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Merck
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Key Documents

D5567

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Sinônimo(s):

Anti-H3K9me2

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

IgG fraction of antiserum

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

peso molecular

antigen 17 kDa

reatividade de espécies

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

técnica(s)

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

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

dimethylation (Lys9)

Descrição geral

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.

Especificidade

ChIP validated

Imunogênio

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.

Aplicação

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

Ações bioquímicas/fisiológicas

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.

forma física

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

nwg

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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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.
Immunity, 44(6), 1271-1283 (2016-06-19)
T helper 17 (Th17) cells are prominently featured in multiple autoimmune diseases, but the regulatory mechanisms that control Th17 cell responses are poorly defined. Here we found that stimulation of OX40 triggered a robust chromatin remodeling response and produced a
J Nakayama et al.
Science (New York, N.Y.), 292(5514), 110-113 (2001-04-03)
The assembly of higher order chromatin structures has been linked to the covalent modifications of histone tails. We provide in vivo evidence that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions

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