Biotin-Histone H3 (14-34) pT22 K23Me3
Histone 3 (H3) is one of the four core histones fundamental for compacting eukaryotic DNA into the nucleosome. The histone tail fragment (14-34) is N terminal biotinylated, lysine 23 has been tri-methylated, and threonine 22 has been phosphorylated (pT22 K23Me3).
Catalogue number crb1000344 Molecular Weight 2456.3 Sequence (one letter code)
Sequence (three letter code)
Purity >95% References
Nagarama et al., (2006). Biological functions of biotinylated histones. J. Nutr.Biochem., 7: 446. PMID: 15992689.
Henneman et al., (2018). Structure and function of archaeal histones. PLoS Genet., 14(9): e1007582. DOI: https://doi.org/10.1371/journal.pgen.1007582.
Su et al., (2016). Reader domain specificity and lysine demethylase-4 family function. Nat. Comms., 7(1): 1. DOI: 10.1038/ncomms13387.
Manufactured in: United Kingdom
H3 is a core component of the nucleosome, functioning in DNA compaction and availability to transcription machinery. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodelling. Similar to the other core histone, H3 has a globular domain and a flexible N-terminal domain, “histone tail” which can undergo modifications such as acetylation, methylation, phosphorylation and ubiquitination. There is a wealth of data recording these modifications but understanding their significance is not as clear. In Caenorhabditis elegans H3K23me3 can be induced by exogenous dsRNA and this modification can persist for four generations after the dsRNA exposure has been stopped. H3K23me3 is enriched in C. elegans heterochromatic regions, the histone methyltransferase SET-32, methylates H3K23 in vitro.
A 20-mer fragment of the N terminal histone tail is provided here with threonine 22 phosphorylated and lysine 23 tri-methylated (pT22 K23Me3) with an N terminal biotin label attached. The biotin label should allow for easy use in detection by fluorescence microscopy, ELISA or western blots. Alternatively, it can be purified for protein-protein interactions with the appropriate affinity purification protocol.