Anti-Human Histone H3 Nonmethyl (Lys9) - Purified No Carrier Protein (H457-GRP)

Nucleosomes are the basic building blocks of chromatin1. Nucleosomes are composed of ~147 bp of DNA wrapped around a histone octamer. This octamer is composed of a central (H3-H4) tetramer that is flanked by two H2A-H2B dimers. Histones H2B and H4 are relatively conserved, but many variants of H2A and H3 exist. H3 variants in humans include H3.1, H3.2, H3.3, H3t/H3.4, H3.5, H3.Y, H3.X, CENP-A, H3.6, H3.7 and H3.8. Both H3.1 and H3.2, which differ by a single amino acid at residue 96, are expressed in S-phase during replication. In contrast, H3.3 is expressed throughout interphase and is enriched over actively transcribed genes and repetitive DNA elements. The other variants are less studied, but all histones are heavily regulated at transcriptional and post-translational levels, including methylation, acetylation, and phosphorylation. Histone modification status has a direct biophysical effect on gene expression and chromatin structure. Lysines may be unmethylated (me0), monomethylated (me1), demethylated (me2), and trimethylated (me3), each with its own regulatory effects. 9B1-2G6 was raised against a synthetic, branched, KLH-conjugated peptide corresponding to human unmethylated Histone H3 amino acids surrounding Lys9. 9B1-2G6 targets H3 when unmethylated (me0) at Lys9. This antibody is also known as the Histone H3K9me0 antibody.