[Lys(Me1)4]-Histone H3 (1-21)-GGK(FAM)-NH2

Product Name: [Lys(Me1)4]-Histone H3 (1-21)-GGK(FAM)-NH2

Sequence One Letter Code: ART-K(Me1)-QTARKSTGGKAPRKQLA-GGK(FAM)-NH2

Sequence Three Letter Code: H-Ala-Arg-Thr-Lys(me)-Gln-Thr-Ala-Arg-Lys-Ser-Thr-Gly-Gly-Lys-Ala-Pro-Arg-Lys-Gln-Leu-Ala-Gly-Gly-Lys(FAM)-NH2

Molecular Weight: 2868.4

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C Protected from light

Research Area: epigenetics

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Fluorescent dyes

Code Nacres: NA.26

Application: This peptide corresponds to residues 1–21 of histone H3 and contains monomethylation at lysine 4 (H3K4me1), an epigenetic modification commonly associated with enhancer regions and transcriptionally poised chromatin states. The peptide includes a C-terminal glycine–glycine (GG) linker and a fluorescent FAM label, enabling fluorescence-based detection in biochemical and biophysical assays. H3K4 monomethylation is recognized by specific chromatin-associated proteins that regulate enhancer activity and gene expression programs. By mimicking the native N-terminal sequence of histone H3 with a defined methylation state, this peptide can be used to investigate the binding of histone modification reader proteins and other chromatin regulators. The fluorescent tag allows convenient monitoring of molecular interactions and facilitates assay development for epigenetic studies. This peptide is therefore useful for research on chromatin regulation, histone methylation recognition, and epigenetic signaling mechanisms.

Current Research: Epigenetic regulation governs how genes are expressed without altering the underlying DNA sequence. Central to this regulation are post-translational modifications (PTMs) of histone proteins, which influence chromatin structure and recruit regulatory complexes that control transcription. Among these modifications, methylation of lysine residues on histone H3 plays a critical role in organizing chromatin states that correspond to active, repressed, or poised gene regulatory regions. One particularly important modification is monomethylation of lysine 4 on histone H3 (H3K4me1), a mark strongly associated with enhancer elements and transcriptionally poised chromatin. Synthetic peptides that replicate histone tail sequences with defined modifications—such as the FAM-labeled H3K4me1 peptide corresponding to residues 1–21 of histone H3—provide powerful tools for dissecting the molecular mechanisms of chromatin regulation. Histone Modifications and the Epigenetic Landscape DNA in eukaryotic cells is packaged into chromatin through its association with histone proteins, forming nucleosomes that regulate DNA accessibility. Each nucleosome consists of DNA wrapped around a histone octamer containing two copies each of histones H2A, H2B, H3, and H4. The N-terminal tails of histones, including histone H3, extend outward from the nucleosome core and serve as platforms for numerous chemical modifications. These modifications—such as acetylation, methylation, phosphorylation, and ubiquitination—collectively form a regulatory system often referred to as the histone code. Specific combinations of these marks influence chromatin structure and determine whether genomic regions are accessible for transcription. Histone methylation is particularly versatile because lysine residues can exist in mono-, di-, or trimethylated states, each associated with distinct regulatory outcomes. These methylation marks are written by histone methyltransferases and interpreted by specialized chromatin “reader” proteins that recognize modified residues. Functional Role of H3K4 Monomethylation Among histone methylation marks, H3K4 methylation plays a prominent role in transcriptional regulation. While H3K4 trimethylation (H3K4me3) is typically enriched at active gene promoters, H3K4 monomethylation (H3K4me1) is predominantly found at enhancer regions—regulatory DNA elements that modulate gene expression by interacting with promoters. Enhancers marked by H3K4me1 often exist in a poised or primed state, meaning they are accessible but not yet fully activated. These regions may later acquire additional modifications, such as histone acetylation, which convert them into fully active enhancers capable of stimulating transcription. H3K4me1 therefore acts as an important signal within the epigenetic landscape, helping identify genomic regions involved in cell type–specific gene regulation and developmental programs. Recognition of H3K4me1 by Chromatin Reader Proteins The functional consequences of histone modifications depend largely on proteins that recognize and bind these marks. Many chromatin-associated proteins contain specialized structural modules—such as PHD fingers, Tudor domains, and chromodomains—that selectively bind methylated lysine residues. Proteins that recognize H3K4 methylation often participate in transcriptional regulation, chromatin remodeling, or enhancer activation. By binding to this mark, these reader proteins help recruit transcriptional coactivators, chromatin remodeling complexes, and additional regulatory factors. Studying how these proteins recognize specific methylation states is crucial for understanding how epigenetic signals translate into functional gene expression programs. Design of the FAM-Labeled H3K4me1 Peptide Synthetic histone peptides allow researchers to study individual histone modifications in a controlled biochemical setting. The peptide described here corresponds to residues 1–21 of histone H3, representing the native N-terminal tail region where many regulatory modifications occur. In this peptide, lysine 4 is monomethylated, accurately reproducing the H3K4me1 modification found in enhancer-associated chromatin. To facilitate experimental detection, the peptide includes two additional features: A C-terminal glycine–glycine (GG) linker, which provides flexibility and spatial separation from the labeling group A fluorescent FAM (5-carboxyfluorescein) tag, enabling fluorescence-based detection The flexible linker helps ensure that the fluorescent label does not interfere with protein binding to the modified histone sequence. Fluorescence-Based Detection and Assay Development The presence of a FAM fluorophore enables the peptide to be used in fluorescence-based biochemical and biophysical assays. Fluorescence detection provides several advantages, including high sensitivity, compatibility with microplate readers, and suitability for real-time monitoring of molecular interactions. For example, researchers can use the peptide in fluorescence polarization or fluorescence resonance assays to measure binding interactions between the histone modification and chromatin-associated proteins. Changes in fluorescence properties can reveal binding affinities, kinetic parameters, or competition with other molecules. The fluorescent tag also allows the peptide to be incorporated into high-throughput assay platforms, making it useful for screening studies that examine protein–histone interactions or small molecules targeting epigenetic regulators. Applications in Epigenetics and Chromatin Biology The FAM-labeled H3K4me1 peptide supports a variety of experimental applications, including: Identification of histone modification reader proteins Quantitative analysis of protein–histone binding interactions Characterization of chromatin regulatory complexes Development of fluorescence-based assays for epigenetic research Because enhancer activity is critical for regulating gene expression during development and differentiation, tools that enable detailed study of enhancer-associated marks such as H3K4me1 are essential for understanding gene regulatory networks. Advancing the Study of Epigenetic Signaling By replicating the native histone H3 N-terminal sequence with a precisely defined H3K4 monomethylation mark, the FAM-labeled H3K4me1 peptide provides a versatile experimental reagent for studying chromatin-associated interactions. The fluorescent tag further enhances its utility by enabling convenient detection in biochemical assays and facilitating assay development. As research into epigenetic regulation continues to expand, peptides that model specific histone modifications will remain valuable tools for exploring enhancer function, chromatin organization, and the molecular mechanisms underlying epigenetic control of gene expression.