Histone H3 (di methyl K27) Recombinant Rabbit Monoclonal Antibody - BSA and Azide free [PSH05-88] (HA751035)

UNIPROT #

P68431

PROTEIN NAME

Di-Methyl-Histone H3 (K27)

SYNONYMS

H3 histone family member E pseudogene antibody;H3 histone family, member A antibody;H3/A antibody;H31_HUMAN antibody;H3F3 antibody;H3FA antibody;Hist1h3a antibody;HIST1H3B antibody;HIST1H3C antibody;HIST1H3D antibody;HIST1H3E antibody;HIST1H3F antibody;HIST1H3G antibody;HIST1H3H antibody;HIST1H3I antibody;HIST1H3J antibody;HIST3H3 antibody;histone 1, H3a antibody;Histone cluster 1, H3a antibody;Histone H3 3 pseudogene antibody;Histone H3.1 antibody;Histone H3/a antibody;Histone H3/b antibody;Histone H3/c antibody;Histone H3/d antibody;Histone H3/f antibody;Histone H3/h antibody;Histone H3/i antibody;Histone H3/j antibody;Histone H3/k antibody;Histone H3/l antibody;H3K27me2

SUBCELLULAR LOCATION

Nucleus, Chromosome.

FUNCTION

The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination. Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development. Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing. Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5). The discovery of histone demethylases, such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1, has shown that methylation is a reversible epigenetic marker.