Millipore Anti-Trimethyl-Histone H3 (Lys4) Rabbit Ab

Millipore Upstate Anti-trimethyl-Histone H3 (Lys4) Rabbit Antibody, 100 uL Net Content, Polyclonal, Trimethylated (Lys4) Epitope, Rabbit Host Species, Affinity Purified, Liquid Form, 7.4 pH, 2 to 8 deg C, Methylation Modification, Human, Vertebrates Species Reactivity. Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. Histone modifications regulate DNA transcription, repair, recombination and replication. Two molecules of each of the four core histones (H2A, H2B, H3 and H4) form an octamer, around which DNA is wrapped in repeating units, called nucleosomes, which limits DNA accessibility to the cellular machineries, which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code and nucleosome remodeling. Histone H3 contains a main globular domain and a long N-terminal tail and is involved with the structure of the nucleosomes of the beads on a string structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. H3K4me3 modifications are reported to occur consistently at transcription start sites and H3K4me3 domain is associated with higher transcription activity and cell identity in pre-implantation development and in the process of deriving embryonic stem cells from the inner cell mass and trophoblast stem cells from the trophectoderm (Ref.: Liu, X., et al (2016). Nature 537(7621), 558-562) (Additional S&H or Hazmat Fees May Apply) - Mill