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ANTI-METHYL-HISTONE H3 (ME-LYS9)(H3K9&
Кат. №: SAB4200625-100UL
Производитель: Sigma-Aldrich
Кол-во:
Цена по запросу
Товар оформляется под заказ
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ANTI-METHYL-HISTONE H3 (ME-LYS9)(H3K9&
Кат. №: SAB4200625-100UL
Производитель: Sigma-Aldrich
Кол-во:
Цена по запросу
Товар оформляется под заказ
Кол-во:
Цена по запросу
Товар оформляется под заказ
Description_x000D_
General description_x000D_
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._x000D_
Immunogen_x000D_
Methylated (Me-Lys9) peptide corresponding to the N-terminus of human histone H3, conjugated to KLH._x000D_
Application_x000D_
Anti-Methyl-Histone H3 (Me-Lys9) (H3K9me1) antibody has been used in immunoblotting and immunocytochemistry._x000D_
Physical form_x000D_
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide._x000D_
Disclaimer_x000D_
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._x000D_
Biochem/physiol Actions_x000D_
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.
Related Categories
Alphabetical Index, Antibodies, MB-ME, Primary Antibodies conjugate
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