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Merck
CN

D5567

Anti-dimethyl-Histone H3 (diMe-Lys9) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

别名:

Anti-H3K9me2

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ARR, ChIP, WB
Citations:
18
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biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 17 kDa

species reactivity

Drosophila, bovine, chicken, Arabidopsis thaliana, Caenorhabditis elegans, human, mouse, frog, rat

technique(s)

ChIP: suitable, microarray: suitable, western blot: 1:1,000-1:2,000 using whole extract of human epitheloid carcinoma HeLa cell line

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

dimethylation (Lys9)

General description

Histone methylation is a complex, dynamic process involved in a number of processes, including transcriptional regulation, chromatin condensation, mitosis and heterochromatin assembly. Conserved lysine residues in the N-terminal tail domains of histone H3, Lys4, Lys9 and Lys27 are the preferred sites of methylation. SET domain-, site-specific histone methyltransferases (HMTases) are involved in methylation of Lys9 in histone 3.

Immunogen

synthetic methylated peptide corresponding to amino acids 5-13 (diMe-Lys9) of human histone H3, conjugated to KLH. This sequence is identical in many species including mouse, rat, bovine, chicken, frog, Drosophila, C. elegans, tetrahymena, and Arabidopsis thaliana histone H3.

Application

Anti-dimethyl-Histone H3 (diMe-Lys9) antibody produced in rabbit has been used in immunoblotting and chromatin immunoprecipitation assay.

Biochem/physiol Actions

ChIP validated
Mono- and dimethylation of H3 at Lys9 are intrinsically linked to epigenetic silencing and heterochromatin assembly. Methylation of H3 at Lys9 generates a binding site for HP1 proteins, a family of heterochromatic adaptor proteins implicated in both gene silencing and in the organization of higher order chromatin.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

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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存储类别

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

常规特殊物品
低风险生物材料
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Jikai Cui et al.
Cell death & disease, 12(6), 501-501 (2021-05-20)
Regulatory T cells play a crucial role in orchestrating immune response and maintaining immune tolerance, and the expression of the Foxp3 gene is indispensable to the differentiation of regulatory T cells. IL-4 shows strong inhibitory effects on Foxp3 expression and
Noma K et al.
Science (New York, N.Y.), 293(5532), 1150-1155 (2001-08-11)
Eukaryotic genomes are organized into discrete structural and functional chromatin domains. Here, we show that distinct site-specific histone H3 methylation patterns define euchromatic and heterochromatic chromosomal domains within a 47-kilobase region of the mating-type locus in fission yeast. H3 methylated
A J Bannister et al.
Nature, 410(6824), 120-124 (2001-03-10)
Heterochromatin protein 1 (HP1) is localized at heterochromatin sites where it mediates gene silencing. The chromo domain of HP1 is necessary for both targeting and transcriptional repression. In the fission yeast Schizosaccharomyces pombe, the correct localization of Swi6 (the HP1
M Lachner et al.
Nature, 410(6824), 116-120 (2001-03-10)
Distinct modifications of histone amino termini, such as acetylation, phosphorylation and methylation, have been proposed to underlie a chromatin-based regulatory mechanism that modulates the accessibility of genetic information. In addition to histone modifications that facilitate gene activity, it is of
Xiang Xiao et al.
Nature communications, 6, 8266-8266 (2015-09-15)
Glucocorticoid-induced TNFR-related protein (GITR) is a costimulatory molecule with diverse effects on effector T cells and regulatory T cells (Tregs), but the underlying mechanism remains poorly defined. Here we demonstrate that GITR ligation subverts the induction of Foxp3(+) Tregs and

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