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Merck

D5567

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Sinónimos:

Anti-H3K9me2

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About This Item

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

origen biológico

rabbit

Nivel de calidad

conjugado

unconjugated

forma del anticuerpo

IgG fraction of antiserum

tipo de anticuerpo

primary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

mol peso

antigen 17 kDa

reactividad de especies

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

técnicas

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

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

dimethylation (Lys9)

Descripción general

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.

Especificidad

ChIP validated

Inmunógeno

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.

Aplicación

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

Acciones bioquímicas o 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.

Cláusula de descargo de responsabilidad

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 clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

nwg

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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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
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
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
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
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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