Histone H3 (23-34)

Product Name: Histone H3 (23-34)

Sequence One Letter Code: KAARKSAPATGG

Sequence Three Letter Code: H-Lys-Ala-Ala-Arg-Lys-Ser-Ala-Pro-Ala-Thr-Gly-Gly-OH

Chemical Formula:C46H83N17O15

Molecular Weight: 1114.4

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Unconjugated

 Code Nacres: NA.26

Application: This peptide corresponds to residues 23–34 of histone H3, a region that frequently undergoes regulatory post-translational modifications involved in chromatin organization and gene expression control. Histone H3 sequences within this region are commonly targeted by methylation and acetylation events that influence transcriptional activity and chromatin accessibility. The peptide is widely used as a substrate in biochemical assays investigating histone-modifying enzymes, including histone methyltransferases, acetyltransferases, and demethylases. It also supports binding studies with chromatin-associated proteins that recognize modified histone tails. By providing a defined histone sequence for controlled experimentation, the peptide facilitates studies of chromatin remodeling, transcriptional regulation, and epigenetic signaling pathways relevant to development, cellular differentiation, and disease.

Current Research: Epigenetic regulation plays a central role in controlling gene expression, chromatin structure, and cellular identity. Among the core mechanisms involved in epigenetic control are post-translational modifications (PTMs) of histone proteins, which influence how DNA is packaged and accessed within the nucleus. Histone H3, one of the four core histone proteins forming nucleosomes, contains multiple regions that are highly susceptible to regulatory modifications. Synthetic peptides derived from histone sequences have therefore become valuable experimental tools for studying the enzymes and protein complexes responsible for interpreting and modifying chromatin signals. The Histone H3 (23–34) peptide corresponds to a specific segment of the histone H3 protein that participates in regulatory processes linked to transcription and chromatin remodeling. Because this region frequently undergoes post-translational modifications such as methylation and acetylation, the peptide provides a defined and controllable substrate for biochemical assays investigating epigenetic regulation. Biological Significance of the Histone H3 23–34 Region Histone proteins form the structural core of nucleosomes, around which genomic DNA is wrapped. The N-terminal tails of histones, particularly those of histone H3, extend outward from the nucleosome structure and serve as major sites for regulatory modifications. These modifications can alter chromatin compaction, recruit chromatin-associated proteins, and influence gene transcription. The sequence spanning residues 23–34 of histone H3 lies within a region that is frequently targeted by enzymatic modification. In living cells, residues within this portion of the histone tail may undergo lysine methylation or acetylation, two modifications that have strong effects on transcriptional regulation. Acetylation typically reduces the positive charge of lysine residues, weakening interactions between histones and DNA and promoting a more open chromatin structure. This relaxed configuration is generally associated with active gene transcription. In contrast, lysine methylation can either activate or repress transcription depending on the specific residue modified and the degree of methylation. These modifications contribute to the broader regulatory framework known as the histone code, in which combinations of PTMs determine chromatin states and gene expression outcomes. Use as a Substrate for Histone-Modifying Enzymes Synthetic peptides corresponding to histone sequences provide an effective platform for studying the enzymes that deposit or remove epigenetic marks. The Histone H3 (23–34) peptide is commonly used in biochemical assays designed to characterize histone-modifying enzymes, including: Histone methyltransferases (HMTs), which catalyze the transfer of methyl groups to lysine residues Histone acetyltransferases (HATs), responsible for adding acetyl groups that promote transcriptional activation Histone demethylases, enzymes that remove methyl marks and help regulate chromatin dynamics Because the peptide contains a defined histone sequence without the complexity of full chromatin structures, it allows researchers to measure enzyme activity under controlled conditions. These assays are widely used to investigate enzyme specificity, catalytic efficiency, and the molecular mechanisms governing histone modification. Studying Chromatin Reader Proteins In addition to enzymes that install or remove epigenetic marks, many proteins function as “readers” of histone modifications. These proteins contain specialized domains—such as bromodomains, chromodomains, and Tudor domains—that recognize specific histone modification patterns and recruit regulatory complexes to chromatin. The Histone H3 (23–34) peptide is frequently used in protein–peptide binding studies designed to examine how chromatin-associated proteins recognize modified histone tails. By introducing specific modifications into the peptide sequence, researchers can analyze how particular PTMs influence protein recruitment and chromatin signaling pathways. Such studies are essential for understanding how epigenetic information is interpreted inside the cell. Applications in Chromatin and Epigenetics Research Because of its well-defined sequence and compatibility with biochemical assays, the Histone H3 (23–34) peptide is widely applied in several areas of molecular and cellular biology research. Common applications include: Enzyme activity assays for histone methyltransferases and acetyltransferases Binding experiments examining chromatin reader domains Epigenetic screening studies evaluating inhibitors targeting histone-modifying enzymes Mechanistic studies of chromatin remodeling complexes These experiments help clarify how histone modifications regulate gene expression and how chromatin structure responds to environmental signals or developmental cues. Relevance to Development and Disease Epigenetic regulation is essential for cellular differentiation and developmental programming, enabling cells with identical genomes to adopt specialized functions. At the same time, disruption of histone modification patterns has been linked to numerous diseases, including cancer, neurological disorders, and metabolic conditions. By providing a simplified model of a histone modification site, the Histone H3 (23–34) peptide enables researchers to dissect the molecular mechanisms that control chromatin states. Insights gained from these studies contribute to a deeper understanding of epigenetic signaling pathways and support the development of therapeutic strategies targeting chromatin regulators. Supporting Controlled Studies of Chromatin Regulation Synthetic histone peptides have become indispensable tools in epigenetics research because they allow precise manipulation of histone sequences and modifications. The Histone H3 (23–34) peptide offers a defined substrate that supports reproducible experiments focused on histone-modifying enzymes and chromatin-binding proteins. Through its use in biochemical assays and mechanistic studies, this peptide continues to facilitate research into chromatin remodeling, transcriptional regulation, and the epigenetic mechanisms that govern cellular function and disease progression.