Histone 3 Antikörper (H3K4me3)

Produktnummer ABIN2668472

Zitiert in 75+ Publikationen. Der Kaninchen Polyklonal anti-Histone 3 Antikörper (ABIN2668472) detektiert spezifisch Histone 3 in WB, IHC, IF, ChIP, ICC, DB, ChIP-seq, CUT&Tag und CUT&RUN. Dieser Antikörper reagiert spezifisch mit Proben aus Human, Maus und Saccharomyces cerevisiae.

Kurzübersicht für Histone 3 Antikörper (H3K4me3) (ABIN2668472)

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

Reaktivität: Human, Maus, Saccharomyces cerevisiae

Wirt: Kaninchen

Klonalität: Polyklonal

Konjugat: Dieser Histone 3 Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), Chromatin Immunoprecipitation (ChIP), Immunocytochemistry (ICC), Dot Blot (DB), ChIP DNA-Sequencing (ChIP-seq), Cleavage Under Targets and Tagmentation (CUT&Tag), Cleavage Under Targets and Release Using Nuclease (CUT&RUN)

Produktdetails anti-Histone 3 Antikörper

Bindungsspezifität: H3K4me3

Verwendungszweck: Histone H3K4me3 antibody (pAb)

Aufreinigung: Unpurified

Immunogen: This Histone H3 trimethyl Lys4 antibody was raised against a peptide including trimethyl-lysine 4 of histone H3.

Anwendungsinformationen

Applikationshinweise: ChIP: 3 - 5 µL per ChIP ChIP-Seq: 3 µL each ICC/IF: 1:500 - 1:1,000 dilution WB: 1:500 - 1:2,000 dilution CUT&Tag: 1 µL per 50 µL reaction* CUT&RUN: 1 µL per 50 µL reaction TIP-ChIP: 2 µL *This antibody has been validated for CUT&Tag using Active Motif's CUT&Tag-IT Assay Kit, Catalog No. 53160. modENCODE validation: this antibody was validated for ChIP-Seq in this study (see reference). NGS-QC certification: this antibody has been processed by the NGS-QC generator. For additional details, click here.. **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.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

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

Referenzen für anti-Histone 3 Antikörper (ABIN2668472)

Henikoff, Henikoff, Kaya-Okur, Ahmad: "Efficient chromatin accessibility mapping in situ by nucleosome-tethered tagmentation." in: eLife, Vol. 9, (2020) (PubMed).

Brahma, Henikoff: "RSC-Associated Subnucleosomes Define MNase-Sensitive Promoters in Yeast." in: Molecular cell, Vol. 73, Issue 2, pp. 238-249.e3, (2019) (PubMed).

Pan, Guan, Liu, Li, Wang, Wu, Zhou, Zhang, Ren, Zhang, Li, Yang, Hao, Yuan, Yuan, Wang, Ju, Mao, Li, Qu, Tang, Liu: "SIRT6 safeguards human mesenchymal stem cells from oxidative stress by coactivating NRF2." in: Cell research, Vol. 26, Issue 2, pp. 190-205, (2016) (PubMed).

Toth, Papp, Brulois, Choi, Gao, Jung: "LANA-Mediated Recruitment of Host Polycomb Repressive Complexes onto the KSHV Genome during De Novo Infection." in: PLoS pathogens, Vol. 12, Issue 9, pp. e1005878, (2016) (PubMed).

Lowe, Gemma, Rakyan, Holland: "Sexually dimorphic gene expression emerges with embryonic genome activation and is dynamic throughout development." in: BMC genomics, Vol. 16, pp. 295, (2015) (PubMed).

Weirich, Kudithipudi, Kycia, Jeltsch: "Somatic cancer mutations in the MLL3-SET domain alter the catalytic properties of the enzyme." in: Clinical epigenetics, Vol. 7, Issue 1, pp. 36, (2015) (PubMed).

Valdez, Li, Murray, Ji, Liu, Popat, Champlin, Andersson: "Comparison of the cytotoxicity of cladribine and clofarabine when combined with fludarabine and busulfan in AML cells: Enhancement of cytotoxicity with epigenetic modulators." in: Experimental hematology, Vol. 43, Issue 6, pp. 448-61.e2, (2015) (PubMed).

Brown, Esterhazy, Sarde, London, Pullabhatla, Osma-Garcia, Al-Bader, Ortiz, Elgueta, Arno, de Rinaldis, Mucida, Lord, Noelle: "Retinoic acid is essential for Th1 cell lineage stability and prevents transition to a Th17 cell program." in: Immunity, Vol. 42, Issue 3, pp. 499-511, (2015) (PubMed).

Sabò, Kress, Pelizzola, de Pretis, Gorski, Tesi, Morelli, Bora, Doni, Verrecchia, Tonelli, Fagà, Bianchi, Ronchi, Low, Müller, Guccione, Campaner, Amati: "Selective transcriptional regulation by Myc in cellular growth control and lymphomagenesis." in: Nature, Vol. 511, Issue 7510, pp. 488-92, (2014) (PubMed).

Fereres, Simón, Mohd-Sarip, Verrijzer, Busturia: "dRYBP counteracts chromatin-dependent activation and repression of transcription." in: PLoS ONE, Vol. 9, Issue 11, pp. e113255, (2014) (PubMed).

Putiri, Tiedemann, Liu, Choi, Robertson: "Impact of human MLL/COMPASS and polycomb complexes on the DNA methylome." in: Oncotarget, Vol. 5, Issue 15, pp. 6338-52, (2014) (PubMed).

Dhimolea, Wadia, Murray, Settles, Treitman, Sonnenschein, Shioda, Soto: "Prenatal exposure to BPA alters the epigenome of the rat mammary gland and increases the propensity to neoplastic development." in: PLoS ONE, Vol. 9, Issue 7, pp. e99800, (2014) (PubMed).

Konsavage, Yochum: "The myc 3' wnt-responsive element suppresses colonic tumorigenesis." in: Molecular and cellular biology, Vol. 34, Issue 9, pp. 1659-69, (2014) (PubMed).

Asmar, Hother, Kulosman, Treppendahl, Nielsen, Ralfkiaer, Pedersen, Møller, Ralfkiaer, de Nully Brown, Grønbæk: "Diffuse large B-cell lymphoma with combined TP53 mutation and MIR34A methylation: Another "double hit" lymphoma with very poor outcome?" in: Oncotarget, Vol. 5, Issue 7, pp. 1912-25, (2014) (PubMed).

DAnselmi, Masiello, Cucina, Proietti, Dinicola, Pasqualato, Ricci, Dobrowolny, Catizone, Palombo, Bizzarri: "Microenvironment promotes tumor cell reprogramming in human breast cancer cell lines." in: PLoS ONE, Vol. 8, Issue 12, pp. e83770, (2014) (PubMed).

Kelso, Baumgart, Eickhoff, Albert, Antrecht, Lemcke, Klebl, Meisterernst: "Cyclin-dependent kinase 7 controls mRNA synthesis by affecting stability of preinitiation complexes, leading to altered gene expression, cell cycle progression, and survival of tumor cells." in: Molecular and cellular biology, Vol. 34, Issue 19, pp. 3675-88, (2014) (PubMed).

Belyea, Xu, Pentz, Medrano, Li, Hu, Turner, Legallo, Jones, Tario, Liang, Gross, Sequeira-Lopez, Gomez: "Identification of renin progenitors in the mouse bone marrow that give rise to B-cell leukaemia." in: Nature communications, Vol. 5, pp. 3273, (2014) (PubMed).

Amatori, Ballarini, Faversani, Belloni, Fusar, Bosari, Pelicci, Minucci, Fanelli: "PAT-ChIP coupled with laser microdissection allows the study of chromatin in selected cell populations from paraffin-embedded patient samples." in: Epigenetics & chromatin, Vol. 7, pp. 18, (2014) (PubMed).

Kumar, Duester: "Retinoic acid controls body axis extension by directly repressing Fgf8 transcription." in: Development (Cambridge, England), Vol. 141, Issue 15, pp. 2972-7, (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).

Details zu Histone 3

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. 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