[pSer10), Lys(Ac)14]-Histone H3 (1-21)-GGK(Biotin)

Product Name: [pSer10), Lys(Ac)14]-Histone H3 (1-21)-GGK(Biotin) - 0.25 mg

Sequence One Letter Code: ARTKQTARK-pS-TGG-K(Ac)-APRKQLA-GGK(Biotin)

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

Molecular Weight: 2845.3

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: This histone H3-derived peptide spans residues 1–21 and contains two key post-translational modifications: phosphorylation at serine 10 and acetylation at lysine 14. These combinatorial modifications are associated with transcriptional activation and chromatin remodeling during processes such as mitosis and gene induction. The peptide includes a C-terminal glycine–glycine linker followed by a biotinylated lysine, enabling immobilization on streptavidin surfaces for affinity-based assays. This design facilitates pull-down experiments, binding studies, and enzyme assays examining the recognition of modified histone tails. The peptide is widely used to investigate histone modification crosstalk and the mechanisms by which chromatin-associated proteins interpret combinatorial epigenetic signals.

Current Research: Epigenetic regulation plays a central role in controlling gene expression, cell cycle progression, and genome stability. Among the many epigenetic mechanisms, post-translational modifications (PTMs) of histone proteins represent one of the most dynamic and extensively studied systems. Histone tails undergo a wide range of modifications—including phosphorylation, acetylation, methylation, and ubiquitination—that collectively form a regulatory framework often referred to as the “histone code.” Synthetic histone peptides containing defined PTMs have therefore become essential tools for dissecting how chromatin-associated proteins interpret these signals. One widely used research reagent is the Histone H3 (1–21) peptide containing phosphorylation at serine 10 (pSer10) and acetylation at lysine 14 (AcLys14), coupled to a biotin tag via a glycine–glycine linker. This precisely engineered peptide reproduces a key segment of the histone H3 N-terminal tail and allows researchers to investigate the functional interplay between phosphorylation and acetylation in chromatin regulation. Biological Significance of Histone H3 Modifications The N-terminal tail of histone H3 is a hotspot for regulatory PTMs that influence chromatin accessibility and transcriptional activity. Among these modifications, phosphorylation of serine 10 (H3S10ph) and acetylation of lysine 14 (H3K14ac) have been strongly associated with transcriptional activation and chromatin remodeling. H3S10 phosphorylation is best known for its role during mitosis, where it contributes to chromosome condensation and segregation. However, this modification is also detected in transcriptionally active regions during gene induction, suggesting that it functions as a regulatory signal beyond cell division. Enzymes such as Aurora kinases and MSK1/2 can catalyze this phosphorylation, linking external signaling pathways to chromatin dynamics. Meanwhile, H3K14 acetylation is commonly associated with relaxed chromatin structure and active transcription. Histone acetyltransferases (HATs) introduce this modification, neutralizing the positive charge of lysine residues and weakening histone–DNA interactions. This structural change allows transcription factors and regulatory complexes to access genomic DNA more easily. When these two modifications occur simultaneously on the same histone tail, they create a combinatorial epigenetic signal that can be recognized by specialized reader proteins. Crosstalk Between Phosphorylation and Acetylation The coexistence of H3S10 phosphorylation and H3K14 acetylation represents a classic example of histone modification crosstalk. Rather than functioning independently, these modifications can influence each other’s deposition, stability, and recognition by chromatin-binding proteins. For example, phosphorylation at serine 10 has been shown to enhance the recruitment of certain acetyltransferases, thereby promoting lysine acetylation nearby. Conversely, acetylation at lysine residues can influence kinase accessibility or stabilize phosphorylation-dependent interactions. This layered regulatory mechanism allows cells to fine-tune chromatin states in response to environmental signals, developmental cues, or stress conditions. Synthetic peptides that contain both modifications provide a controlled experimental platform for studying these complex interactions. Biotinylated Design for Affinity-Based Experiments The biotinylated lysine at the C-terminus, connected through a flexible glycine–glycine linker, significantly expands the experimental versatility of this peptide. Biotin binds with extremely high affinity to streptavidin, enabling stable immobilization on streptavidin-coated beads, plates, or biosensor surfaces. This design supports several widely used biochemical and molecular biology techniques, including: Pull-down assays to identify proteins that recognize modified histone tails Protein–peptide binding studies for chromatin reader domains Enzyme activity assays examining histone-modifying enzymes Epigenetic screening experiments evaluating inhibitor or ligand interactions Because the peptide mimics a naturally modified histone tail while remaining experimentally tractable, it provides a reliable platform for dissecting protein–histone interactions in vitro. Applications in Epigenetics and Chromatin Research Researchers commonly use the H3 (1–21) pSer10/AcLys14 biotinylated peptide to investigate how chromatin-associated proteins recognize combinations of histone marks. Proteins containing bromodomains, chromodomains, or other epigenetic reader motifs often display selective binding preferences depending on the modification pattern present on histone tails. By comparing binding profiles across peptides carrying different PTM combinations, scientists can better understand how epigenetic information is encoded and interpreted. These insights are particularly important in areas such as cancer biology, developmental regulation, and transcriptional signaling, where abnormal histone modification patterns frequently contribute to disease. In addition, this peptide serves as a useful reagent in drug discovery and inhibitor screening, especially for compounds targeting histone-modifying enzymes or reader domains. Advancing the Study of the Histone Code Decoding the histone code remains a major challenge in modern molecular biology. Synthetic histone peptides containing defined post-translational modifications provide a powerful approach for isolating specific epigenetic signals and studying their biological consequences. The Histone H3 (1–21) pSer10 / AcLys14 peptide with a biotin tag offers researchers a versatile and highly controlled model of combinatorial histone modifications. By enabling precise biochemical assays and protein interaction studies, it continues to support advances in our understanding of chromatin regulation and epigenetic signaling networks.