Histone H3 (22-30) K27Me3 Ac-TKAAR-[K(Me)3]-SAP-amide


Histone H3 (22-30)-K27Me3 is derived from Histone 3 (H3) which is one of the four core histones fundamental for compacting eukaryotic DNA into the nucleosome. The lysine 27 has been trimethylated.

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Catalogue number crb1000664
Sequence (one letter code) Ac-TKAAR-[K(Me)3]-SAP-amide
Sequence (three letter code) Acetyl-Thr-Lys-Ala-Ala-Arg-[Lys(Me)3]-Ser-Ala-Pro-NH2
Molecular Weight 1012.6
Purity >95%
Storage -20°C

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. Bio-chem. (7) 446–448. PMID: 15992689

Henneman et al (2018) Structure and function of archaeal histones. PLOS. DOI: https://doi.org/10.1371/journal.pgen.1007582

Kim et al (2013) Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes. Mol. Cell. Bio. (24) 4936 PMID: 24126056

The Histone H3 (22-30)-K27Me3 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. Both 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. 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. Due to histones containing a large number of lysine and arginine residues they have a positive net charge which interacts in an electrostatic manner 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 function to alter to change the positioning of the nucleosome, allowing the DNA it to be either available to the transcription machinery or inaccessible.

The Histone H3 (20-36)’s lysine 27 has been trimethylated which is usually a marker of repressive chromatin. H3K27 trimethylation also prevents H3 from interacting with SET1-like complexes, thus inhibiting the trimethylation of H3K4.

Histone H3 (22-30) K27Me3

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