[Lys(Me1)27/36]-Histone H3 (21-44)-GK(Biotin)

Product Name: [Lys(Me1)27/36]-Histone H3 (21-44)-GK(Biotin)

Sequence One Letter Code: ATKAAR-K(Me1)-SAPATGGV-K(Me1)-KPHRYRPG-GK(Biotin)

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

Molecular Weight: 2945.6

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: Histone H3 (21–44) K27Me1/K36Me1-GK(Biotin) is a synthetic peptide derived from histone H3 containing mono-methylation at lysine 27 and lysine 36. These methylation marks are associated with fine regulation of chromatin structure and transcriptional activity. The peptide includes a C-terminal GK-biotin tag that enables efficient capture and immobilization in streptavidin-based affinity assays. This design allows convenient application in pull-down experiments, interaction profiling, and enzymatic activity studies. By presenting two distinct methyl-lysine modifications within the same sequence context, the peptide provides a useful model for investigating combinatorial histone modification patterns and their effects on chromatin-associated proteins. It is widely used to explore lysine methylation-dependent signaling pathways and histone modification cross-talk.

Current Research: Histone methylation is a central mechanism in epigenetic regulation, influencing chromatin structure, transcriptional activity, and the recruitment of regulatory protein complexes. Unlike some histone modifications that function independently, many histone marks operate in combination, forming complex patterns that guide chromatin-associated proteins and transcriptional programs. Synthetic histone peptides that reproduce these combinatorial modification states are essential tools for studying how multiple epigenetic signals are interpreted within chromatin. Histone H3 (21–44) K27Me1/K36Me1-GK(Biotin) is a synthetic peptide derived from the histone H3 sequence containing mono-methylation at lysine 27 (H3K27Me1) and lysine 36 (H3K36Me1). The peptide also includes a C-terminal GK-biotin tag, enabling efficient immobilization and capture through streptavidin-based affinity systems. By presenting two methylated lysine residues within the same sequence context, this peptide provides a useful model for investigating the functional interplay between histone modifications. Histone H3 and Epigenetic Regulation Histone H3 is one of the four core histone proteins that assemble into nucleosomes, the repeating structural units of chromatin. Within nucleosomes, DNA is wrapped around a histone octamer composed of H2A, H2B, H3, and H4. The histone proteins contain flexible tail regions and structured domains that are subject to numerous post-translational modifications (PTMs). These modifications—including methylation, acetylation, phosphorylation, and ubiquitination—form a dynamic regulatory network that controls chromatin accessibility and gene expression. Different combinations of histone modifications can recruit specific regulatory proteins, creating a system often referred to as the histone code. Residues within the 21–44 region of histone H3 contain important modification sites that influence transcriptional regulation and chromatin organization. Studying these sites together allows researchers to understand how multiple epigenetic signals cooperate to regulate chromatin states. Biological Roles of H3K27 and H3K36 Methylation Both lysine 27 (K27) and lysine 36 (K36) of histone H3 are well-characterized regulatory residues that undergo various methylation states, including mono-, di-, and trimethylation. These modifications contribute to different chromatin functions depending on their context. H3K27 methylation is frequently associated with transcriptional repression when present in higher methylation states, but monomethylation at K27 (H3K27Me1) has been linked to the fine-tuning of chromatin organization and gene activity. It may participate in regulating chromatin structure and marking regions undergoing dynamic transcriptional control. H3K36 methylation is commonly associated with actively transcribed gene bodies. H3K36Me1, the monomethylated form, can participate in early steps of transcriptional regulation and may act as a precursor state that leads to higher methylation levels during active transcription. The simultaneous presence of these two methylation marks within the same histone sequence provides an opportunity to examine how different regulatory signals cooperate to influence chromatin behavior. Combinatorial Histone Modifications and Cross-Talk Histone modifications rarely function in isolation. Instead, they operate within combinatorial patterns, where multiple modifications influence one another and collectively determine the recruitment of chromatin-binding proteins. The presence of both H3K27Me1 and H3K36Me1 in the same histone segment offers a model for studying epigenetic cross-talk—the process by which one histone modification affects the recognition or activity of another. For example, certain chromatin regulators may require specific combinations of methylation marks to bind efficiently to histone substrates. By providing a defined dual-modification state, this peptide enables researchers to examine how chromatin-associated proteins interpret complex histone modification patterns. Structural Design of the GK(Biotin) Peptide The Histone H3 (21–44) K27Me1/K36Me1-GK(Biotin) peptide is engineered to maintain the biologically relevant sequence context while incorporating features that facilitate experimental analysis. The peptide contains: Residues 21–44 of histone H3, representing a regulatory chromatin-interaction region Mono-methylation at lysine 27 and lysine 36, mimicking naturally occurring histone marks A C-terminal GK linker, providing separation between the peptide and affinity tag Biotin conjugation, enabling capture and immobilization in streptavidin-based assays The linker ensures that the biotin tag does not interfere with protein recognition of the histone sequence, preserving the peptide’s functional interaction surface. Advantages of Biotinylated Histone Peptides Biotinylation is widely used in biochemical research because of the strong and specific interaction between biotin and streptavidin. This interaction enables stable immobilization of peptides in various experimental platforms. For histone peptides, biotinylation allows: Pull-down assays to identify histone-binding proteins Affinity purification of chromatin-associated complexes Immobilization on streptavidin-coated surfaces Proteomics-based interaction profiling using mass spectrometry These features make biotinylated histone peptides powerful tools for analyzing modification-dependent protein recognition. Applications in Epigenetics and Chromatin Biology The Histone H3 (21–44) K27Me1/K36Me1-GK(Biotin) peptide is widely used in studies investigating how multiple histone modifications influence chromatin signaling and transcriptional regulation. Typical applications include: Protein interaction profiling Researchers use the peptide in pull-down assays to identify proteins that recognize dual methylation states. Histone modification cross-talk studies The peptide allows analysis of how combinations of methyl-lysine marks influence chromatin-binding protein recruitment. Enzyme activity studies The peptide can serve as a substrate for examining lysine methyltransferases or demethylases involved in chromatin regulation. Epigenetic signaling research Scientists can investigate how chromatin regulatory complexes interpret complex modification patterns within histone tails. Enabling Research on Combinatorial Epigenetic Signaling Understanding how multiple histone modifications cooperate to regulate chromatin is essential for decoding epigenetic signaling pathways. Synthetic peptides that present defined combinations of modifications provide a simplified yet biologically meaningful platform for studying these mechanisms. The Histone H3 (21–44) K27Me1/K36Me1-GK(Biotin) peptide combines two important methylation marks within a single histone sequence while incorporating a biotin tag for experimental versatility. Through applications in pull-down assays, protein interaction studies, and enzymatic analyses, this peptide supports ongoing research into how combinatorial histone modifications shape chromatin structure and gene regulation.