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Merck
모든 사진(6)

주요 문서

05-1242

Sigma-Aldrich

Anti-trimethyl-Histone H3 (Lys9) Antibody, clone 6F12-H4

clone 6F12-H4, from mouse

동의어(들):

H3K9me3, Histone H3 (tri methyl K9), H3 histone family, member T, histone 3, H3, histone cluster 3, H3

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About This Item

UNSPSC 코드:
12352203
eCl@ss:
32160702
NACRES:
NA.41

생물학적 소스

mouse

Quality Level

항체 형태

purified antibody

항체 생산 유형

primary antibodies

클론

6F12-H4, monoclonal

종 반응성

mouse, human

기술

ChIP: suitable (ChIP-seq)
dot blot: suitable
immunofluorescence: suitable
inhibition assay: suitable (peptide)
western blot: suitable

동형

IgG1κ

NCBI 수납 번호

UniProt 수납 번호

배송 상태

wet ice

타겟 번역 후 변형

trimethylation (Lys9)

유전자 정보

human ... H3C1(8350)
mouse ... H3C1(360198)

일반 설명

Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Subsequently, 146 base pairs of DNA are wrapped around the octamer, forming a nucleosome, the basic subunit of chromatin. Histone modifications regulate DNA transcription, repair, recombination, and replication. The most commonly studied modifications are acetylation, phosphorylation, methylation, and ubiquitination. These modifications can alter local chromatin architecture, or recruit trans-acting factors that recognize specific histone modifications (the "histone code" hypothesis). Trimethylation of histone H3 on Lys9 (H3K9me3) is one of the most highly studied epigenetic marks. H3K9me3 functions in the repression of euchromatic genes, and in epigenetic control of heterochromatin assembly, most likely via acting as a recognition motif for the binding of chromatin-associated proteins, such as Swi6 or HP1α/β. The enzymes responsible for H3K9me3 formation are SUV39H1 and SUV39H2.

특이성

Based on sequence homology, broad species cross-reactivity is expected with all mammals, Drosophila, Xenopus, and Arabidopsis.

애플리케이션

Chromatin Immunoprecipitation (ChIP):
Representative data from a previous lot. Sonicated 3T3 L1 chromatin was subjected to chromatin immunoprecipitation using anti- trimethyl-histone H3 (Lys9) and the Magna ChIP G (Cat. #17-611) Kit. Successful immunoprecipitation of trimethylhistone H3 (Lys9) associated DNA fragments was verified by qPCR using primers flanking the p16 promoter.

Peptide Inhibition Analysis:
Peptide blocking assay demonstrates distinct preference of the antibody for the trimethyl form vs. the dimethyl form.


Chromatin Immunoprecipitation (ChIP):
ChIP analysis of known chromosomal Suv39h targets (H3K9me3 in major satellites, mouseES cells).


Dot Blot Analysis:
Dot-blot analysis demonstrating specificity of anti-H3K9me3, clone 6F12-H4 for trimethyl Lys9 of histone H3.
Use Anti-trimethyl-Histone H3 (Lys9) Antibody, clone 6F12-H4 (mouse monoclonal antibody) validated in ChIP, PIA, IF, DB, ChIP-seq, WB to detect trimethyl-Histone H3 (Lys9) also known as H3K9me3, Histone H3 (tri methyl K9).

품질

Routinely evaluated by Western Blot on HeLa acid extracts.

Western Blot Analysis: A 0.5 – 5 μg dilution of this lot detected trimethyl histone H3 (Lys9) in HeLa acid extracts.

표적 설명

~17 kDa

물리적 형태

Format: Purified

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

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문서 라이브러리 방문

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Molecular medicine reports, 9(6), 2283-2292 (2014-04-11)
The present study aimed to investigate the role of histone modification and DNA methylation in epidermal growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1) silencing in gastric cancer (GC). In the present study, four GC cell lines, and 45 paired
Kirk J McManus et al.
The Journal of biological chemistry, 281(13), 8888-8897 (2005-12-24)
Histone methylation is unique among post-translational histone modifications by virtue of its stability. It is thought to be a relatively stable and heritable epigenetic mark for gene-specific regulation. In this study, we use quantitative in situ approaches to investigate the
Cai Qi et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 34(13), 4494-4508 (2014-03-29)
Dendritic arborization is one of the key determinants of precise circuits for information processing in neurons. Unraveling the molecular mechanisms underlying dendrite morphogenesis is critical to understanding the establishment of neuronal connections. Here, using gain- and loss-of-function approaches, we defined

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