[Lys(Ac)4]-Histone H3 (1-21)-GGK(Biotin)

Product Name: [Lys(Ac)4]-Histone H3 (1-21)-GGK(Biotin)

Sequence One Letter Code: ART-K(Ac)-QTARKSTGGKAPRKQLA-GGK(biotin)

Sequence Three Letter Code: H-Ala-Arg-Thr-Lys(Ac)-Gln-Thr-Ala-Arg-Lys-Ser-Thr-Gly-Gly-Lys-Ala-Pro-Arg-Lys-Gln-Leu-Ala-Gly-Gly-Lys(biotin)-OH

Molecular Weight: 2765.4

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 (1–21) K4Ac-GGK(Biotin) represents the N-terminal tail of histone H3 with acetylation at lysine 4 and biotinylation introduced through a C-terminal GGK linker. Acetylation at H3K4 is a conserved post-translational modification regulated by the histone acetyltransferase Mst1 and observed across multiple species. This modification functions as a chromodomain switch that reduces the binding affinity of Chp1 for H3K9-methylated tails while promoting interactions with HP1 proteins, thereby influencing chromatin structure and epigenetic signaling. The C-terminal biotin tag enables efficient immobilization and capture in streptavidin-based assays, making the peptide suitable for binding studies and protein interaction analysis. It is widely applied in research investigating chromatin remodeling, histone code interpretation, and acetylation-dependent regulation of gene expression.

Current Research: Epigenetic regulation relies heavily on chemical modifications of histone proteins that influence chromatin structure and gene expression. Among these modifications, histone acetylation plays a critical role in controlling DNA accessibility and recruiting chromatin-associated proteins. Synthetic histone peptides that replicate specific modification patterns provide valuable experimental tools for dissecting these regulatory mechanisms. One such reagent is Histone H3 (1–21) K4Ac-GGK(Biotin), a modified peptide representing the N-terminal tail of histone H3 with acetylation at lysine 4 (H3K4Ac) and a biotin tag introduced through a GGK linker. This peptide enables researchers to investigate how acetylation-dependent signals influence chromatin-binding proteins and epigenetic regulation. The Importance of the Histone H3 N-Terminal Tail Histone H3 is a core component of the nucleosome and plays a central role in organizing DNA within chromatin. The N-terminal tail of histone H3, which extends outward from the nucleosome core, is highly flexible and enriched with lysine residues that undergo numerous post-translational modifications (PTMs). These modifications form part of the histone code, a regulatory system that determines how chromatin-associated proteins recognize and interact with nucleosomes. The first 20–30 amino acids of histone H3 contain several key regulatory residues that can be acetylated, methylated, phosphorylated, or ubiquitinated. These modifications influence transcriptional activity, DNA repair, and chromatin remodeling by altering nucleosome structure or by recruiting specialized binding proteins. Because this region is highly accessible and functionally important, synthetic peptides corresponding to the H3 (1–21) sequence are commonly used in biochemical assays that investigate histone modification recognition and chromatin signaling pathways. H3K4 Acetylation and Epigenetic Regulation Within the histone H3 tail, lysine 4 (K4) is a well-studied regulatory site. While it is frequently associated with methylation in transcriptional regulation, acetylation at this position has also been observed and is conserved across multiple organisms. This modification is regulated by the histone acetyltransferase Mst1, an enzyme involved in chromatin organization and gene regulation. Acetylation at H3K4 can influence chromatin structure by altering the binding behavior of histone-recognition proteins. Studies have shown that this modification can function as a chromodomain switch, modifying the interaction landscape of histone tails. For example, H3K4 acetylation has been reported to reduce the binding affinity of the chromodomain protein Chp1 for H3K9-methylated histone tails. At the same time, the modification can promote interactions with heterochromatin protein 1 (HP1) family proteins. Through these mechanisms, H3K4 acetylation contributes to the regulation of heterochromatin structure, transcriptional control, and epigenetic signaling pathways. Investigating how this modification alters protein recognition is essential for understanding chromatin dynamics and regulatory networks within the genome. Design Features of the K4Ac-GGK(Biotin) Peptide The Histone H3 (1–21) K4Ac-GGK(Biotin) peptide is engineered to reproduce the biologically relevant region of the histone H3 tail while incorporating structural features that facilitate experimental use. The peptide contains: Residues 1–21 of histone H3, representing the regulatory N-terminal region Acetylation at lysine 4, mimicking the naturally occurring H3K4Ac modification A C-terminal GGK linker, which provides spatial separation from the peptide sequence Biotin conjugation at the lysine residue, enabling affinity capture The GGK linker ensures that the biotin tag does not interfere with the native histone sequence, preserving the ability of the peptide to interact with chromatin-binding proteins. Advantages of Biotinylated Histone Peptides Biotinylation provides a highly efficient strategy for immobilizing peptides in biochemical assays. Biotin binds strongly to streptavidin or avidin, allowing peptides to be captured on beads, plates, or biosensor surfaces with exceptional stability. This feature offers several practical advantages in epigenetics research: Efficient pull-down assays to isolate histone-binding proteins Affinity purification of chromatin-associated complexes Immobilization for binding kinetics studies Compatibility with proteomics workflows, including mass spectrometry Because the interaction between biotin and streptavidin is extremely strong, biotinylated peptides provide reliable platforms for identifying and characterizing protein interactions. Applications in Chromatin and Epigenetics Research The Histone H3 (1–21) K4Ac-GGK(Biotin) peptide is widely used in studies exploring histone modification signaling and chromatin regulation. Typical applications include: Protein interaction studies Researchers use the peptide to identify proteins that recognize acetylated histone tails, including chromodomain-containing proteins and other chromatin regulators. Chromatin remodeling research The peptide can help investigate how histone acetylation influences chromatin structure and nucleosome organization. Histone code interpretation By isolating specific histone modifications, scientists can study how combinations of PTMs regulate gene expression and chromatin behavior. Epigenetic signaling pathways The peptide supports research into how histone acetylation modulates interactions between histones and regulatory complexes involved in transcriptional control. Advancing the Study of Histone Modification Networks Synthetic histone peptides have become indispensable tools for unraveling the complex regulatory networks that govern chromatin biology. By mimicking specific modification states within histone tails, they allow researchers to analyze individual molecular events that would otherwise be difficult to isolate within intact chromatin. The Histone H3 (1–21) K4Ac-GGK(Biotin) peptide combines a biologically significant histone modification with a robust affinity tag, making it well suited for biochemical and proteomic studies. Through applications in pull-down assays, interaction mapping, and chromatin signaling research, this peptide supports ongoing efforts to understand how histone acetylation shapes gene regulation and epigenetic inheritance.