Histone H3 (1-8)

Product Name: Histone H3 (1-8)

Sequence One Letter Code: ARTKQTAR

Sequence Three Letter Code: H-Ala-Arg-Thr-Lys-Gln-Thr-Ala-Arg-OH

Chemical Formula:C37H70N16O12

Molecular Weight: 931.1

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Disease Research

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: This peptide corresponds to the N-terminal residues 1–8 of histone H3, a region that forms part of the histone tail extending from the nucleosome core. The H3 N-terminal tail is a key regulatory platform for post-translational modifications such as methylation, acetylation, and phosphorylation that influence chromatin structure and gene expression. Because many chromatin-modifying enzymes target this region, the peptide is commonly used as a substrate in enzymatic assays examining histone acetyltransferase and methyltransferase activity. It also supports binding studies with chromatin-associated proteins that recognize histone tail modifications. The peptide is widely applied in epigenetics research investigating chromatin dynamics, transcriptional regulation, and mechanisms of gene expression control in development and disease.

Current Research: Chromatin organization plays a fundamental role in regulating gene expression, DNA replication, and genome stability. At the center of chromatin regulation are histone proteins, which package DNA into nucleosomes and provide platforms for regulatory post-translational modifications (PTMs). Among these proteins, histone H3 contains a highly dynamic N-terminal tail that undergoes numerous chemical modifications influencing chromatin structure and transcriptional activity. The Histone H3 (1–8) peptide, corresponding to the first eight amino acid residues of the histone H3 N-terminus, is widely used as a model substrate for studying these regulatory mechanisms. The Histone H3 N-Terminal Tail in Chromatin Biology Histone H3 is one of the core histones that form the nucleosome, the fundamental structural unit of chromatin. Each nucleosome consists of DNA wrapped around an octamer of histone proteins, including two copies each of H2A, H2B, H3, and H4. While the central histone core stabilizes the nucleosome structure, the N-terminal histone tails extend outward from the nucleosome, making them accessible to regulatory enzymes and chromatin-associated proteins. The N-terminal region of histone H3, including residues 1–8, is particularly important because it contains amino acids that frequently undergo post-translational modifications. These chemical modifications serve as molecular signals that influence chromatin accessibility and transcriptional outcomes. Common modifications occurring in the H3 N-terminal region include: Lysine acetylation, which is generally associated with transcriptional activation Lysine methylation, which can either activate or repress transcription depending on the site and methylation state Serine phosphorylation, often linked to signaling events and chromatin remodeling Together, these modifications contribute to the complex regulatory framework known as the histone code, in which combinations of histone marks coordinate gene expression programs. Importance of the H3 (1–8) Sequence The first eight residues of histone H3 represent a critical segment of the histone tail that participates in chromatin signaling. This region contains lysine residues and other amino acids that serve as targets for histone-modifying enzymes. Because of its short and well-defined structure, the H3 (1–8) sequence is particularly suitable for controlled biochemical studies. Synthetic peptides derived from this region allow researchers to isolate the effects of specific histone sequences without the complexity of full nucleosome structures. As a result, the Histone H3 (1–8) peptide is commonly used as a model substrate in enzymatic assays and binding experiments. Studying Histone-Modifying Enzymes A major application of the Histone H3 (1–8) peptide is the study of enzymes that add or remove epigenetic marks. Many of these enzymes specifically recognize residues within the H3 N-terminal tail. Researchers frequently use the peptide in enzymatic activity assays to evaluate the function of: Histone acetyltransferases (HATs), which add acetyl groups to lysine residues and promote transcriptionally active chromatin Histone methyltransferases (HMTs), which catalyze the transfer of methyl groups and contribute to chromatin regulation Histone demethylases, enzymes that remove methyl modifications and regulate epigenetic states By providing a defined substrate, the H3 (1–8) peptide allows scientists to measure enzyme specificity, catalytic efficiency, and modification patterns under controlled experimental conditions. Investigating Chromatin Reader Proteins In addition to enzymes that modify histones, numerous proteins function as “readers” of histone modifications. These proteins contain specialized recognition domains that bind to specific histone marks and recruit additional regulatory complexes. The Histone H3 (1–8) peptide is frequently used in protein–peptide interaction assays to study how chromatin-associated proteins recognize histone tail sequences and modifications. Such experiments help clarify how epigenetic information is interpreted and transmitted within the cell. These studies are essential for understanding the molecular basis of transcriptional regulation and chromatin remodeling. Applications in Epigenetics and Gene Regulation Research Because of its defined sequence and compatibility with biochemical assays, the Histone H3 (1–8) peptide has become a widely used tool in epigenetics and chromatin biology research. Typical experimental applications include: Enzyme activity assays for histone acetyltransferases and methyltransferases Binding studies with chromatin reader domains Screening assays for inhibitors targeting histone-modifying enzymes Mechanistic studies of transcriptional regulation and chromatin remodeling These experiments contribute to a deeper understanding of how histone modifications influence gene expression and cellular identity. Relevance to Development and Disease Epigenetic regulation is essential for processes such as cell differentiation, development, and environmental adaptation. At the same time, abnormal histone modification patterns are linked to numerous diseases, including cancer, neurological disorders, and metabolic conditions. Studying histone tail sequences like H3 (1–8) helps researchers identify the molecular pathways that control chromatin states and gene expression. Insights gained from these studies support the development of new therapeutic strategies targeting epigenetic regulators. Supporting Advances in Chromatin Research Synthetic histone peptides have become indispensable tools for dissecting the molecular details of chromatin regulation. The Histone H3 (1–8) peptide provides a minimal yet functionally important segment of the histone tail that is frequently targeted by regulatory enzymes. By serving as a defined substrate for enzymatic assays and protein interaction studies, this peptide continues to support research exploring chromatin dynamics, transcriptional control, and epigenetic mechanisms that shape cellular function in health and disease.