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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

Synonym(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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

7E7-H12, monoclonal

form

buffered aqueous solution

mol wt

antigen ~17 kDa

species reactivity

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

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

monomethylation (Lys9)

Gene Information

human ... H3C1(8350)

General description

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.

Immunogen

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.

Biochem/physiol Actions

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.

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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