[Lys(Ac)14]-Histone H3 (1-19)

Product Name: [Lys(Ac)14]-Histone H3 (1-19)

Sequence One Letter Code: ARTKQTARKSTGG-K(Ac)-APRKQ

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

Chemical Formula:C87H159N35O26

Molecular Weight: 2112.5

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: This synthetic peptide represents residues 1–19 of histone H3 with acetylation at lysine 14 (H3K14ac), a hallmark of transcriptionally active chromatin. H3K14 acetylation is recognized by bromodomain-containing proteins, including chromatin remodeling factors such as polybromo, facilitating recruitment of transcriptional machinery. The peptide is widely used to characterize acetylation-dependent protein interactions and bromodomain binding specificity. It is suitable for biochemical binding assays, structural studies, and validation of acetyl-lysine-specific antibodies. This reagent supports mechanistic investigations into chromatin remodeling and transcriptional activation pathways.

Current Research: Histone acetylation is one of the most important post-translational modifications regulating chromatin accessibility and gene expression. By neutralizing the positive charge of lysine residues on histone tails, acetylation alters nucleosome interactions and creates binding platforms for specialized chromatin reader proteins. Among these regulatory marks, acetylation of lysine 14 on histone H3 (H3K14ac) is strongly associated with transcriptionally active chromatin. Synthetic peptides containing this modification provide valuable tools for studying how acetylation signals are interpreted by chromatin-associated proteins. The H3 (1–19) K14ac peptide represents the N-terminal region of histone H3 with site-specific acetylation at lysine 14, enabling detailed investigation of acetylation-dependent signaling pathways. Histone H3 N-Terminal Tail and Epigenetic Regulation Histone H3 is one of the four core histone proteins that assemble into nucleosomes, which package DNA into chromatin. Each nucleosome contains a histone octamer composed of two copies each of H2A, H2B, H3, and H4, around which DNA is wrapped. The N-terminal tail of histone H3 extends from the nucleosome surface and contains multiple lysine residues that are targets for regulatory modifications. This region is highly dynamic and subject to various post-translational modifications, including acetylation, methylation, and phosphorylation. These chemical changes regulate chromatin structure and recruit proteins that influence transcription, DNA repair, and chromatin remodeling. The peptide corresponding to residues 1–19 of histone H3 includes several regulatory sites, with lysine 14 serving as a key acetylation site linked to active transcription. Functional Role of H3K14 Acetylation Acetylation at lysine 14 of histone H3 (H3K14ac) is a well-established marker of transcriptionally active chromatin. The addition of an acetyl group neutralizes the positive charge on the lysine side chain, weakening interactions between histones and DNA. This results in a more relaxed chromatin structure that allows transcription factors and RNA polymerase complexes to access DNA more easily. Beyond its structural effects, H3K14ac also functions as a signal for recruitment of chromatin regulatory proteins. Many of these proteins contain specialized domains that recognize acetylated lysine residues. Through these interactions, acetylation marks help coordinate the assembly of transcriptional machinery and chromatin remodeling complexes at gene promoters. Bromodomain Recognition of Acetylated Histones A major class of proteins that recognize acetylated lysine residues is the bromodomain family. Bromodomains are conserved protein modules that selectively bind acetylated histone tails, allowing regulatory proteins to localize to specific chromatin regions. One example is polybromo, a chromatin remodeling factor that contains multiple bromodomains capable of recognizing acetylated histone residues. Binding of bromodomain-containing proteins to acetylated histones helps recruit ATP-dependent chromatin remodeling complexes that reposition nucleosomes and facilitate transcriptional activation. The H3 (1–19) K14ac peptide provides a defined substrate for studying these interactions and examining how bromodomains discriminate between different acetylation sites on histones. Design and Experimental Advantages of the Synthetic Peptide The H3 (1–19) K14ac peptide reproduces the N-terminal region of histone H3 while incorporating a precisely defined acetylation modification at lysine 14. Because the peptide maintains the natural sequence context surrounding the modification site, it effectively mimics the recognition surface presented by histone tails in chromatin. Using synthetic peptides offers several advantages in experimental studies. They allow researchers to isolate the effect of a single modification without interference from additional histone marks or nucleosome components. This controlled environment makes it possible to examine modification-specific protein interactions with high precision. Applications in Protein–Histone Interaction Studies One of the most common uses of the H3K14ac peptide is in biochemical binding assays designed to identify proteins that recognize acetylated histone tails. By incubating the peptide with purified proteins or cellular extracts, researchers can detect and characterize interactions between acetylated histones and chromatin-associated factors. These experiments help clarify how transcriptional regulators are recruited to active chromatin regions and how acetylation marks contribute to the formation of transcriptionally competent chromatin structures. Structural and Biophysical Investigations Synthetic histone peptides are also widely used in structural biology studies aimed at understanding how reader domains interact with modified histone residues. Techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy often rely on defined peptide substrates to determine the molecular basis of histone recognition. The H3K14ac peptide provides a useful ligand for examining how bromodomains and other acetyl-lysine binding modules interact with histone tails at the atomic level. Validation of Acetyl-Lysine–Specific Antibodies Another important application of modified histone peptides is validation of antibodies that detect specific histone acetylation marks. Because antibodies used in chromatin research must distinguish between closely related modification sites, synthetic peptides provide reliable standards for evaluating antibody specificity. The H3 (1–19) K14ac peptide can be used in assays such as ELISA, western blotting, and chromatin immunoprecipitation controls to confirm that antibodies accurately recognize the H3K14 acetylation mark. Supporting Research on Chromatin Remodeling and Transcription Through its ability to model a key histone modification associated with active genes, the H3K14ac peptide supports research into chromatin remodeling, transcriptional activation, and epigenetic signaling pathways. By enabling controlled biochemical and structural studies, the peptide helps researchers dissect how histone acetylation influences gene regulation. Conclusion The H3 (1–19) K14ac peptide represents a well-defined tool for studying acetylation-dependent chromatin signaling. By reproducing the N-terminal region of histone H3 with site-specific acetylation at lysine 14, the peptide allows researchers to investigate how bromodomain-containing proteins and other chromatin regulators recognize acetylated histone tails. Its applications include protein–histone interaction assays, structural studies of bromodomain binding, and validation of acetylation-specific antibodies, making it a valuable reagent for advancing research into transcriptional regulation and chromatin remodeling mechanisms.