[Lys(Ac)8]-Histone H4 (1-25)-GSGSK(Biotin)

Product Name: [Lys(Ac)8]-Histone H4 (1-25)-GSGSK(Biotin)

Sequence One Letter Code: SGRGKGG-K(Ac)-GLGKGGAKRHRKVLRDN-GSGSK(Biotin)

Sequence Three Letter Code: H-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys(Ac)-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)8]-Histone H4 (1–25)-GSGSK(Biotin) is a synthetic peptide corresponding to the N-terminal tail of histone H4 with acetylation at lysine 8 and a C-terminal biotinylated GSGSK linker. Acetylation at H4K8 is an important epigenetic modification associated with transcriptional activation and chromatin remodeling. This modification can facilitate the recruitment of bromodomain-containing proteins, including the BRG1 subunit of the SWI/SNF chromatin-remodeling complex, which plays a key role in regulating gene expression. The biotin label enables efficient immobilization and detection in streptavidin-based assays, supporting pull-down and protein interaction studies. This peptide is widely used to investigate acetylation-dependent chromatin remodeling, histone code interpretation, and regulatory mechanisms that control transcriptional activity.

Current Research: Histone acetylation is a central mechanism in epigenetic regulation, influencing chromatin structure, transcriptional activation, and the recruitment of chromatin-associated proteins. Acetylation of lysine residues on histone tails neutralizes their positive charge, reducing histone–DNA interactions and promoting a more accessible chromatin configuration. Synthetic histone peptides containing defined acetylation marks are widely used to study how these modifications regulate chromatin dynamics and gene expression. [Lys(Ac)8]-Histone H4 (1–25)-GSGSK(Biotin) is a synthetic peptide corresponding to the N-terminal 25 amino acids of histone H4, with site-specific acetylation at lysine 8 (H4K8Ac). The peptide also incorporates a C-terminal GSGSK linker with a biotin tag, enabling efficient immobilization and enrichment in streptavidin-based assay systems. This design allows researchers to examine acetylation-dependent protein recognition and chromatin remodeling mechanisms in controlled biochemical experiments. Histone H4 and the Function of the N-Terminal Tail Histone H4 is one of the four core histone proteins that assemble into nucleosomes, the repeating structural units of chromatin. Each nucleosome contains approximately 147 base pairs of DNA wrapped around an octamer composed of histones H2A, H2B, H3, and H4. While the histone core provides structural stability, the N-terminal tails of histones extend outward from the nucleosome surface and serve as regulatory platforms for post-translational modifications. The first 20–30 residues of histone H4 contain several lysine residues that can undergo modifications such as acetylation, methylation, and phosphorylation. These modifications help regulate chromatin structure and control the recruitment of transcription factors, chromatin remodelers, and other regulatory proteins. Among these residues, lysine 8 (K8) is an important acetylation site associated with active chromatin states and transcriptional regulation. Biological Significance of H4K8 Acetylation Acetylation at histone H4 lysine 8 (H4K8Ac) is commonly observed in transcriptionally active chromatin regions. Like other lysine acetylation events, this modification neutralizes the positive charge of lysine, weakening the electrostatic interaction between histones and DNA. This structural change contributes to a more open chromatin conformation that allows transcriptional machinery to access DNA more efficiently. Beyond altering chromatin structure directly, acetylated lysines serve as recognition signals for acetyl-lysine binding proteins, particularly those containing bromodomains. Bromodomain-containing proteins recognize acetylated histone tails and help recruit regulatory complexes that promote gene activation. H4K8 acetylation has been linked to the recruitment of proteins involved in chromatin remodeling, including components of the SWI/SNF chromatin-remodeling complex. In particular, the BRG1 subunit of SWI/SNF contains domains capable of interacting with acetylated histone residues, facilitating chromatin remodeling events that regulate gene expression. Through these mechanisms, H4K8 acetylation contributes to transcriptional activation and dynamic chromatin regulation. Structural Design of the GSGSK(Biotin) Peptide The [Lys(Ac)8]-Histone H4 (1–25)-GSGSK(Biotin) peptide is engineered to reproduce the biologically relevant histone sequence while incorporating features that facilitate biochemical assays. Key design elements include: Histone H4 residues 1–25, representing the regulatory N-terminal tail Acetylation at lysine 8, mimicking the H4K8Ac epigenetic mark A C-terminal GSGSK linker, providing flexible separation between the peptide and the affinity tag Biotin conjugation at the lysine residue, enabling capture through streptavidin binding The flexible GSGSK linker ensures that the biotin tag remains accessible for streptavidin binding while minimizing interference with protein recognition of the histone sequence. Advantages of Biotinylated Histone Peptides Biotinylated peptides are widely used in molecular biology due to the extremely strong and specific interaction between biotin and streptavidin. This interaction enables reliable immobilization of peptides on experimental platforms such as beads, plates, or biosensor surfaces. For histone peptides, biotinylation enables: Pull-down assays to identify acetylation-dependent binding proteins Affinity purification of chromatin-associated complexes Stable immobilization for biochemical and biophysical studies Compatibility with proteomics workflows, including mass spectrometry These capabilities make biotinylated histone peptides valuable tools for studying chromatin regulatory mechanisms. Applications in Epigenetics and Chromatin Research The [Lys(Ac)8]-Histone H4 (1–25)-GSGSK(Biotin) peptide is widely used in experiments designed to investigate acetylation-dependent chromatin regulation. Typical research applications include: Protein interaction studies The peptide can be used in pull-down assays to identify proteins that recognize the H4K8Ac modification. Chromatin remodeling research Researchers use the peptide to investigate how acetylated histone tails recruit chromatin remodeling complexes such as SWI/SNF. Bromodomain binding assays The peptide provides a useful substrate for analyzing interactions between acetylated histone residues and bromodomain-containing proteins. Transcriptional regulation studies Scientists can examine how histone acetylation influences the recruitment of transcriptional coactivators and regulatory complexes. Supporting Research on Acetylation-Dependent Chromatin Remodeling Histone acetylation plays a crucial role in regulating chromatin accessibility and gene expression. By creating binding sites for acetyl-lysine recognition domains, acetylated histones help coordinate the recruitment of transcriptional machinery and chromatin remodeling complexes. The [Lys(Ac)8]-Histone H4 (1–25)-GSGSK(Biotin) peptide provides a convenient and biologically relevant model for studying these mechanisms. By combining a defined histone acetylation mark with a biotin affinity tag, this peptide enables efficient pull-down assays and interaction studies that help researchers explore how acetylation-dependent signaling pathways regulate chromatin structure and transcriptional activity.