Description
Histone H3K27Me3 (21-44)-GK-biotin is a peptide fragment of histone H3 that corresponds to amino acid residues 22-45 of the human histone H3.1 and 3.2 sequences. It is trimethylated at lysine 27 and biotinylated via a C-terminal GK linker. Trimethylation of histone H3 at lysine 27 is associated with gene silencing.1 It is involved in tumor progression through its regulation by enhancer of zeste homolog 2 (EZH2) and transcriptional repression of tumor suppressor genes.2,3 Levels of H3K27Me3 are reduced in 293 T-REx cells containing EEDR236T and SUZ12G610V mutations and in lymphoblastoid cells isolated from patients with Weaver syndrome, a rare overgrowth disorder characterized by EZH2, EED, or SUZ12 mutations, cancer susceptibility, and various distinctive physical features.4 Histone H3K27Me3 (21-44)-GK-biotin has been used as a substrate for histone lysine demethylases (KDMs) to determine substrate specificity.5WARNING This product is not for human or veterinary use.
References
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10.1016/j.tig.2015.11.001[2] Z WU. Polycomb protein EZH2 regulates cancer cell fate decision in response to DNA damage[J]. Cell Death and Differentiation, 2011, 18 11: 1771-1779. DOI:
10.1038/cdd.2011.48[3] LU GAN. Epigenetic regulation of cancer progression by EZH2: from biological insights to therapeutic potential.[J]. Biomarker Research, 2018, 6: 10. DOI:
10.1186/s40364-018-0122-2[4] ERI IMAGAWA. Mutations in genes encoding polycomb repressive complex 2 subunits cause Weaver syndrome[J]. Human Mutation, 2017, 38 6: 637-648. DOI:
10.1002/humu.23200[5] TUOMAS LAUKKA . Cancer-associated 2-oxoglutarate analogues modify histone methylation by inhibiting histone lysine demethylases[J]. Journal of Molecular Biology, 2018, 430 18: Pages 3081-3092. DOI:
10.1016/j.jmb.2018.06.048