Histone H3 (1-20) K4Me3, K9Ac, pS10-GG-Biotin
Histone H3 (1 – 20) is derived from the histone tail. Lysine 4 of Histone H3 (1 – 20) K4Me3 has been tri-methylated, lysine 9 has been acetylated, and serine 10 has been phosphorylated and labelled with Biotin.
Catalogue number crb1001682 Molecular Weight 2814.5 Sequence (one letter code)
Sequence (three letter code)
Modifications Lysine 4 of Histone H3 (1 - 20) K4Me3 has been tri-methylated, lysine 9 has been acetylated, serine 10 has been phosphorylated and labelled with the Biotin. Purity >95% Storage -20°C References
Henneman et al., (2018). Structure and function of archaeal histones. PLoS Genet., 14(9): e1007582. DOI: https://doi.org/10.1371/journal.pgen.1007582.
Hyland et al., (2005). Insights into the Role of Histone H3 and Histone H4 Core Modifiable Residues in Saccharomyces cerevisiae. Mol. Cell. Bio., 22: 10060. PMID: 16260619.
Kothapalli et al., (2006). Biological functions of biotinylated histones. J. Nutr. Biochem., (7): 446. PMID: 15992689.
Manufactured in: United Kingdom
Histone H3 (1 – 20) K4Me3 is derived from Histone 3 (H3), which is one of the four core histones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core. H4 and H3 are highly conserved and perform roles in binding to segments of DNA which enter and leave the nucleosome and in chromatin formation. Like 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. Due to histones containing many lysine and arginine residues, they have a positive net charge which interacts electrostatically with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone-modifying enzymes which target histone proteins. Both processes alter the positioning of the nucleosome, allowing the DNA to be either available or inaccessible to the transcription machinery.
Histone tails can undergo multiple modifications, including acetylation, methylation, ubiquitylation and sumoylation. The modification pattern is believed to alter chromatin function/structure. Lysine 4 of histone H3 (1 – 20) K4Me3 has been tri-methylated, lysine 9 has been acetylated, and serine 10 has been phosphorylated and labelled with Biotin. This peptide can be used to study the function of this pattern on chromatin availability and histone effectors via crystallisation, pull-down assays and protein blots.
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