[Lys(Me3)20]-Histone H4 (8-30)-WGK(Biotin)

Product Name: [Lys(Me3)20]-Histone H4 (8-30)-WGK(Biotin)

Sequence One Letter Code: Ac-KGLGKGGAKRHR-K(Me3)-VLRDNIQGITWG-K(biotin)

Sequence Three Letter Code: Ac-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lye(Me3)-Val-Leu-Arg-Asp-Asn-Ile-Gln-Gly-Ile-Thr-Trp-Gly-Lys(biotin)

Molecular Weight: 3186

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)20]-Histone H4 (8–30)-WGK(Biotin) is a synthetic histone H4 peptide spanning residues 8–30 and containing trimethylation at lysine 20, a key epigenetic modification associated with chromatin compaction, genome stability, and DNA damage response pathways. Trimethylation at H4K20 plays an important role in regulating cell cycle progression and recruiting proteins involved in DNA repair and chromatin organization. The peptide includes a C-terminal WGK spacer with a biotinylated lysine residue, enabling efficient capture and enrichment using streptavidin-based systems. This format facilitates pull-down assays, protein interaction profiling, and biochemical studies of methyl-lysine recognition. The peptide is widely used as a research tool for investigating chromatin-associated factors, histone methylation signaling pathways, and the molecular mechanisms underlying epigenetic regulation.

Current Research: Histone methylation is a central mechanism in epigenetic regulation, influencing chromatin architecture, genome stability, and the recruitment of regulatory protein complexes. Among the many histone methylation marks identified in chromatin, trimethylation of histone H4 at lysine 20 (H4K20me3) plays a critical role in maintaining chromatin integrity and coordinating cellular responses to DNA damage. Synthetic histone peptides containing defined methylation states provide powerful tools for investigating how these modifications are recognized and interpreted within chromatin. [Lys(Me3)20]-Histone H4 (8–30)-WGK(Biotin) is a synthetic peptide corresponding to residues 8–30 of histone H4, incorporating trimethylation at lysine 20 and a C-terminal WGK spacer with a biotinylated lysine residue. This design enables efficient immobilization and affinity capture using streptavidin-based systems, making the peptide well suited for biochemical assays and protein interaction studies. Histone H4 and Chromatin Organization Histone H4 is one of the four core histone proteins that assemble into nucleosomes, the structural units that package DNA within the nucleus. Each nucleosome consists of approximately 147 base pairs of DNA wrapped around a histone octamer composed of histones H2A, H2B, H3, and H4. The histone proteins contain flexible tail regions that extend from the nucleosome surface and serve as platforms for regulatory modifications. These post-translational modifications (PTMs)—including methylation, acetylation, phosphorylation, and ubiquitination—modulate chromatin structure and control the recruitment of chromatin-binding proteins. The region of histone H4 spanning residues 8–30 includes several important regulatory residues, including lysine 20, which is a key site of histone methylation involved in chromatin compaction and genome stability. Biological Significance of H4K20 Trimethylation Trimethylation at lysine 20 of histone H4 (H4K20me3) is a well-characterized epigenetic modification associated with condensed chromatin and heterochromatin formation. This modification contributes to the regulation of several important cellular processes. One of the primary roles of H4K20me3 is the maintenance of chromatin compaction and structural stability. By promoting interactions between nucleosomes and chromatin-associated proteins, the modification helps establish regions of tightly packed chromatin that are often transcriptionally repressed. H4K20 trimethylation is also closely linked to genome stability and DNA damage response pathways. Proteins involved in DNA repair frequently recognize methylated histone residues as part of the signaling mechanisms that coordinate repair processes following genomic damage. The presence of H4K20me3 can help recruit specific repair factors to sites of DNA breaks. In addition, this modification plays a role in cell cycle regulation, particularly during DNA replication and chromatin maturation. Proper regulation of H4K20 methylation states is essential for maintaining genomic integrity during cell division. Design of the Trimethylated Histone Peptide The [Lys(Me3)20]-Histone H4 (8–30)-WGK(Biotin) peptide is engineered to reproduce the natural sequence context surrounding lysine 20 while incorporating features that facilitate experimental analysis. Key structural elements include: Histone H4 residues 8–30, representing a biologically relevant chromatin interaction region Trimethylation at lysine 20, mimicking the H4K20me3 epigenetic mark A C-terminal WGK spacer, providing separation between the histone sequence and the affinity tag Biotin conjugation at the lysine residue, enabling efficient capture in streptavidin-based assays The WGK spacer ensures that the biotin tag remains accessible while minimizing interference with protein recognition of the histone sequence. Advantages of Biotinylated Histone Peptides Biotinylation provides a highly effective method for immobilizing peptides in biochemical assays. The interaction between biotin and streptavidin is extremely strong and specific, allowing peptides to be captured reliably on assay platforms. For histone peptides, biotinylation offers several experimental advantages: Pull-down assays for identifying methyl-lysine binding proteins Affinity purification of chromatin-associated complexes Stable immobilization on streptavidin-coated beads or surfaces Compatibility with proteomic workflows, including mass spectrometry These features enable researchers to analyze protein interactions with methylated histone residues under controlled experimental conditions. Applications in Chromatin and Epigenetics Research The [Lys(Me3)20]-Histone H4 (8–30)-WGK(Biotin) peptide is widely used in studies investigating how histone methylation influences chromatin organization and protein recruitment. Typical research applications include: Protein interaction profiling Researchers use the peptide in pull-down assays to identify proteins that selectively recognize the H4K20me3 modification. DNA damage response studies The peptide helps investigate proteins involved in genome stability and DNA repair pathways that respond to H4K20 methylation. Histone methylation signaling research Scientists can examine how chromatin regulatory complexes interpret methyl-lysine marks. Chromatin structure studies The peptide provides a model system for analyzing how histone methylation contributes to chromatin compaction and epigenetic regulation. Advancing Research on Epigenetic Signaling Epigenetic modifications such as histone methylation form a complex signaling network that controls chromatin organization and gene regulation. Understanding how specific methylation marks are recognized by chromatin-associated proteins is essential for deciphering this regulatory system. The [Lys(Me3)20]-Histone H4 (8–30)-WGK(Biotin) peptide combines a biologically significant histone modification with a robust affinity tag, providing a versatile experimental platform for studying methyl-lysine recognition and chromatin signaling pathways. Through applications in pull-down assays, protein interaction studies, and DNA repair research, this peptide supports ongoing efforts to understand how histone methylation contributes to genome stability and epigenetic regulation.