[Lys(Me2)27]-Histone H3 (23-34)

Product Name: [Lys(Me2)27]-Histone H3 (23-34)

Sequence One Letter Code: KAAR-K(Me2)-SAPATGG

Sequence Three Letter Code: H-Lys-Ala-Ala-Arg-Lys(Me2)-Ser-Ala-Pro-Ala-Thr-Gly-Gly-OH

Molecular Weight: 1142.3

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: This peptide corresponds to residues 23–34 of histone H3 and contains dimethylation at lysine 27 (H3K27me2), an epigenetic modification involved in transcriptional regulation and chromatin organization. Methylation at lysine 27 of histone H3 is associated with Polycomb-mediated gene repression and the formation of facultative heterochromatin during development. By reproducing this modification within a defined histone tail sequence, the peptide provides a useful tool for studying histone methylation–dependent protein interactions and chromatin regulation mechanisms. It is commonly used in enzyme assays involving histone methyltransferases and demethylases, as well as binding studies with methyl-lysine reader proteins and Polycomb group complexes. This peptide supports research in epigenetics, developmental biology, and disease-related chromatin dysregulation.

Current Research: Introduction to Histone H3 Lysine 27 Methylation Epigenetic regulation of gene expression is largely controlled by chemical modifications on histone proteins. Among these modifications, lysine methylation on histone H3 plays a crucial role in determining whether chromatin is transcriptionally active or repressed. One particularly important site is lysine 27 on histone H3 (H3K27), where methylation states can influence chromatin structure, developmental gene regulation, and cellular identity. The H3K27me2 peptide, corresponding to residues 23–34 of histone H3 with dimethylation at lysine 27, reproduces a key epigenetic modification associated with transcriptional regulation and chromatin organization. Synthetic peptides containing this modification provide valuable reagents for studying chromatin-associated protein interactions and enzymatic activities involved in epigenetic regulation. Structural Features of the H3K27me2 Peptide The histone H3 (23–34) peptide represents a segment of the N-terminal histone tail that extends from the nucleosome core. Histone tails are flexible regions that undergo a variety of post-translational modifications, including methylation, acetylation, and phosphorylation. These modifications serve as signals that recruit regulatory proteins responsible for controlling chromatin accessibility and gene expression. In this peptide, lysine 27 is dimethylated (K27me2), mimicking a naturally occurring modification found in chromatin. By incorporating this specific methylation state into a defined sequence, the peptide enables researchers to examine how proteins recognize and respond to methylated histone residues. Role of H3K27 Methylation in Gene Repression Methylation at histone H3 lysine 27 is strongly associated with Polycomb-mediated transcriptional repression. Polycomb group (PcG) proteins are chromatin regulators that maintain genes in a silent state during development and cellular differentiation. These proteins assemble into multiprotein complexes that modify histones and regulate chromatin structure. H3K27 methylation marks are involved in the formation of facultative heterochromatin, a type of chromatin that remains condensed and transcriptionally inactive but can be reactivated under certain conditions. The dimethylated state (H3K27me2) often serves as an intermediate or regulatory state in the establishment and maintenance of repressive chromatin domains. Through these mechanisms, H3K27 methylation contributes to developmental gene regulation, lineage specification, and epigenetic memory. Applications in Histone Modification Enzyme Studies Synthetic histone peptides containing defined methylation states are widely used in enzyme activity assays involving histone-modifying enzymes. The H3K27me2 peptide is commonly used to investigate enzymes that regulate histone methylation dynamics. Researchers use the peptide to study the activity of histone methyltransferases, which add methyl groups to lysine residues, and histone demethylases, which remove them. By providing a substrate that mimics a naturally modified histone tail, the peptide enables detailed analysis of enzyme specificity, catalytic mechanisms, and regulatory interactions. These studies are essential for understanding how epigenetic marks are established and maintained in chromatin. Investigating Methyl-Lysine Reader Proteins Another important application of the H3K27me2 peptide is in binding assays involving methyl-lysine reader proteins. These proteins contain specialized domains that recognize methylated lysine residues and translate epigenetic marks into functional outcomes. Reader proteins bind selectively to modified histone tails and recruit additional regulatory factors that influence chromatin structure and transcriptional activity. Using synthetic peptides allows researchers to evaluate how strongly these proteins interact with specific methylation states. Such experiments help identify the molecular mechanisms by which chromatin-binding proteins interpret epigenetic signals. Applications in Polycomb Complex Studies Because H3K27 methylation is closely linked to Polycomb group complexes, the peptide is frequently used in studies investigating Polycomb-mediated gene repression. Researchers use the peptide to analyze how Polycomb proteins recognize methylated histone residues and how these interactions contribute to the establishment of repressive chromatin domains. These investigations provide insights into the mechanisms that maintain stable gene repression during development and cellular differentiation. Relevance to Epigenetics and Disease Research Changes in histone methylation patterns are associated with numerous diseases, including cancer and developmental disorders. Dysregulation of H3K27 methylation can lead to abnormal gene expression and disruption of normal cellular identity. By enabling detailed analysis of histone methylation–dependent interactions, the H3K27me2 peptide supports research aimed at understanding epigenetic mechanisms underlying development and disease. It also contributes to efforts focused on identifying therapeutic targets within chromatin regulatory pathways. Conclusion The H3K27me2 peptide derived from histone H3 residues 23–34 reproduces a key epigenetic modification involved in transcriptional repression and chromatin organization. By mimicking the dimethylated lysine 27 mark found in native chromatin, the peptide provides a powerful tool for studying histone methylation–dependent protein interactions. Widely used in enzyme activity assays, protein–peptide binding studies, and investigations of Polycomb-mediated chromatin regulation, this peptide supports research in epigenetics, developmental biology, and disease-associated chromatin dysregulation.