[Lys(Me3)27]-Histone H3 (23-34)-GGK(Biotin)

Product Name: [Lys(Me3)27]-Histone H3 (23-34)-GGK(Biotin)

Sequence One Letter Code: KAAR-K(Me3)-SAPATGG-GGK(Biotin)

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

Molecular Weight: 1626

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(Me3)27]-Histone H3 (23–34)-GGK(Biotin) is a synthetic histone H3 peptide spanning residues 23–34, featuring trimethylation at lysine 27 and C-terminal biotinylation via a GGK linker. Trimethylated H3K27 is a hallmark epigenetic modification associated with Polycomb-mediated transcriptional repression and silencing of CpG island–containing genes, particularly in cancer. The biotin tag enables affinity purification, pull-down assays, and chromatin-binding studies. This peptide is widely used to investigate histone modification–dependent protein interactions, Polycomb complex recruitment, and chromatin regulation mechanisms. It supports epigenetics research focused on transcriptional repression, oncogenic silencing pathways, and modification-specific signaling networks.

Current Research: [Lys(Me3)27]-Histone H3 (23–34)-GGK(Biotin) is a synthetic histone tail peptide corresponding to residues 23–34 of human histone H3, containing a trimethylated lysine at position 27 (H3K27me3) and a C-terminal GGK spacer conjugated to biotin. This design enables precise interrogation of modification-dependent chromatin interactions while facilitating affinity-based capture through streptavidin systems. H3K27 trimethylation is a canonical repressive epigenetic mark catalyzed primarily by the Polycomb Repressive Complex 2 (PRC2), whose catalytic subunit EZH2 (or EZH1 in certain contexts) deposits mono-, di-, and trimethyl marks on lysine 27 of histone H3. Among these, H3K27me3 is strongly associated with stable transcriptional repression and is enriched at promoters of developmentally regulated genes, especially CpG island–containing loci. In embryonic stem cells and differentiated tissues, this modification contributes to lineage specification by maintaining silencing of alternative fate genes. In cancer biology, dysregulation of H3K27 methylation is a frequent pathogenic event. Overexpression or activating mutations of EZH2 can lead to aberrant accumulation of H3K27me3 and inappropriate silencing of tumor suppressor genes. Conversely, loss-of-function mutations in PRC2 components or gain-of-function mutations in histone H3 (e.g., H3K27M in certain gliomas) can globally alter chromatin repression patterns. The [Lys(Me3)27]-H3 (23–34) peptide provides a defined substrate to dissect how specific protein complexes recognize this epigenetic mark. Functionally, H3K27me3 is read by chromodomain-containing proteins, particularly members of the Polycomb Repressive Complex 1 (PRC1), such as CBX family proteins. Binding of PRC1 to H3K27me3-enriched chromatin promotes histone ubiquitination (e.g., H2AK119ub) and compaction of chromatin structure, reinforcing transcriptional silencing. The synthetic peptide enables in vitro analysis of these reader–mark interactions under controlled conditions. The C-terminal GGK(Biotin) modification facilitates immobilization on streptavidin-coated beads or surfaces, enabling pull-down assays and quantitative binding studies. Researchers commonly use this peptide in chromatin-binding assays to identify and validate H3K27me3-interacting proteins from nuclear extracts. Coupled with mass spectrometry, it supports unbiased identification of modification-specific binding partners. Competitive binding assays using unmodified or differently modified H3 peptides further allow discrimination of mark-specific interactions. In addition to protein interaction studies, the peptide is used to evaluate antibody specificity. Antibodies targeting H3K27me3 must distinguish trimethylated lysine from mono- or dimethyl states and from neighboring modifications. Defined synthetic peptides provide rigorous controls for dot blots, ELISA assays, and epitope mapping experiments. Structural and biophysical investigations also benefit from this reagent. Surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), and fluorescence polarization assays can quantify binding affinities between H3K27me3 and reader domains. Such analyses clarify how methylation state and adjacent amino acids influence recognition dynamics. In epigenetics research more broadly, [Lys(Me3)27]-Histone H3 (23–34)-GGK(Biotin) supports mechanistic studies of transcriptional repression, chromatin remodeling, and oncogenic silencing networks. It is particularly relevant in investigations examining how Polycomb-mediated repression interfaces with DNA methylation, histone deacetylation, and three-dimensional chromatin organization. Overall, this biotinylated, site-specifically trimethylated histone H3 peptide is a precise molecular tool for studying H3K27me3-dependent protein recruitment and chromatin regulation. Its defined modification and affinity tag enable robust biochemical and proteomic analyses central to understanding transcriptional repression mechanisms in development and cancer.