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Merck
Összes fotó(6)

Fontos dokumentumok

07-360

Sigma-Aldrich

Anti-acetyl-Histone H3 (Lys27) Antibody

serum, Upstate®

Szinonimák:

H3K27Ac, Histone H3 (acetyl K27)

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
klón:
polyclonal
application:
ChIP
DB
WB
faj reaktivitás:
human, vertebrates, Saccharomyces cerevisiae
technika/technikák:
ChIP: suitable (ChIP-seq)
dot blot: suitable
western blot: suitable
citations:
171

biológiai forrás

rabbit

Minőségi szint

antitest forma

serum

antitest terméktípus

primary antibodies

klón

polyclonal

faj reaktivitás

human, vertebrates, Saccharomyces cerevisiae

faj reaktivitás (homológia által előrejelzett)

yeast (based on 100% sequence homology)

gyártó/kereskedő neve

Upstate®

technika/technikák

ChIP: suitable (ChIP-seq)
dot blot: suitable
western blot: suitable

izotípus

IgG

NCBI elérési szám

UniProt elérési szám

kiszállítva

dry ice

célzott transzláció utáni módosítás

acetylation (Lys27)

Géninformáció

human ... HIST1H3F(8968)

Általános leírás

Histone H3 (UniProt: P61830) is encoded by the HHT1 (also known as YBR010W, YBR0201, HHT2, SIN2, YNL031C, N2749) gene (Gene ID: 852295) in yeast. Histone H3 is a core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histone H3 can undergo various post-translational modifications that either activate or repression gene expression. Histone H3 can undergo mon-, di-, or trimethylation. Trimethylated H3K27 is shown to be tightly associated with inactive gene promoters and monomethylated H3K27 is associated with active promoters. The dimethylated H3K27 has a distribution pattern similar to H3K27. Histone H3 can also undergo acetylation at Lys9, 14, 18, 23, 27 and 56. Acetylation of histone H3 leads to transcriptional activation. Acetylation of histone defines the openness of chromatin as acetylated histones cannot pack as well together as deacetylated histones. H3K27ac as an important enhancer mark that can distinguish between active and poised enhancer elements and enhancer proximal genes that lack H3K27ac enrichment display lower expression levels compared with the average enhancer proximal gene. It is shown that amounts of H3K27ac is gradually declines fom the earliest pronuclear stage to 8-cell stage, corresponding to the major embryonic genome activation (EGA), followed by re-acetylation of H3K27 from the morula stage onwards accompanying the first cell lineage specification in IVF embryos. In Drosophila, H3K27ac is present at high levels in early embryos and declines after 4 hours as the level of trimethylated H3K27 increases. (Ref.: Creyghton, MP et al. ( ). Proc. Natl. Acad. Sci. USA 107(50); 21931-21936; Tie, F et al (2009). Dvelopment 136 (18); 3131-3141)..

Egyediség

Recognizes Histone H3 acetylated on lysine 27.

Immunogén

Epitope: Lys27
KLH-conjugated linear peptide corresponding to 11 amino acids from the N-terminal region of human histone H3 acetylated on Lysine 27.

Alkalmazás

ChIP-seq Analysis: Chromatin immunoprecipitation was performed using the Magna ChIP HiSens kit (cat# 17-10460), 2 µl of anti-acetyl-Histone H3 (Lys27) antibody (cat# 07-360), 20 µL Protein A/G beads, and 1e6 crosslinked HeLa cell chromatin followed by DNA purification using magnetic beads. Libraries were prepared from Input and ChIP DNA samples using standard protocols with Illumina barcoded adapters, and analyzed on Illumina HiSeq instrument. An excess of fourteen million reads from FastQ files were mapped using Bowtie (http://bowtie-bio.sourceforge.net/manual.shtml) following TagDust (http://genome.gsc.riken.jp/osc/english/dataresource/) tag removal. Peaks were identified using MACS (http://luelab.dfci.harvard.edu/MACS/), with peaks and reads visualized as a custom track in UCSC Genome Browser (http://genome.ucsc.edu) from BigWig and BED files. The highest 25% of peaks identified in the 07-360 dataset showed 96% overlap with peaks identified in the ENCODE H3K27Ac BROAD Histone track for HeLa S3.
Anti-acetyl-Histone H3 (Lys27) Antibody is a rabbit polyclonal antibody for detection of Histone H3 acetylated on lysine 27. Also known as Anti-H3K27ac this antibody is published in peer reviewed journals and is specificity verified by dot blot (DB) and validated in ChIP, ChIP-seq, WB, DB, Mplex.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Histones

Minőség

Evaluated by Western Blotting in acid extract of HeLa cells treated with 5 mM sodium butyrate.

Western Blotting Analysis: A 1:5,000 dilution of this antibody detected acetyl-Histone H3 (Lys27) in acid extract of HeLa cells treated with 5 mM sodium butyrate.cells

Cél megnevezése

17 kDa

Fizikai forma

Rabbit polyclonal antiserum with 0.05% sodium azide and 30% glycerol.
Unpurified

Tárolás és stabilitás

Maintain for 2 years at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Analízis megjegyzés

Control
Acid extracted proteins from HeLa cells treated with sodium butyrate

Egyéb megjegyzések

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Jogi információk

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Jogi nyilatkozat

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Dokumentumtár megtekintése

Az ügyfelek ezeket is megtekintették

Quantitative mass spectrometry of histones H3.2 and H3.3 in Suz12-deficient mouse embryonic stem cells reveals distinct, dynamic post-translational modifications at Lys-27 and Lys-36.
Jung, HR; Pasini, D; Helin, K; Jensen, ON
Molecular and Cellular Proteomics null
A global change in RNA polymerase II pausing during the Drosophila midblastula transition.
Chen, K; Johnston, J; Shao, W; Meier, S; Staber, C; Zeitlinger, J
eLife null
Jean-Philippe Lambert et al.
Journal of proteomics, 118, 81-94 (2014-10-05)
Mapping protein-protein interactions for chromatin-associated proteins remains challenging. Here we explore the use of BioID, a proximity biotinylation approach in which a mutated biotin ligase (BirA*) is fused to a bait of interest, allowing for the local activation of biotin
Sascha Venturelli et al.
The Plant cell, 27(11), 3175-3189 (2015-11-05)
To secure their access to water, light, and nutrients, many plant species have developed allelopathic strategies to suppress competitors. To this end, they release into the rhizosphere phytotoxic substances that inhibit the germination and growth of neighbors. Despite the importance
Hiromu Tanaka et al.
The Journal of biological chemistry, 291(12), 6316-6330 (2016-01-21)
B lymphocyte-induced maturation protein 1 (Blimp-1) encoded by Prdm1 is a master regulator of plasma cell differentiation. The transcription factor Bach2 represses Blimp-1 expression in B cells to stall terminal differentiation, by which it supports reactions such as class switch

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