[Lys(Ac)8]-Histone H4 (1-21)-GGK(Biotin)

Product Name: [Lys(Ac)8]-Histone H4 (1-21)-GGK(Biotin)

Sequence One Letter Code: Ac-SGRGKGG-K(Ac)-GLGKGGAKRHRKV-GGK(Biotin)

Sequence Three Letter Code: H-Ala-Arg(Me1)-Thr-Lys-Gln-Thr-Ala-Arg-Lys-Ser-Thr-Gly-Gly-Lys-Ala-Pro-Arg-Lys-Gln-Leu-Ala-Gly-Gly-Lys(Biotin)-NH2

Molecular Weight: 2644.2

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 (1–21)-GGK(Biotin) is a synthetic peptide corresponding to the N-terminal tail of histone H4, acetylated at lysine 8 and biotinylated via a C-terminal GGK linker. Acetylation at H4K8 induces conformational changes in nucleosomes that enhance chromatin accessibility and facilitate transcription factor recruitment. The C-terminal biotin tag enables affinity capture using streptavidin-based systems, supporting pull-down and interaction assays. This peptide is extensively used in epigenetics research to investigate acetyl-lysine recognition by bromodomain-containing proteins, chromatin remodeling complexes, and transcriptional regulators. It provides a defined substrate for studying histone modification–dependent signaling and the molecular mechanisms governing transcriptional activation.

Current Research: Epigenetic regulation of gene expression is largely governed by post-translational modifications (PTMs) of histone proteins, which influence chromatin structure and the recruitment of regulatory protein complexes. Among these modifications, lysine acetylation plays a key role in transcriptional activation and chromatin remodeling. Acetylation reduces the positive charge of histone lysine residues, weakening interactions between histones and DNA and thereby promoting a more accessible chromatin configuration. One particularly important modification is acetylation at lysine 8 of histone H4 (H4K8ac), which has been associated with transcriptionally active chromatin regions and dynamic nucleosome remodeling. Synthetic peptides such as [Lys(Ac)8]-Histone H4 (1–21)-GGK(Biotin) provide a well-defined platform for investigating the molecular mechanisms underlying histone acetylation–dependent signaling. Recent research has emphasized the importance of acetyl-lysine recognition by chromatin reader proteins. Many regulatory proteins contain specialized domains that selectively recognize acetylated histone residues. Among these, bromodomains are the most extensively studied acetyl-lysine binding modules. Bromodomain-containing proteins function as chromatin readers that interpret histone acetylation marks and recruit transcriptional machinery or chromatin remodeling complexes. The acetylated H4K8 peptide serves as a defined ligand for examining how bromodomain proteins interact with acetylated histone tails. By using peptides bearing specific acetylation patterns, researchers can analyze binding affinity, specificity, and structural determinants that guide these interactions. The biotin tag attached through a C-terminal GGK linker greatly expands the utility of this peptide in biochemical assays. Biotinylated histone peptides can be immobilized on streptavidin-coated matrices, enabling affinity purification and pull-down experiments designed to capture interacting proteins from nuclear extracts. These assays allow investigators to identify proteins that selectively recognize H4K8 acetylation. When combined with mass spectrometry–based proteomics, this approach facilitates large-scale identification of chromatin-associated factors involved in transcriptional regulation and chromatin remodeling. Another important research direction involves studying how histone acetylation influences nucleosome structure and chromatin accessibility. Acetylation of lysine residues in histone tails, including H4K8, can alter nucleosome stability and the interaction between histones and DNA. Structural and biochemical studies using defined histone peptides help researchers examine how specific modifications affect nucleosome dynamics. These experiments contribute to a better understanding of how chromatin transitions between condensed and open states during gene activation. Histone H4K8 acetylation has also been linked to transcription factor recruitment and the assembly of transcriptional complexes. When chromatin becomes acetylated, transcriptional coactivators and remodeling enzymes are often recruited to promoter and enhancer regions. Synthetic peptides such as H4 (1–21) with K8 acetylation allow investigators to dissect the individual contributions of this modification to the formation of transcriptionally active chromatin environments. Such studies provide insights into how epigenetic marks coordinate gene expression programs in response to developmental cues or environmental stimuli. Beyond fundamental chromatin biology, H4K8 acetylation is increasingly studied in the context of disease-associated epigenetic alterations, particularly in cancer and inflammatory conditions. Abnormal patterns of histone acetylation can disrupt gene expression networks involved in cell proliferation, differentiation, and immune regulation. Because bromodomain-containing proteins are major readers of acetylated histones, inhibitors targeting these proteins have emerged as promising epigenetic therapies. Peptides such as [Lys(Ac)8]-Histone H4 (1–21)-GGK(Biotin) are frequently used to evaluate the binding properties of bromodomains and to screen compounds that disrupt these interactions. In addition, histone peptides bearing defined modifications are valuable tools for investigating histone modification cross-talk, where combinations of different PTMs influence chromatin behavior. By introducing single or multiple modifications into synthetic histone fragments, researchers can systematically analyze how various epigenetic signals interact to regulate chromatin structure and gene transcription. In summary, [Lys(Ac)8]-Histone H4 (1–21)-GGK(Biotin) is a widely used reagent in epigenetics and chromatin biology research. Its defined acetylation mark and biotin affinity tag enable detailed investigation of histone modification recognition, chromatin remodeling mechanisms, and transcriptional regulation. Through applications in pull-down assays, proteomics, and structural studies, this peptide continues to support research aimed at understanding how epigenetic modifications control gene expression in both normal physiology and disease.