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SAB4200625

Sigma-Aldrich

Anti-Methyl-Histone H3 (Me-Lys9)(H3K9me1) antibody, Mouse monoclonal

clone 7E7-H12, purified from hybridoma cell culture

Synonyme(s) :

9430068D06RIK, H3.3A, H3.3B, H3F3, H3F3A, H3F3A/H3F3B, H3F3B, HISTONE 3B, LOC100045490, RP11−396C23.1, wu:fb58e10, zgc:56193, zgc:86731

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

7E7-H12, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~17 kDa

Espèces réactives

human

Concentration

~1 mg/mL

Technique(s)

immunoblotting: 2.5-5 μg/mL using human HeLa cells.
immunocytochemistry: 2.5-5 μg/mL using human HeLa cells.

Isotype

IgG1

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

monomethylation (Lys9)

Informations sur le gène

human ... H3C1(8350)

Description générale

Anti-Methyl-Histone H3 (Me-Lys9) (H3K9me1) antibody, Mouse Monoclonal (mouse IgG1 isotype) is derived from the hybridoma 7E7-H12 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a methylated (Me-Lys9) peptide corresponding to the N-terminus of human histone H3, conjugated to KLH.

Immunogène

Methylated (Me-Lys9) peptide corresponding to the N-terminus of human histone H3, conjugated to KLH.

Application

Anti-Methyl-Histone H3 (Me-Lys9) (H3K9me1) antibody has been used in immunoblotting and immunocytochemistry.

Actions biochimiques/physiologiques

Histones are subjected to extensive covalent modifications that play an important role in development and in cancer. These modifications include phosphorylation, methylation, acetylation and ubiquitination. Histones H3 and H4 are the predominant histones modified by methylation and are highly methylated in mammalian cells. Histone methylation, like acetylation, is a complex, dynamic process involving several processes, including transcriptional regulation, chromatin condensation, mitosis, and heterochromatin assembly. Moreover, lysine residues can be mono-, di-, and tri-methylated, adding further complexity to the regulation of chromatin structure. Conserved lysine residues in the N-terminal tail domains of histone H3, Lys4, Lys9 and Lys27 are the preferred sites of methylation. Methylation of H3 at Lys9 is a modification intrinsically linked to epigenetic silencing and heterochromatin assembly.

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)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena
Strahl B D, et al.
Proceedings of the National Academy of Sciences of the USA, 96(26), 14967-14972 (1999)
Cancer epigenetics: from mechanism to therapy
Dawson M A and Kouzarides T
Cell, 150(1), 12-27 (2012)
B D Strahl et al.
Proceedings of the National Academy of Sciences of the United States of America, 96(26), 14967-14972 (1999-12-28)
Studies into posttranslational modifications of histones, notably acetylation, have yielded important insights into the dynamic nature of chromatin structure and its fundamental role in gene expression. The roles of other covalent histone modifications remain poorly understood. To gain further insight
Mark A Dawson et al.
Cell, 150(1), 12-27 (2012-07-10)
The epigenetic regulation of DNA-templated processes has been intensely studied over the last 15 years. DNA methylation, histone modification, nucleosome remodeling, and RNA-mediated targeting regulate many biological processes that are fundamental to the genesis of cancer. Here, we present the
Tony Kouzarides
Cell, 128(4), 693-705 (2007-02-27)
The surface of nucleosomes is studded with a multiplicity of modifications. At least eight different classes have been characterized to date and many different sites have been identified for each class. Operationally, modifications function either by disrupting chromatin contacts or
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