[Lys(Me3)27]-Histone H3 (23-34)

Product Name: [Lys(Me3)27]-Histone H3 (23-34)

Sequence One Letter Code: KAAR-K(Me3)-SAPATGG

Sequence Three Letter Code: H-Lys-Ala-Ala-Arg-Lys(Me3)-Ser-Ala-Pro-Ala-Thr-Gly-Gly-OH

Molecular Weight: 1157.4

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: [Lys(Me3)27]-Histone H3 (23–34) is a synthetic peptide corresponding to histone H3 residues 23–34 with site-specific trimethylation at lysine 27 (H3K27me3), a key repressive chromatin mark catalyzed by Polycomb Repressive Complex 2 (PRC2). This modification is essential for gene silencing, regulation of developmental gene expression, and maintenance of cell identity. Dysregulation of H3K27me3 is strongly associated with cancer, stem cell plasticity, and developmental disorders. This peptide is widely used in epigenetics research to investigate Polycomb-mediated repression, PRC2 activity, and histone–protein interactions. It is also suitable for binding assays, enzyme activity studies, and antibody validation, providing a reliable tool for studying chromatin dynamics and epigenetic regulation mechanisms.

Current Research: Epigenetic regulation of gene expression relies heavily on post-translational modifications of histone proteins, which shape chromatin structure and influence transcriptional outcomes. Among these modifications, trimethylation of lysine 27 on histone H3 (H3K27me3) is one of the most well-characterized repressive marks. [Lys(Me3)27]-Histone H3 (23–34) is a synthetic peptide designed to replicate this modification within a defined segment of the histone H3 sequence, providing a powerful tool for investigating chromatin silencing mechanisms, Polycomb group protein function, and epigenetic regulation. H3K27 Trimethylation and Gene Silencing H3K27me3 is a hallmark of transcriptionally repressed chromatin and plays a central role in controlling gene expression programs during development and differentiation. This modification is catalyzed by the Polycomb Repressive Complex 2 (PRC2), a multi-protein complex that includes key enzymatic components such as EZH2, which carries out the methyltransferase activity. Once established, H3K27me3 serves as a binding platform for additional Polycomb group proteins, particularly those in Polycomb Repressive Complex 1 (PRC1). These complexes work together to compact chromatin, inhibit transcriptional initiation, and maintain long-term gene silencing. This epigenetic mark is especially important for regulating genes involved in developmental pathways, lineage specification, and maintenance of cell identity, ensuring that genes inappropriate for a given cell type remain inactive. Structural Design of the Peptide The [Lys(Me3)27]-Histone H3 (23–34) peptide corresponds to amino acids 23 through 34 of the histone H3 N-terminal region. Within this sequence, lysine at position 27 is trimethylated, accurately reproducing the H3K27me3 modification found in chromatin. By isolating this specific modification within a short peptide, researchers can study its functional consequences in a controlled biochemical context. Synthetic histone peptides are particularly valuable because they allow precise interrogation of single modification states without interference from other histone marks. This defined structure makes the peptide well suited for analyzing how proteins recognize and respond to the H3K27me3 signal. Polycomb Complex Function and Chromatin Regulation The establishment and maintenance of H3K27me3 marks are tightly regulated by Polycomb group proteins. PRC2 catalyzes methylation of lysine 27, while PRC1 recognizes this modification and contributes to chromatin compaction through ubiquitination of histone H2A and structural remodeling. Together, these complexes form a self-reinforcing silencing system that maintains repressed chromatin states over time. This system is essential for stable gene repression during development, allowing cells to preserve their identity across multiple cell divisions. Disruption of Polycomb-mediated regulation can lead to inappropriate gene activation or silencing, contributing to disease. Applications in Epigenetics and Chromatin Research Because it faithfully reproduces a critical repressive histone mark, [Lys(Me3)27]-Histone H3 (23–34) is widely used in studies focused on epigenetic regulation and chromatin dynamics. Typical applications include: Histone–protein interaction studies to identify H3K27me3-binding proteins Enzyme activity assays for PRC2 and related methyltransferases Binding assays involving Polycomb group proteins Antibody validation experiments for detecting H3K27me3 Biochemical studies of chromatin signaling pathways These experimental approaches help elucidate how H3K27me3 is written, read, and maintained within the genome. Role in Development and Disease H3K27 trimethylation is essential for proper embryonic development and tissue differentiation. It regulates genes that control developmental timing and lineage commitment, ensuring that cells adopt and maintain appropriate functional identities. However, dysregulation of H3K27me3 has been strongly linked to disease. In cancer, alterations in PRC2 activity or mutations in histone proteins can lead to abnormal gene silencing or activation. For example, overexpression or mutation of EZH2 has been associated with tumor progression and epigenetic reprogramming. Additionally, changes in H3K27me3 patterns are implicated in stem cell plasticity and developmental disorders, highlighting the importance of this modification in maintaining normal cellular function. A Reliable Tool for Studying Epigenetic Silencing Synthetic histone peptides such as [Lys(Me3)27]-Histone H3 (23–34) provide a precise and versatile platform for studying the molecular mechanisms underlying epigenetic regulation. By replicating the H3K27me3 modification, this peptide enables researchers to investigate how Polycomb complexes establish and maintain transcriptionally repressed chromatin states. Through applications in binding assays, enzyme studies, and chromatin research, this peptide supports a deeper understanding of gene silencing, chromatin organization, and the epigenetic mechanisms that govern development and disease.