Anti-Dimethyl-Histone H3 (Lys27) Rabbit mAb

WB, IHC-P, ICC/IF

Histone H3

Store at -20°C. Avoid freeze/thaw cycles.

Stable for 12 months from date of receipt/reconstitution.

The ε-amino lysine methylation of proteins is an important reversible modification controlling protein activity. The amino-terminal tails of core histones undergo lysine methylation in multiple sites, termed as “histone code” or “epigenetic code”. Lysine methylation in core histones is a major determinant for theformation of active and inactive regions of the genome and therefore playsvital roles in multiple cellular events. In most species, lysine methylationoccurs primarily on histones H3 (Lys4, 9, 27, 36, 79), and H4 (Lys20) and hasbeen implicated in both transcriptional activation and silencing. Methylation in histones modulated by specific histone methyltransferases (HMTs) and histone demethylases (HDMs). The level of methyllysineis found impaired in the pathologies of cancers and other diseases, therefore, enzymes regulating histone lysine methylation have become promising targets for anti-cancer drugs. 

PBS, Glycerol, BSA

Lys27

The ε-amino lysine methylation of proteins is an important reversible modification controlling protein activity. The amino-terminal tails of core histones undergo lysine methylation in multiple sites, termed as “histone code” or “epigenetic code”. Lysine methylation in core histones is a major determinant for theformation of active and inactive regions of the genome and therefore playsvital roles in multiple cellular events. In most species, lysine methylationoccurs primarily on histones H3 (Lys4, 9, 27, 36, 79), and H4 (Lys20) and hasbeen implicated in both transcriptional activation and silencing. Methylation in histones modulated by specific histone methylases (HMTs) and histone demethylases (HDMs). The level of methyllysineis found impaired in the pathologies of cancers and other diseases, therefore, enzymes regulating histone lysine methylation have become promising targets for anti-cancer drugs.