[Lys(Me2)20]-Histone H4 (8-30)-WGK(Biotin)

Product Name: [Lys(Me2)20]-Histone H4 (8-30)-WGK(Biotin)

Sequence One Letter Code: Ac-KGLGKGGAKRHR-K(Me2)-VLRDNIQGITWG-K(biotin)

Sequence Three Letter Code: Ac-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys(Me1)-Val-Leu-Arg-Asp-Asn-Ile-Gln-Gly-Ile-Thr--Trp-Gly-Lys(biotin)

Molecular Weight: 3171

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Disease Research

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: [Lys(Me2)20]-Histone H4 (8–30)-WGK(Biotin) is a synthetic histone H4 peptide spanning residues 8–30, dimethylated at lysine 20 and biotinylated at the C-terminus. H4K20 dimethylation is an important epigenetic modification associated with chromatin compaction, DNA damage response, and gene regulation. The biotin tag enables affinity purification and interaction assays to identify modification-specific binding proteins. This peptide is widely used in epigenetics research to investigate histone modification–dependent recruitment of chromatin regulators, DNA repair factors, and transcriptional complexes. It supports biochemical assays, proteomic studies, and chromatin signaling analyses.

Current Research: [Lys(Me2)20]-Histone H4 (8–30)-WGK(Biotin) is a synthetic peptide corresponding to residues 8–30 of histone H4, containing site-specific dimethylation at lysine 20 (H4K20me2) and a C-terminal WGK-biotin tag for affinity-based applications. The H4 N-terminal tail is a key regulatory domain that extends from the nucleosome core and undergoes multiple post-translational modifications (PTMs) that influence chromatin structure and genome stability. Among these, methylation at lysine 20 plays a central role in chromatin compaction and DNA damage signaling. H4K20 methylation exists in mono-, di-, and trimethylated states, each associated with distinct biological functions. H4K20me2 is the most abundant methylation state in mammalian cells and is broadly distributed across the genome. It has been implicated in maintaining chromatin integrity and serving as a platform for recruitment of DNA repair proteins. The dimethylated form is particularly important in the DNA damage response (DDR), where it contributes to recognition of double-strand breaks. One of the best-characterized H4K20me2 reader proteins is 53BP1 (tumor protein p53-binding protein 1). The tandem Tudor domain of 53BP1 specifically recognizes dimethylated H4K20, enabling localization of 53BP1 to sites of DNA damage. This recruitment influences pathway choice between non-homologous end joining (NHEJ) and homologous recombination (HR) repair mechanisms. The synthetic H4 (8–30) peptide bearing K20me2 is widely used to examine this interaction in vitro, providing a defined substrate for binding assays and structural studies. The WGK(Biotin) modification at the C-terminus enables immobilization on streptavidin-coated beads or sensor chips, facilitating pull-down assays and proteomic profiling. Nuclear extracts incubated with the peptide can be analyzed to identify proteins that preferentially bind H4K20me2 compared with unmodified or differently methylated variants. When coupled with mass spectrometry, this approach supports unbiased identification of modification-specific interaction partners. In addition to DNA repair research, H4K20me2 is linked to chromatin compaction and transcriptional regulation. Although H4K20me3 is more strongly associated with constitutive heterochromatin, the dimethylated state contributes to higher-order chromatin organization and may influence gene expression indirectly through structural effects. The synthetic peptide allows researchers to dissect how specific methylation states affect binding of chromatin-associated factors and remodeling complexes. The peptide is also used in enzymatic studies of histone methyltransferases and demethylases that regulate H4K20 methylation. SETD8 (also known as PR-Set7) catalyzes monomethylation at H4K20, while SUV420H1 and SUV420H2 are responsible for di- and trimethylation. Defined methylated peptides serve as standards for evaluating enzyme specificity and catalytic activity in vitro. Additionally, they are essential for validating antibodies directed against specific H4K20 methylation states to ensure selectivity in immunoblotting and chromatin immunoprecipitation (ChIP) assays. Because H4K20 methylation status is altered in certain cancers and genomic instability syndromes, this peptide supports research into epigenetic dysregulation and tumor biology. Comparative binding studies and inhibitor screening assays frequently incorporate H4K20me2 peptides to examine therapeutic targeting of chromatin readers or writers involved in the DNA damage response. Overall, [Lys(Me2)20]-Histone H4 (8–30)-WGK(Biotin) is a well-defined epigenetic probe for studying H4K20 dimethylation–dependent chromatin signaling. Its site-specific modification and biotin tag enable affinity purification, reader protein characterization, and enzyme profiling. The peptide is a valuable tool in research focused on DNA repair mechanisms, chromatin compaction, transcriptional regulation, and epigenetic contributions to genome stability and disease.