[Lys(Ac)5]-Histone H4 (1-21)-GGK(Biotin)

Product Name: [Lys(Ac)5]-Histone H4 (1-21)-GGK(Biotin)

Sequence One Letter Code: Ac-SGRG-K(Ac)-GGKGLGKGGAKRHRKV-GGK(Biotin)

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

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)5]-Histone H4 (1–21)-GGK(Biotin) is a synthetic N-terminal histone H4 peptide acetylated at lysine 5 and biotinylated at the C-terminus through a GGK linker. Acetylation at H4K5 is associated with chromatin relaxation and transcriptional activation by promoting nucleosome destabilization and transcription factor access. The biotin moiety enables efficient affinity-based capture and detection in biochemical assays. This peptide is commonly used to examine acetylation-dependent recruitment of chromatin readers, histone acetyltransferases, and remodeling complexes. It supports mechanistic investigations into histone modification cross-talk, enzyme specificity, and regulatory pathways governing gene expression in normal and disease-associated chromatin states.

Current Research: Histone post-translational modifications (PTMs) are central to the regulation of chromatin structure and gene expression. Among these modifications, lysine acetylation plays a pivotal role in transcriptional activation by altering histone–DNA interactions and facilitating recruitment of transcriptional machinery. Histone H4 lysine 5 acetylation (H4K5ac) is one of the key regulatory marks found within the N-terminal tail of histone H4 and is frequently associated with chromatin relaxation and active transcriptional states. Synthetic peptides such as [Lys(Ac)5]-Histone H4 (1–21)-GGK(Biotin) provide a defined molecular tool for investigating the biochemical and structural consequences of this modification and for identifying proteins that recognize acetylated histone residues. One major area of research focuses on how acetylated histone marks recruit chromatin reader proteins. Many regulatory proteins contain specialized domains that recognize acetylated lysine residues, including bromodomains, which are found in numerous transcriptional coactivators and chromatin remodeling complexes. H4K5ac is a known ligand for several bromodomain-containing proteins involved in transcriptional regulation and chromatin remodeling. Using acetylated histone peptides such as H4 (1–21) with K5 acetylation, researchers can perform biochemical binding assays to measure how specific reader domains interact with acetylated histone tails. These studies help define the molecular recognition mechanisms that allow cells to interpret epigenetic signals. The biotin tag attached through a C-terminal GGK linker significantly enhances the experimental versatility of this peptide. Biotinylated histone peptides can be immobilized on streptavidin-coated surfaces or magnetic beads, enabling affinity-based assays that capture interacting proteins from nuclear extracts. Such pull-down experiments allow researchers to identify chromatin-associated proteins that preferentially bind acetylated histone tails. When combined with mass spectrometry–based proteomics, these approaches facilitate large-scale mapping of histone modification–dependent protein interaction networks. Another important research application involves studying the role of H4K5 acetylation in nucleosome dynamics and chromatin accessibility. Acetylation neutralizes the positive charge of lysine residues, weakening electrostatic interactions between histones and the negatively charged DNA backbone. This change promotes a more open chromatin configuration that allows transcription factors and RNA polymerase complexes to access regulatory DNA sequences. Synthetic peptides representing the modified histone tail enable researchers to dissect how individual acetylation marks contribute to nucleosome destabilization and chromatin remodeling processes. Recent studies have also highlighted the involvement of H4K5 acetylation in histone modification cross-talk, where multiple epigenetic marks cooperate to regulate chromatin behavior. Histone tails often contain combinations of modifications such as acetylation, methylation, and phosphorylation, which collectively influence protein recruitment and gene expression patterns. Using synthetic histone peptides bearing specific modifications allows investigators to systematically evaluate how different combinations of PTMs affect the binding preferences of chromatin regulators. H4K5 acetylation has also been implicated in disease-associated epigenetic alterations, particularly in cancer and inflammatory disorders. Abnormal acetylation patterns can disrupt normal gene expression programs and contribute to pathological cellular states. Because bromodomain-containing proteins are key readers of acetylated histones, they have become important targets for epigenetic drug discovery. Histone peptides such as [Lys(Ac)5]-Histone H4 (1–21)-GGK(Biotin) are frequently used in assays designed to evaluate bromodomain binding affinity and to screen for small-molecule inhibitors that disrupt acetyl-lysine recognition. In addition to drug discovery, the peptide is valuable for studying the specificity of histone acetyltransferases (HATs) and other chromatin-modifying enzymes. Researchers can use defined peptide substrates to determine how these enzymes recognize histone tails and catalyze acetylation at particular lysine residues. Understanding enzyme specificity is critical for deciphering how epigenetic marks are established and maintained in the genome. In summary, [Lys(Ac)5]-Histone H4 (1–21)-GGK(Biotin) is a widely used reagent in chromatin and epigenetics research. Its defined acetylation mark and biotin affinity tag enable detailed investigation of histone modification–dependent protein interactions, chromatin remodeling mechanisms, and transcriptional regulation. Through applications in pull-down assays, proteomic analyses, and enzymatic studies, this peptide continues to support research aimed at understanding how epigenetic modifications control gene expression in both normal cellular processes and disease-associated chromatin states.