H3K27(Me) (15-34)

Product Name: H3K27(Me) (15-34)

Purity: 95%

Molar Mass: 1994.3

Chemical Formula: C85H152N30O25

Storage: Store at -20??

Sequence: APRKQLATKAARKSAPATGG

Application: H3K27(Me) (15-34) is a synthetic peptide corresponding to the amino acids 15-34 of histone H3, specifically methylated at the lysine 27 (K27) residue. This post-translational modification plays a pivotal role in the regulation of gene expression by contributing to the formation of repressive chromatin structures. H3K27 methylation is catalyzed by the Polycomb Repressive Complex 2 (PRC2) and is crucial for maintaining stem cell pluripotency and differentiation, as well as for the development and progression of various cancers. The H3K27(Me) (15-34) peptide is a valuable tool in epigenetic research, facilitating studies on chromatin dynamics, gene regulation, and the development of targeted epigenetic therapies.

Current Research:

H3K27(Me) (15-34) is a synthetic peptide corresponding to amino acids 15 to 34 of histone H3, incorporating methylation at lysine 27 (K27). This modification serves as a repressive chromatin mark, playing a pivotal role in gene silencing and the maintenance of cellular identity.
Role of H3K27 Methylation in Gene Regulation
Methylation at H3K27 is catalyzed by the Polycomb Repressive Complex 2 (PRC2), leading to transcriptional repression of target genes. This epigenetic mark is crucial for processes such as X-chromosome inactivation, genomic imprinting, and the suppression of developmental genes in stem cells.
Applications of H3K27(Me) (15-34) in Research
The H3K27(Me) (15-34) peptide is utilized as a substrate in studies investigating the activity of histone methyltransferases and demethylases. It aids in elucidating the mechanisms of enzymes that add or remove methyl groups at H3K27, thereby enhancing our understanding of epigenetic regulation.
Implications in Disease and Therapeutics
Aberrant methylation at H3K27 is implicated in various diseases, including cancer. Overexpression of PRC2 components can lead to excessive H3K27 methylation, resulting in the silencing of tumor suppressor genes. Conversely, loss of H3K27 methylation due to mutations in demethylases can activate oncogenes. Consequently, targeting the enzymes that modulate H3K27 methylation is being explored as a therapeutic strategy in oncology.
Conclusion
The H3K27(Me) (15-34) peptide serves as a valuable tool in epigenetic research, facilitating the study of histone modifications and their impact on gene expression. Understanding the dynamics of H3K27 methylation is essential for developing novel therapeutic approaches for diseases associated with epigenetic dysregulation.

Reference: Rai, A. N., Vargas, M. L., Wang, L., Andersen, E. F., Miller, E. L., & Simon, J. A. (2013). Elements of the polycomb repressor SU (Z) 12 needed for histone H3-K27 methylation, the interface with E (Z), and in vivo function. Molecular and cellular biology.