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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

Synonyme(s) :

Anti-H3K9me2

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 17 kDa

Espèces réactives

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

dimethylation (Lys9)

Description générale

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.

Spécificité

ChIP validated

Immunogène

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
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
T Jenuwein et al.
Science (New York, N.Y.), 293(5532), 1074-1080 (2001-08-11)
Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or
S Rea et al.
Nature, 406(6796), 593-599 (2000-08-19)
The organization of chromatin into higher-order structures influences chromosome function and epigenetic gene regulation. Higher-order chromatin has been proposed to be nucleated by the covalent modification of histone tails and the subsequent establishment of chromosomal subdomains by non-histone modifier factors.

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