyam, Du, Ivanova, Chakraborty, Ji, Zhang, Alt, Schatz, Sen: "Localized epigenetic changes induced by DH recombination restricts recombinase to DJH junctions." in: Nature immunology, Vol. 13, Issue 12, pp. 1205-12, (2012) (PubMed).

    Milavetz, Kallestad, Gefroh, Adams, Woods, Balakrishnan: "Virion-mediated transfer of SV40 epigenetic information." in: Epigenetics, Vol. 7, Issue 6, pp. 528-34, (2012) (PubMed).

    Liang, He, Zhang: "Kdm2b promotes induced pluripotent stem cell generation by facilitating gene activation early in reprogramming." in: Nature cell biology, Vol. 14, Issue 5, pp. 457-66, (2012) (PubMed).

    Chandrasekharan, Huang, Chen, Sun: "Histone H2B C-terminal helix mediates trans-histone H3K4 methylation independent of H2B ubiquitination." in: Molecular and cellular biology, Vol. 30, Issue 13, pp. 3216-32, (2010) (PubMed).

    Honda, Selker: "Direct interaction between DNA methyltransferase DIM-2 and HP1 is required for DNA methylation in Neurospora crassa." in: Molecular and cellular biology, Vol. 28, Issue 19, pp. 6044-55, (2008) (PubMed).

  • Target

    Histone 3 (H3) (Histone H3 (H3))

    Andere Bezeichnung

    Histone H3

    Hintergrund

    Histone H3 is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of Histone H2A, Histone H2B, Histone H3 and Histone H4). Histone H1 is a linker histone, present at the interface between the nucleosome core and DNA entry/exit points. Histone H1 is responsible for establishing higher-order chromatin structure. Chromatin is subject to a variety of chemical modifications, including post-translational modifications of the histone proteins and the methylation of cytosine residues in the DNA. Reported histone modifications include acetylation, methylation, phosphorylation, ubiquitylation, glycosylation, ADP-ribosylation, carbonylation and SUMOylation, these modifications play a major role in regulating gene expression. The methylation of histones can occur on two different residues: arginine or lysine. Histone methylation can be associated with transcriptional activation or repression, depending on the methylated residue. Lysine 4 of histone H3 can be mono-, di- or trimethylated by different histone methyltransferases (HMTs) such as SET1 or ASH1. Methylation of Lys4 is often associated with transcriptional activation. The demethylase LSD1 is able to demethylate histone H3 Lys4.

    Molekulargewicht

    17 kDa

    Gen-ID

    3020

    NCBI Accession

    NP_003522
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