[Lys(Ac)5]-Histone H4 (1-25)-GSGSK(Biotin)

Product Name: [Lys(Ac)5]-Histone H4 (1-25)-GSGSK(Biotin)

Sequence One Letter Code: SGRG-K(Ac)-GGKGLGKGGAKRHRKVLRDN-GSGSK(Biotin)

Sequence Three Letter Code: H-Ser-Gly-Arg-Gly-Lys(Ac)-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val-Leu-Arg-Asp-Asn-Gly-Ser-Gly-Ser-Lys(Biotin)-OH

Molecular Weight: 3274.9

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(Ac)5]-Histone H4 (1–25)-GSGSK(Biotin) is a synthetic histone H4 peptide comprising residues 1–25 with acetylation at lysine 5 and a C-terminal GSGSK linker bearing a biotin tag. Acetylation of H4K5 is an important modification associated with histone deposition during DNA replication and chromatin assembly. This modification plays a role in recruiting histone chaperones and chromatin assembly factors that facilitate nucleosome formation and genome maintenance. The C-terminal biotin modification enables efficient capture and enrichment using streptavidin-based affinity systems, allowing convenient use in pull-down assays and protein interaction studies. This peptide serves as a valuable research tool for investigating nucleosome assembly mechanisms, histone chaperone activity, and epigenetic regulation of chromatin structure.

Current Research: The dynamic organization of chromatin is essential for DNA replication, transcription, and genome stability. Histone proteins play a central role in these processes by packaging DNA into nucleosomes and providing regulatory platforms for epigenetic modifications. Among these modifications, histone acetylation is widely recognized for its influence on chromatin structure and protein recruitment. Synthetic histone peptides carrying defined acetylation marks provide valuable tools for investigating these regulatory mechanisms in controlled experimental systems. [Lys(Ac)5]-Histone H4 (1–25)-GSGSK(Biotin) is a synthetic peptide corresponding to the N-terminal 25 amino acids of histone H4, containing site-specific acetylation at lysine 5 (H4K5Ac). The peptide also incorporates a C-terminal GSGSK linker with a biotin tag, allowing efficient immobilization and enrichment through streptavidin-based affinity systems. This design makes the peptide well suited for pull-down assays and interaction studies focused on chromatin assembly and histone chaperone activity. The Role of Histone H4 in Chromatin Structure Histone H4 is one of the four core histone proteins that form nucleosomes, the fundamental structural units of chromatin. In nucleosomes, approximately 147 base pairs of DNA are wrapped around an octamer composed of histones H2A, H2B, H3, and H4. The histone proteins contain flexible N-terminal tails that extend outward from the nucleosome core and serve as regulatory regions for post-translational modifications. The N-terminal tail of histone H4, particularly residues 1–25, contains several lysine residues that undergo modifications such as acetylation, methylation, and phosphorylation. These modifications regulate chromatin organization by influencing histone–DNA interactions and recruiting proteins that control transcription, DNA repair, and nucleosome assembly. Biological Significance of H4K5 Acetylation Acetylation at lysine 5 of histone H4 (H4K5Ac) is a well-characterized epigenetic modification closely associated with histone deposition during DNA replication and chromatin assembly. Newly synthesized histone H4 molecules are often acetylated at lysines 5 and 12 before being incorporated into chromatin. This acetylation pattern plays an important role in coordinating the assembly of nucleosomes following DNA replication. H4K5Ac helps recruit histone chaperones and chromatin assembly factors, which assist in delivering histones to newly synthesized DNA and organizing them into nucleosome structures. These chaperones and assembly factors ensure that newly replicated DNA is properly packaged into chromatin, maintaining genome stability and epigenetic continuity during cell division. Histone Chaperones and Nucleosome Assembly Histone chaperones are specialized proteins that guide histones during nucleosome formation and prevent inappropriate interactions between histones and DNA. Acetylated histone tails often serve as recognition signals for these chaperone proteins. H4K5 acetylation has been linked to the recruitment and activity of several chromatin assembly factors involved in nucleosome formation. These interactions facilitate the proper deposition of histone H4 and help maintain chromatin organization during DNA replication and repair processes. Studying how histone chaperones recognize acetylated histone tails is therefore important for understanding the mechanisms that regulate chromatin assembly and genome maintenance. Design of the GSGSK(Biotin) Peptide The [Lys(Ac)5]-Histone H4 (1–25)-GSGSK(Biotin) peptide is engineered to maintain the natural histone sequence surrounding the modification site while incorporating structural features that facilitate biochemical analysis. Key design components include: Histone H4 residues 1–25, representing the regulatory N-terminal tail Acetylation at lysine 5, mimicking the H4K5Ac modification found in newly synthesized histones A C-terminal GSGSK linker, providing flexible separation between the peptide and the affinity tag Biotin conjugation, enabling efficient capture using streptavidin-based systems The GSGSK linker helps ensure that the biotin tag does not interfere with protein recognition of the histone sequence, preserving the peptide’s biological relevance. Advantages of Biotinylated Histone Peptides Biotinylated peptides are widely used in biochemical research because of the extremely strong interaction between biotin and streptavidin. This interaction allows peptides to be immobilized reliably on assay platforms such as beads, microplates, or biosensor surfaces. For histone peptides, biotinylation enables: Pull-down assays to identify histone-binding proteins Affinity purification of chromatin-associated complexes Stable immobilization for biochemical and biophysical analysis Compatibility with proteomic workflows, including mass spectrometry These capabilities allow researchers to analyze modification-dependent protein interactions with high specificity. Applications in Chromatin and Epigenetics Research The [Lys(Ac)5]-Histone H4 (1–25)-GSGSK(Biotin) peptide is widely used in studies investigating histone deposition, nucleosome assembly, and chromatin organization. Typical research applications include: Histone chaperone interaction studies The peptide can be used in pull-down assays to identify proteins that recognize H4K5 acetylation during chromatin assembly. Nucleosome assembly research Researchers use the peptide to investigate how histone modifications influence nucleosome formation and chromatin structure. DNA replication–associated chromatin studies Because H4K5 acetylation is linked to newly synthesized histones, the peptide helps explore chromatin assembly during DNA replication. Epigenetic regulation analysis Scientists can examine how acetylation-dependent protein recruitment influences chromatin organization and gene regulation. Supporting Research on Chromatin Assembly and Genome Stability The proper assembly of nucleosomes following DNA replication is essential for maintaining genome integrity and preserving epigenetic information. Histone modifications such as H4K5 acetylation play a key role in coordinating these processes by guiding the interaction between histones and chromatin assembly factors. The [Lys(Ac)5]-Histone H4 (1–25)-GSGSK(Biotin) peptide provides a convenient experimental platform for studying these mechanisms. By combining a biologically relevant histone modification with a biotin affinity tag, the peptide enables efficient pull-down assays and interaction studies that help researchers investigate nucleosome assembly, histone chaperone activity, and epigenetic regulation of chromatin structure.