[Arg(Me2s)26]-Histone H3 (15-36)-GGK(Biotin)

Product Name: [Arg(Me2s)26]-Histone H3 (15-36)-GGK(Biotin)

Sequence One Letter Code: APRKQLATKAA-R(Me2s)-KSAPATGGVK-GGK(biotin)

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

Molecular Weight: 2704.4

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: Histone H3 (15–36) R26Me2s-GGK(Biotin) is a synthetic peptide corresponding to residues 15–36 of histone H3 and containing symmetric dimethylation at arginine 26. Symmetric arginine dimethylation is an important epigenetic modification that influences chromatin structure and transcriptional regulation through selective recognition by methyl-arginine binding proteins. The peptide includes a C-terminal GGK linker with a biotin tag, allowing efficient affinity capture, immobilization, and detection in streptavidin-based assays. This format enables convenient use in pull-down experiments and protein interaction studies. Histone H3 R26 methylation has been associated with regulation of gene expression and chromatin dynamics, making this peptide a valuable research tool for studying PRMT-mediated signaling pathways and arginine methylation-dependent protein recognition.

Current Research: Histone arginine methylation is an important component of epigenetic regulation that influences chromatin structure, transcriptional activity, and protein recruitment to chromatin. Among these modifications, symmetric dimethylation of arginine residues plays a key role in regulating histone–protein interactions and signaling pathways within the nucleus. Synthetic histone peptides that incorporate defined methylation states provide valuable tools for studying these processes in controlled experimental settings. Histone H3 (15–36) R26Me2s-GGK(Biotin) is a synthetic peptide corresponding to residues 15–36 of histone H3 and containing symmetric dimethylation at arginine 26 (H3R26me2s). The peptide also includes a C-terminal GGK linker with a biotin tag, enabling efficient immobilization and capture in streptavidin-based assays. This design allows researchers to investigate how arginine methylation influences chromatin-associated protein interactions and epigenetic signaling. Histone H3 and the Regulation of Chromatin Structure Histone H3 is one of the four core histone proteins that assemble into nucleosomes, the structural units of chromatin. DNA wraps around histone octamers composed of H2A, H2B, H3, and H4, creating a compact structure that regulates genome accessibility. The histone proteins contain flexible tails and structured regions that can undergo numerous post-translational modifications (PTMs), which help control transcription and chromatin organization. While the N-terminal tail of histone H3 contains many well-characterized modification sites, residues located slightly downstream—such as the 15–36 region—also contribute to regulatory signaling and chromatin dynamics. Modifications within this segment can influence interactions with chromatin-binding proteins and transcriptional regulators, making it an important region for studying histone-mediated regulatory mechanisms. Arginine Methylation and Epigenetic Signaling Arginine methylation is a common histone modification catalyzed by protein arginine methyltransferases (PRMTs). These enzymes transfer methyl groups from S-adenosylmethionine (SAM) to the guanidinium group of arginine residues, producing different methylation states including monomethylation, asymmetric dimethylation, and symmetric dimethylation. Symmetric dimethylation (me2s) is produced by type II PRMT enzymes, such as PRMT5, and is associated with specific regulatory outcomes in chromatin biology. This modification can influence gene expression by modulating chromatin accessibility or by recruiting proteins that specifically recognize methylated arginine residues. The modification of histone H3 at arginine 26 (H3R26) has been implicated in the regulation of transcription and chromatin structure. Methylation at this site may affect the binding of regulatory proteins and contribute to signaling pathways that coordinate gene activation or repression. Because arginine methylation alters both the chemical properties of histone residues and the recognition landscape of chromatin-binding proteins, studying this modification is essential for understanding how epigenetic signals are interpreted within the cell. Design of the R26Me2s-GGK(Biotin) Peptide The Histone H3 (15–36) R26Me2s-GGK(Biotin) peptide is engineered to replicate the biologically relevant histone sequence while incorporating features that facilitate experimental analysis. The peptide contains: Residues 15–36 of histone H3, representing a functionally important chromatin-interaction region Symmetric dimethylation at arginine 26, mimicking the H3R26me2s modification A C-terminal GGK linker, providing separation between the histone sequence and the affinity tag Biotin conjugation at the lysine residue, enabling efficient capture and detection The GGK linker helps ensure that the biotin tag does not interfere with protein recognition of the histone sequence. This allows the peptide to maintain a biologically relevant interaction surface while still being easily immobilized in biochemical assays. Advantages of Biotinylated Histone Peptides Biotinylation is widely used in molecular biology because of the extremely strong interaction between biotin and streptavidin. This binding pair enables stable immobilization of peptides on assay platforms such as beads, microplates, or biosensor surfaces. For histone peptides, biotinylation offers several practical advantages: Efficient pull-down assays to isolate methylation-dependent binding proteins Affinity purification of chromatin-associated complexes Stable immobilization for biochemical or biophysical analysis Compatibility with proteomic workflows, including mass spectrometry These capabilities make biotinylated peptides powerful tools for studying how chromatin-associated proteins recognize specific histone modification states. Applications in Chromatin and Epigenetics Research The Histone H3 (15–36) R26Me2s-GGK(Biotin) peptide is commonly used in experiments that investigate the biological roles of arginine methylation in chromatin regulation. Typical applications include: Protein interaction studies Researchers can use the peptide in pull-down assays to identify proteins that selectively bind to symmetrically dimethylated arginine residues. PRMT pathway research The peptide serves as a model substrate for studying the activity and signaling pathways of PRMT enzymes involved in arginine methylation. Epigenetic recognition studies Scientists can analyze how methyl-arginine binding domains recognize specific histone modification patterns. Chromatin remodeling investigations Understanding how arginine methylation affects protein recruitment helps clarify mechanisms controlling chromatin structure and transcription. Advancing the Understanding of Arginine Methylation in Chromatin Arginine methylation is an important regulatory mechanism that influences chromatin organization and gene expression. The ability of specific proteins to recognize methylated histone residues allows these modifications to function as signals within the broader epigenetic regulatory network. The Histone H3 (15–36) R26Me2s-GGK(Biotin) peptide provides a convenient and biologically relevant model for studying these processes. By combining a defined histone modification with a robust biotin affinity tag, this peptide supports experimental approaches aimed at identifying methylation-dependent interactions and characterizing PRMT-mediated signaling pathways. Through applications in pull-down assays, interaction mapping, and chromatin biology research, this peptide contributes to ongoing efforts to better understand how arginine methylation shapes chromatin dynamics and transcriptional regulation.