[Arg(Me2a)3]-Histone H4 (1-23)-GGK(Biotin)

Product Name: [Arg(Me2a)3]-Histone H4 (1-23)-GGK(Biotin)

Sequence One Letter Code: SG-R(Me2a)-GKGGKGLGKGGAKRHRKVLR-GGK(Biotin)

Sequence Three Letter Code: H-Ser-Gly-Arg(Me2a)-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val-Leu-Arg-Gly-Gly-Lys(Biotin)-OH

Molecular Weight: 2857.6

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: Histone H4 (1–23) R3Me2a-GGK(Biotin) is a synthetic peptide corresponding to the N-terminal tail of histone H4 with asymmetric dimethylation at arginine 3 and a C-terminal GGK-biotin linker. This modification is catalyzed by protein arginine methyltransferase 1 (PRMT1) and represents an important epigenetic mark associated with transcriptional activation. Asymmetric dimethylation of H4R3 can promote subsequent p300-mediated histone acetylation, contributing to the activation of estrogen-responsive genes and other transcriptional programs. The incorporated biotin tag facilitates affinity purification, immobilization, and interaction studies using streptavidin-based systems. This peptide is widely used in epigenetics and chromatin research to investigate histone modification cross-talk, methylation-dependent protein interactions, and regulatory mechanisms controlling gene expression.

Current Research: Epigenetic regulation relies on a complex network of histone modifications that control chromatin accessibility and gene expression. Among these modifications, arginine methylation plays an important role in coordinating transcriptional activation and chromatin signaling. Synthetic histone peptides that incorporate defined modification states provide powerful experimental models for studying these processes. Histone H4 (1–23) R3Me2a-GGK(Biotin) is a synthetic peptide corresponding to the N-terminal tail of histone H4 with asymmetric dimethylation at arginine 3 (H4R3me2a) and a C-terminal GGK linker bearing a biotin tag. This peptide mimics a biologically significant histone modification and enables researchers to analyze methylation-dependent chromatin interactions using streptavidin-based assay systems. The Regulatory Importance of the Histone H4 N-Terminal Tail Histone H4 is a core component of nucleosomes, the structural units that organize genomic DNA into chromatin. Each nucleosome contains DNA wrapped around an octamer of histone proteins, including two copies each of H2A, H2B, H3, and H4. The N-terminal tail of histone H4 extends outward from the nucleosome core and is highly accessible to chromatin-modifying enzymes and regulatory proteins. This region contains several residues that undergo post-translational modifications (PTMs) such as acetylation, methylation, and phosphorylation. These modifications influence chromatin architecture by altering histone–DNA interactions and by recruiting proteins that regulate transcription and chromatin remodeling. Because the histone H4 N-terminal tail plays such a central role in chromatin signaling, synthetic peptides derived from this sequence are widely used to investigate histone modification pathways and protein recognition mechanisms. Arginine Methylation at Histone H4R3 One of the most important regulatory modifications within the histone H4 tail occurs at arginine 3 (R3). This residue can be methylated by protein arginine methyltransferases (PRMTs), which transfer methyl groups from S-adenosylmethionine (SAM) to the guanidinium group of arginine. PRMT1, a type I protein arginine methyltransferase, catalyzes the formation of asymmetric dimethylarginine (me2a) at H4R3. This modification has been associated with transcriptional activation and chromatin remodeling. The presence of H4R3me2a can influence the recruitment of regulatory proteins and promote downstream histone modifications that further enhance transcription. Research has shown that asymmetric dimethylation of H4R3 can stimulate p300-mediated histone acetylation, creating a cooperative modification pathway that facilitates gene activation. This cross-talk between methylation and acetylation is particularly important in the regulation of estrogen-responsive genes and other transcriptional programs controlled by nuclear hormone receptors. Through these interactions, H4R3 methylation contributes to the broader epigenetic network that governs chromatin accessibility and transcriptional regulation. Structural Design of the R3Me2a-GGK(Biotin) Peptide The Histone H4 (1–23) R3Me2a-GGK(Biotin) peptide is engineered to reproduce the biologically relevant N-terminal sequence of histone H4 while incorporating features that facilitate experimental analysis. Key components of the peptide include: Residues 1–23 of histone H4, representing the regulatory N-terminal region Asymmetric dimethylation at arginine 3, mimicking the H4R3me2a modification A C-terminal GGK linker, providing separation between the peptide and affinity tag Biotin attached to the lysine residue, enabling streptavidin-based capture The GGK linker helps preserve the natural recognition surface of the histone sequence while allowing the peptide to be easily immobilized in biochemical assays. Advantages of Biotinylated Histone Peptides Biotinylation is widely used in molecular biology because of the extremely strong and specific interaction between biotin and streptavidin. This interaction enables peptides to be immobilized efficiently on assay platforms such as beads, microplates, or biosensor surfaces. For histone peptides, the presence of a biotin tag offers several experimental advantages: Pull-down assays for identifying histone-binding proteins Affinity purification of chromatin-associated complexes Stable immobilization for biochemical or biophysical studies Compatibility with proteomics workflows, including mass spectrometry These features make biotinylated histone peptides highly useful for studying how proteins recognize specific histone modification states. Applications in Epigenetics and Chromatin Research The Histone H4 (1–23) R3Me2a-GGK(Biotin) peptide is commonly used in experiments that investigate the biological roles of arginine methylation and histone modification cross-talk. Typical research applications include: Protein interaction analysis The peptide can be used in pull-down assays to identify proteins that selectively recognize the H4R3me2a modification. Histone modification cross-talk studies Researchers can examine how H4R3 methylation influences subsequent histone acetylation and other epigenetic marks. PRMT signaling pathway research The peptide serves as a model substrate for studying the activity and regulatory mechanisms of PRMT1 and related enzymes. Chromatin remodeling investigations Understanding how methylated histone tails interact with chromatin regulators helps clarify mechanisms that control gene expression. Advancing Research in Epigenetic Regulation Epigenetic signaling involves coordinated interactions between multiple histone modifications and chromatin-associated proteins. Synthetic peptides that reproduce specific modification states provide a controlled platform for exploring these complex regulatory networks. By combining asymmetric arginine dimethylation at H4R3 with a biotin affinity tag, the Histone H4 (1–23) R3Me2a-GGK(Biotin) peptide offers a versatile tool for studying methylation-dependent chromatin interactions. Its use in pull-down assays, protein interaction studies, and epigenetic signaling research supports ongoing efforts to understand how histone modifications regulate chromatin structure and transcriptional activation.