[Lys(Ac)14]-Histone H3 (9-19)

Product Name: [Lys(Ac)14]-Histone H3 (9-19)

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

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

Chemical Formula:C50H90N18O16

Molecular Weight: 1199.4

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Disease Research

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: [Lys(Ac)14]-Histone H3 (9–19) is a synthetic histone H3 peptide acetylated at lysine 14, a modification associated with transcriptionally active chromatin. H3K14 acetylation facilitates recruitment of bromodomain-containing proteins and transcriptional regulators. This peptide is widely used to study acetylation-dependent protein interactions, antibody specificity, and chromatin regulatory mechanisms. It serves as a reference reagent in assays investigating epigenetic regulation and gene expression changes linked to cancer and other diseases.

Current Research: Histone post-translational modifications (PTMs) are central regulators of chromatin structure and gene expression. Among these, acetylation of lysine residues within histone tails is strongly associated with transcriptionally active chromatin. [Lys(Ac)14]-Histone H3 (9–19) is a synthetic peptide corresponding to residues 9–19 of human histone H3, incorporating site-specific acetylation at lysine 14 (H3K14ac). This modification represents a well-characterized epigenetic mark linked to transcriptional activation and chromatin accessibility. As a defined biochemical reagent, the acetylated H3 peptide is widely used to interrogate acetylation-dependent protein interactions and regulatory mechanisms. Lysine acetylation neutralizes the positive charge of the ε-amino group, weakening electrostatic interactions between histone tails and negatively charged DNA. This reduction in histone–DNA affinity contributes to a more open chromatin conformation that facilitates transcription factor binding and RNA polymerase recruitment. H3K14 acetylation is frequently enriched at active promoters and enhancers and is catalyzed by histone acetyltransferases (HATs) such as GCN5 and p300/CBP. The [Lys(Ac)14]-H3 (9–19) peptide reproduces this modification within the context of adjacent residues that contribute to reader protein recognition. One of the primary functions of H3K14ac is recruitment of bromodomain-containing proteins. Bromodomains recognize acetyl-lysine motifs through a conserved hydrophobic binding pocket, mediating association of transcriptional coactivators and chromatin remodelers with acetylated histones. The synthetic acetylated peptide is commonly employed in pull-down assays to evaluate binding specificity of bromodomain proteins such as BRD2, BRD3, BRD4, and other chromatin-associated factors. Comparison with non-acetylated H3 (9–19) controls allows clear assessment of acetylation-dependent interactions. The peptide is also widely used to validate antibody specificity. In immunoblotting, ELISA, or peptide array formats, [Lys(Ac)14]-H3 (9–19) serves as a positive control for anti-H3K14ac antibodies. Inclusion of modified and unmodified peptides enables rigorous evaluation of cross-reactivity and modification selectivity. Such validation is essential in chromatin immunoprecipitation (ChIP) and other epigenetic assays, where accurate detection of specific histone marks underpins interpretation of gene regulatory landscapes. In mechanistic studies, the peptide supports characterization of chromatin-modifying enzymes. Histone deacetylases (HDACs) remove acetyl groups from lysine residues, counteracting HAT activity and contributing to transcriptional repression. The acetylated H3 (9–19) peptide can be used as a substrate in deacetylation assays to measure HDAC catalytic activity and evaluate inhibitor potency. These assays are central to drug discovery efforts targeting HDACs in oncology and inflammatory diseases. The H3K14ac modification also participates in combinatorial “histone code” regulation, where multiple PTMs collectively influence chromatin state. Although the synthetic peptide represents a single modification, it provides a controlled platform for studying the individual contribution of H3K14 acetylation to protein recruitment and transcriptional regulation. It can be incorporated into peptide arrays or multiplex binding assays to examine how neighboring residues influence reader domain recognition. In cancer biology, dysregulated histone acetylation patterns are associated with aberrant gene expression programs and epigenetic instability. Alterations in H3K14ac levels have been observed in various malignancies, reflecting changes in HAT or HDAC activity. The [Lys(Ac)14]-H3 (9–19) peptide therefore supports mechanistic exploration of how acetylation-dependent chromatin remodeling contributes to tumorigenesis and therapeutic response. In summary, [Lys(Ac)14]-Histone H3 (9–19) is a site-specifically acetylated peptide that models a transcriptionally active chromatin mark. By enabling analysis of bromodomain binding, antibody specificity, and deacetylase activity, it serves as a foundational reagent in epigenetics research. Its application advances understanding of chromatin regulation and gene expression control in normal physiology and disease states.