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H7162

Sigma-Aldrich

Anti-methyl-Histone H3 (Me-Lys9) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-H3K9me1
MDL number:
MFCD04974759
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

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

technique(s)

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

UniProt accession no.

P68431

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

monomethylation (Lys9)

Gene Information

human ... H3F3A(3020) , H3F3B(3021) , HIST1H3A(8350) , HIST1H3B(8358) , HIST1H3C(8352) , HIST1H3D(8351) , HIST1H3E(8353) , HIST1H3F(8968) , HIST1H3G(8355) , HIST1H3H(8357) , HIST1H3I(8354) , HIST1H3J(8356) , HIST2H3A(333932) , HIST2H3C(126961) , HIST3H3(8290)
mouse ... H3f3a(15078) , H3f3b(15081) , Hist1h3a(360198) , Hist1h3b(319150) , Hist1h3c(319148) , Hist1h3d(319149) , Hist1h3e(319151) , Hist1h3f(260423) , Hist1h3g(97908) , Hist1h3h(319152) , Hist1h3i(319153) , Hist2h3b(319154) , Hist2h3c1(15077) , Hist2h3c2(97114)
rat ... H3f3b(117056)

General description

Histones are proteins that form the nucleosome along with DNA. A nucleosome consists of core histone octamers made of two heterodimers of H2A and H2B along with two heterodimers of H3 and H4. This octamer is bound by the DNA and H1 protein. The HIST3H3 gene is mapped on the human chromosome at 1q42.13.

Specificity

Anti-Methyl-Histone H3 [Me-Lys9] recognizes histone H3 methylated on Lys9.

Immunogen

synthetic methylated peptide corresponding to amino acids 7-20 [Me-Lys9] of human histone H3. The sequence is identical in many species.

Application

Anti-methyl-Histone H3 (Me-Lys9) antibody produced in rabbit may be used in immunoblotting.

Biochem/physiol Actions

Histones H3 and H4 are the predominant histones modified by methylation and are highly methylated in mammalian cells. 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, Lys-4, Lys-9 and Lys-27 are the preferred sites of methylation. Methylation of H3 at Lys-9 is a modification intrinsically linked to epigenetic silencing and heterochromatin assembly. Histone H3 is methylated at Lys-9 by site-specific H3 methyltransferases (HMTases) and generates a binding site for heterochromatin protein 1 (HP1).

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots at −20 °C. Repeated freezing and thawing is not recom-mended. Storage in frost-free freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

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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Emanuely Silva Chrun et al.
Pathology, research and practice, 213(11), 1329-1339 (2017-09-09)
Among the epigenetic changes, histone acetylation has been recognized as a fundamental process that strongly affects gene expression regulation. Disrupt of this phenomenon has been linked to carcinogenesis. In this review, we analysed studies reporting the process of histone modification
B D Strahl et al.
Nature, 403(6765), 41-45 (2000-01-19)
Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of
J C Rice et al.
Current opinion in cell biology, 13(3), 263-273 (2001-05-10)
Post-translational addition of methyl groups to the amino-terminal tails of histone proteins was discovered more than three decades ago. Only now, however, is the biological significance of lysine and arginine methylation of histone tails being elucidated. Recent findings indicate that
Thomas H A Ederveen et al.
Biochimica et biophysica acta, 1809(10), 577-586 (2011-07-26)
Histones are highly basic, relatively small proteins that complex with DNA to form higher order structures that underlie chromosome topology. Of the four core histones H2A, H2B, H3 and H4, it is H3 that is most heavily modified at the

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