[Lys(Ac)23]-Histone H3 (21-44)-GK(Biotin)

Product Name: [Lys(Ac)23]-Histone H3 (21-44)-GK(Biotin)

Sequence One Letter Code: AT-K(Ac)-AARKSAPATGGVKKPHRYRPG-GK(Biotin)

Sequence Three Letter Code: H-Ala-Thr-Lys(Ac)-Ala-Ala-Arg-Lys-Ser-Ala-Pro-Ala-Thr-Gly-Gly-Val-Lys-Lys-Pro-His-Arg-Tyr-Arg-Pro-Gly-Gly-Lys(Biotin)-OH

Molecular Weight: 2959.6

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)23]-Histone H3 (21–44)-GK(Biotin) is a synthetic histone H3 peptide acetylated at lysine 23 and biotinylated at the C-terminus. Acetylation at H3K23 is associated with transcriptional activation and dynamic chromatin remodeling. The biotin tag enables affinity purification and pull-down assays to identify interacting chromatin reader proteins. This peptide is widely used in epigenetics research to dissect histone modification–dependent protein recognition, chromatin complex assembly, and transcriptional regulation. It supports mechanistic studies of histone acetylation in both physiological and disease-associated chromatin states.

Current Research: Post-translational modifications of histone proteins play a central role in regulating chromatin structure and gene expression. Among these modifications, lysine acetylation is one of the most extensively studied epigenetic marks due to its involvement in transcriptional activation and chromatin remodeling. Acetylation neutralizes the positive charge of lysine residues within histone tails, weakening histone–DNA interactions and promoting a more open chromatin configuration that facilitates transcription factor access. The modification H3K23ac, corresponding to acetylation of lysine 23 on histone H3, has gained increasing attention as a regulatory mark associated with active transcription and dynamic chromatin states. Synthetic peptides such as [Lys(Ac)23]-Histone H3 (21–44)-GK(Biotin) provide a powerful platform for investigating how this modification influences chromatin-associated protein interactions and gene regulation. Recent research has focused on understanding how histone acetylation is recognized by chromatin reader proteins. These proteins contain specialized domains—such as bromodomains, YEATS domains, and other acetyl-lysine recognition modules—that selectively bind acetylated histone residues. The acetylated H3K23 peptide serves as a defined molecular probe for identifying and characterizing proteins that specifically recognize this epigenetic mark. Because the peptide is biotinylated at the C-terminus, it can be immobilized on streptavidin-coated matrices and used in affinity purification or pull-down assays to isolate interacting proteins from nuclear extracts. Such experiments help map the networks of chromatin-associated factors that respond to histone acetylation. Another important area of current investigation involves the role of H3K23 acetylation in transcriptional regulation and chromatin remodeling. Studies using histone peptides and chromatin reconstitution systems have shown that acetylation at this position can influence the recruitment of transcriptional coactivators, histone acetyltransferases (HATs), and chromatin remodeling complexes. These factors collectively regulate nucleosome positioning and accessibility of regulatory DNA elements. By using defined peptides such as [Lys(Ac)23]-H3 (21–44), researchers can dissect how individual histone modifications contribute to the formation of transcriptionally active chromatin environments. The peptide is also widely used in epigenetic profiling and proteomic studies. In chromatin biology research, biotinylated histone peptides are often used in combination with mass spectrometry–based proteomics to identify proteins that preferentially bind specific histone marks. This approach enables systematic characterization of histone modification–dependent interaction networks. By comparing proteins captured by acetylated versus non-acetylated peptides, investigators can determine how particular modifications influence protein recruitment and chromatin complex assembly. In addition to fundamental studies of chromatin regulation, H3K23 acetylation has been linked to disease-associated epigenetic changes, particularly in cancer and inflammatory disorders. Aberrant histone acetylation patterns can alter gene expression programs that control cell proliferation, differentiation, and immune responses. Researchers therefore use histone peptides bearing defined modifications to study how chromatin-binding proteins recognize altered epigenetic landscapes in disease states. Understanding these interactions may help identify potential targets for epigenetic therapies, including inhibitors of bromodomain-containing proteins and histone-modifying enzymes. The peptide is also valuable in studies investigating the cross-talk between multiple histone modifications. Chromatin regulation often involves complex combinations of modifications that collectively influence protein recruitment and chromatin dynamics. Using synthetic histone peptides allows researchers to introduce specific modifications individually or in combination, enabling systematic analysis of how different epigenetic marks interact to control gene expression. Overall, [Lys(Ac)23]-Histone H3 (21–44)-GK(Biotin) is a versatile reagent widely used in epigenetics research. Its defined acetylation mark and affinity tag enable detailed investigation of histone modification–dependent protein recognition, chromatin complex assembly, and transcriptional regulation. Through applications in biochemical assays, proteomics, and chromatin interaction studies, this peptide continues to support efforts aimed at understanding the molecular mechanisms of epigenetic control in both normal cellular processes and disease-associated chromatin states.