[Lys(Me3)79]-Histone H3 (69-89)-K(Biotin)

Product Name: [Lys(Me3)79]-Histone H3 (69-89)-K(Biotin) - 0.25 mg

Sequence One Letter Code: RLVREIAQDF-K(Me3)-TDLRFQSSAV-K(Biotin)

Sequence Three Letter Code: H-Arg-Leu-Val-Arg-Glu-Ile-Ala-Gln-Asp-Phe-Lys(Me3)-Thr-Asp-Leu-Arg-Phe-Gln-Ser-Ser-Ala-Val-Lys(biotin)-OH

Molecular Weight: 2876.3 Purity: 95% Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: [Lys(Me3)79]-Histone H3 (69–89)-K(Biotin) is a synthetic peptide representing histone H3 residues 69–89 with trimethylation at lysine 79 (H3K79me3) and a C-terminal biotinylated lysine. H3K79 methylation is an important epigenetic mark involved in transcriptional regulation, DNA damage response, and cell cycle control. Unlike many histone modifications that occur in the histone tail, lysine 79 methylation is located within the globular domain of histone H3, giving it distinct regulatory functions. The biotin tag facilitates affinity-based detection and pull-down assays for studying protein interactions. This peptide is widely used in research on DOT1L-mediated methylation, chromatin signaling pathways, and epigenetic mechanisms involved in development, leukemia, and other diseases.

Current Research: Epigenetic modifications of histone proteins are central to the regulation of gene expression and chromatin structure. Among these modifications, methylation of lysine 79 on histone H3 (H3K79) has gained significant attention due to its involvement in transcriptional regulation, DNA damage responses, and cell cycle progression. [Lys(Me3)79]-Histone H3 (69–89)-K(Biotin) is a synthetic histone peptide designed to replicate this specific modification while incorporating a biotin tag that enables affinity-based detection and interaction studies. Because it models a biologically important chromatin mark, this peptide is widely used in research investigating DOT1L-mediated methylation, chromatin signaling pathways, and epigenetic mechanisms associated with development and disease. Unique Characteristics of H3K79 Methylation Most histone modifications occur on the flexible N-terminal tails of histone proteins. In contrast, lysine 79 of histone H3 is located within the globular domain of the nucleosome core. This distinctive location gives H3K79 methylation unique structural and functional properties compared with other histone modifications. H3K79 can exist in mono-, di-, or trimethylated states, each contributing to different aspects of chromatin regulation. The trimethylated form (H3K79me3) is generally associated with actively transcribed genomic regions and plays a role in regulating transcriptional elongation. Genome-wide analyses have shown that H3K79 methylation often correlates with gene bodies of actively expressed genes, suggesting that this modification contributes to transcriptional maintenance and chromatin organization during gene expression. Because the modification occurs within the nucleosome core rather than the histone tail, it may influence nucleosome stability and interactions with chromatin-associated proteins in ways distinct from other histone marks. DOT1L: The Enzyme Responsible for H3K79 Methylation The methylation of H3K79 is catalyzed by DOT1L (Disruptor of Telomeric Silencing 1-Like), a conserved histone methyltransferase that specifically targets lysine 79 on histone H3. Unlike many histone methyltransferases that contain SET domains, DOT1L uses a unique catalytic mechanism to modify the nucleosomal substrate. DOT1L activity plays an important role in several biological processes, including: Regulation of transcriptional programs DNA damage signaling and repair Cell cycle progression Maintenance of chromatin structure Dysregulation of DOT1L-mediated methylation has been linked to multiple diseases, particularly mixed-lineage leukemia (MLL)-rearranged leukemias, where abnormal recruitment of DOT1L leads to inappropriate H3K79 methylation and activation of oncogenic gene expression programs. Because of its involvement in disease, DOT1L has become an important target for epigenetic drug discovery and cancer research. Design of the Synthetic Histone Peptide The [Lys(Me3)79]-Histone H3 (69–89)-K(Biotin) peptide is designed to mimic the region of histone H3 surrounding lysine 79. The peptide includes residues 69–89 of histone H3, which encompass the structural context required for studying interactions involving the H3K79 methylation site. Within this sequence, lysine 79 is trimethylated, reproducing the H3K79me3 modification found in chromatin. At the C-terminus, the peptide contains an additional biotinylated lysine residue, allowing the peptide to be captured or immobilized through the strong interaction between biotin and streptavidin. This configuration enables efficient use of the peptide in affinity purification, protein interaction assays, and biochemical detection methods. Studying Protein Interactions with H3K79me3 Histone modifications often serve as molecular signals that recruit chromatin-associated proteins with specialized epigenetic reader domains. These proteins interpret histone marks and translate them into functional outcomes such as gene activation, chromatin remodeling, or DNA repair signaling. Using a biotinylated peptide that reproduces the H3K79me3 modification allows researchers to isolate proteins that recognize or interact with this specific histone mark. In typical experiments, the peptide can be immobilized on streptavidin-coated beads or surfaces, enabling pull-down assays that capture interacting proteins from cellular extracts. After enrichment, these proteins can be identified using mass spectrometry, immunoblotting, or other proteomic techniques. Such studies provide insight into the molecular networks that regulate chromatin structure and transcription. Applications in Chromatin and Epigenetics Research Because it combines a biologically relevant histone modification with a convenient affinity tag, [Lys(Me3)79]-Histone H3 (69–89)-K(Biotin) is widely used in studies exploring epigenetic regulation and chromatin signaling pathways. Common research applications include: Affinity pull-down assays to identify H3K79me3-binding proteins Protein–peptide interaction studies involving chromatin regulatory complexes Biochemical assays examining histone modification recognition Proteomic analyses of chromatin-associated proteins Investigation of DOT1L-dependent methylation pathways These experiments help clarify how histone methylation marks regulate gene expression and how chromatin signaling networks respond to cellular stimuli. Relevance to Development and Disease H3K79 methylation is involved in several critical biological processes, including embryonic development, transcriptional regulation, and genome stability. Changes in the distribution or activity of this histone modification can alter gene expression patterns and influence cellular identity. In cancer biology, abnormal H3K79 methylation patterns—often driven by dysregulated DOT1L activity—have been linked to leukemia and other malignancies. Because of this connection, researchers are actively exploring how targeting DOT1L or modulating H3K79 methylation might provide new therapeutic strategies. Synthetic peptides that replicate this modification provide a controlled experimental system for studying these mechanisms. A Valuable Tool for Studying DOT1L and Epigenetic Signaling By faithfully reproducing the H3K79 trimethylation mark within the globular domain region of histone H3, [Lys(Me3)79]-Histone H3 (69–89)-K(Biotin) offers a powerful platform for investigating chromatin signaling and epigenetic regulation. The incorporated biotin tag enables convenient affinity capture and detection, making the peptide compatible with a wide range of biochemical and proteomic assays. As research continues to uncover the complex roles of histone methylation in gene regulation and disease, tools like this peptide remain essential for advancing our understanding of DOT1L function, chromatin dynamics, and epigenetic mechanisms that shape cellular behavior.