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.
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)
Chromatin modifications and their function
Kouzarides, Tony
Cell, 128(4), 693-705 (2007)
Cancer epigenetics: from mechanism to therapy
Dawson M A and Kouzarides T
Cell, 150(1), 12-27 (2012)
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