Anti-monomethyl Histone H3 (Lys79), clone RM147 Antibody clone RM147, from rabbit

Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Subsequently, 146 base pairs of DNA are wrapped around the octamer, forming a nucleosome, the basic subunit of chromatin. Histone modifications regulate DNA transcription, repair, recombination, and replication. The most commonly studied modifications are acetylation, phosphorylation, methylation, and ubiquitination. Lysine methylation occurs in three distinct states, having either one (me1), two (me2) or three (me3) methyl groups attached to the amine group of the lysine side chain. Methylation of Lysine 79 in Histone 3 acts as a marker of inactive chromatin regions. Methylation by Dot1 methylase on lysine-79 (Lys79) of Histone H3 is criticial for transcriptional silencing, and it is thought that silencing proteins such as Sir3 function by blocking Dot1 methylation.