[Lys(Me3)4]-Histone H3 (1-10)

Product Name: [Lys(Me3)4]-Histone H3 (1-10)

Sequence One Letter Code: ART-K(Me3)-QTARKS

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

Molecular Weight: 1189.5

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: [Lys(Me3)4]-Histone H3 (1–10) is a synthetic N-terminal histone H3 peptide with trimethylation at lysine 4 (H3K4me3), a hallmark epigenetic modification associated with active transcription. This mark is enriched at promoter regions of expressed genes and plays a key role in transcription initiation and chromatin accessibility. H3K4me3 is involved in recruiting transcription factors and chromatin-regulatory complexes that facilitate gene activation. This peptide is widely used in epigenetics research to study histone reader proteins, methyltransferase specificity, and mechanisms linking chromatin modifications to transcriptional regulation. It is suitable for binding assays, antibody validation, and functional studies of gene activation and chromatin dynamics.

Current Research: Epigenetic regulation of gene expression is tightly controlled by post-translational modifications of histone proteins, particularly within their N-terminal tails. Among these, trimethylation of lysine 4 on histone H3 (H3K4me3) is one of the most well-established markers of transcriptionally active chromatin. [Lys(Me3)4]-Histone H3 (1–10) is a synthetic peptide that reproduces this key modification within the first 10 amino acids of histone H3, providing a precise and widely used tool for investigating transcriptional regulation and chromatin dynamics. H3K4 Trimethylation and Active Gene Expression H3K4 methylation exists in three states—mono-, di-, and trimethylation—each associated with distinct genomic features. Among these, H3K4me3 is strongly enriched at promoter regions of actively transcribed genes, particularly near transcription start sites (TSS). This modification plays a critical role in: Transcription initiation, by marking promoters poised for activation Chromatin accessibility, facilitating an open and transcriptionally permissive structure Recruitment of transcription machinery, including RNA polymerase II and coactivators Genome-wide studies have consistently shown a strong correlation between H3K4me3 levels and gene expression, making it a defining feature of active chromatin landscapes. Structural Design of the Peptide The [Lys(Me3)4]-Histone H3 (1–10) peptide corresponds to the extreme N-terminal region of histone H3, which is highly accessible and densely modified in vivo. Within this sequence, lysine at position 4 is trimethylated, accurately replicating the H3K4me3 epigenetic mark. Because the peptide is short and well-defined, it enables researchers to isolate the functional effects of this single modification without interference from other histone marks. This simplicity makes it particularly suitable for biochemical and molecular interaction studies. Recruitment of Histone Reader Proteins H3K4me3 functions as a recognition signal for a wide range of epigenetic reader proteins, many of which contain specialized domains such as plant homeodomain (PHD) fingers. These domains selectively bind trimethylated lysine residues and mediate downstream transcriptional processes. Binding of reader proteins to H3K4me3 facilitates: Assembly of transcriptional activation complexes Recruitment of chromatin remodelers Stabilization of open chromatin configurations Through these interactions, H3K4me3 serves as a critical link between histone modifications and transcriptional activation. Role in Chromatin Regulation and Transcriptional Control The presence of H3K4me3 at gene promoters helps establish a chromatin environment that is conducive to transcription. It often works in coordination with other epigenetic marks, such as histone acetylation, to promote gene expression. In addition to its role in activation, H3K4me3 is also involved in: Regulation of transcriptional fidelity, preventing inappropriate initiation Coordination of transcription with RNA processing Integration of signaling pathways that influence gene expression These functions highlight the importance of H3K4me3 in maintaining precise control over gene regulation. Applications in Epigenetics Research Because it faithfully reproduces a key active histone mark, [Lys(Me3)4]-Histone H3 (1–10) is widely used in studies focused on chromatin biology and transcriptional regulation. Common applications include: Protein–peptide binding assays to identify H3K4me3-interacting proteins Histone methyltransferase and demethylase studies Antibody validation experiments for detecting H3K4me3 Biochemical assays investigating transcription-related chromatin interactions Functional studies of gene activation mechanisms These experimental approaches allow researchers to dissect how histone modifications influence transcription at a molecular level. Relevance to Development and Disease H3K4 trimethylation is essential for regulating gene expression programs during development, differentiation, and cellular response to environmental cues. Proper distribution of this mark ensures that genes required for specific cellular functions are appropriately activated. Alterations in H3K4me3 patterns have been linked to cancer, developmental disorders, and epigenetic dysregulation, often resulting in aberrant gene expression. Understanding how this modification is established and interpreted is therefore critical for both basic biology and disease research. A Fundamental Tool for Studying Active Chromatin Synthetic histone peptides such as [Lys(Me3)4]-Histone H3 (1–10) provide a controlled and precise platform for investigating the molecular basis of epigenetic regulation. By replicating the H3K4me3 modification, this peptide enables detailed analysis of how chromatin marks drive transcription initiation and gene activation. Through applications in binding studies, enzyme assays, and chromatin research, this peptide continues to support advances in understanding epigenetic signaling, transcriptional control, and the dynamic regulation of gene expression.