[Arg(Me2s)3]-Histone H4 (1-23)-GGK(Biotin)

Product Name: [Arg(Me2s)3]-Histone H4 (1-23)-GGK(Biotin)

Sequence One Letter Code: SG-R(Me2s)-GKGGKGLGKGGAKRHRKVLR-GGK(Biotin)

Sequence Three Letter Code: H-Ser-Gly-Arg(Me2s)-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: [Arg(Me2s)3]-Histone H4 (1–23)-GGK(Biotin) is a synthetic peptide corresponding to the N-terminal tail of histone H4 with symmetric dimethylation at arginine 3 and a C-terminal biotin modification introduced through a GGK linker. Symmetric dimethylation of H4R3 is an epigenetic mark generated by protein arginine methyltransferases and plays an important role in transcriptional regulation. This modification can promote transcriptional activation by facilitating p300-mediated histone acetylation and influencing chromatin accessibility. The C-terminal biotin tag allows efficient immobilization and enrichment using streptavidin-based systems, enabling pull-down assays and interaction studies. This peptide is widely used to investigate arginine methylation–dependent protein recognition, histone modification cross-talk, and regulatory pathways controlling transcription and metabolic gene expression.

Current Research: Epigenetic regulation relies on a diverse set of histone modifications that influence chromatin structure, transcriptional activity, and the recruitment of regulatory proteins. Among these modifications, arginine methylation plays an important role in controlling gene expression and coordinating interactions between histones and chromatin-associated complexes. Synthetic histone peptides containing defined modification states provide valuable experimental models for investigating these processes. [Arg(Me2s)3]-Histone H4 (1–23)-GGK(Biotin) is a synthetic peptide corresponding to the N-terminal tail of histone H4, incorporating symmetric dimethylation at arginine 3 (H4R3me2s) and a C-terminal GGK linker with a biotin tag. This design preserves the biologically relevant histone sequence while enabling efficient capture and immobilization using streptavidin-based systems. The peptide is widely used to explore arginine methylation–dependent signaling pathways, histone modification cross-talk, and protein recognition mechanisms involved in transcriptional regulation. The Regulatory Role of the Histone H4 N-Terminal Tail Histone H4 is one of the four core histone proteins that form nucleosomes, the fundamental structural units of chromatin. DNA wraps around a histone octamer composed of histones H2A, H2B, H3, and H4, creating a compact yet dynamic structure that regulates genome accessibility. The N-terminal tail of histone H4, encompassing the first 20–25 amino acids, extends outward from the nucleosome surface and serves as a key regulatory region. This segment contains residues that undergo multiple post-translational modifications (PTMs) such as acetylation, methylation, and phosphorylation. These modifications influence chromatin structure by altering histone–DNA interactions and by recruiting proteins that regulate transcription, DNA repair, and chromatin remodeling. Among these regulatory residues, arginine 3 (R3) is an important site for histone methylation and epigenetic signaling. Symmetric Dimethylation at H4R3 Arginine methylation is catalyzed by protein arginine methyltransferases (PRMTs), a group of enzymes that transfer methyl groups from S-adenosylmethionine (SAM) to arginine residues in histones and other proteins. Depending on the enzyme involved, arginine can be converted into monomethylarginine, asymmetric dimethylarginine, or symmetric dimethylarginine. The modification present in this peptide, symmetric dimethylation at H4R3 (H4R3me2s), is generated by type II PRMT enzymes such as PRMT5. This modification has been implicated in regulating chromatin structure and transcriptional activity. Studies have shown that methylation at H4R3 can influence chromatin accessibility and facilitate downstream histone modifications. In particular, H4R3 methylation has been reported to promote p300-mediated histone acetylation, linking arginine methylation to acetylation-dependent transcriptional activation pathways. Through these interactions, H4R3 methylation contributes to the broader regulatory network that controls gene expression and chromatin dynamics. Design of the H4R3Me2s-GGK(Biotin) Peptide The [Arg(Me2s)3]-Histone H4 (1–23)-GGK(Biotin) peptide is engineered to replicate the biologically relevant sequence of the histone H4 tail while incorporating functional features that enhance its experimental utility. The peptide includes: Histone H4 residues 1–23, representing the regulatory N-terminal tail Symmetric dimethylation at arginine 3, mimicking the H4R3me2s epigenetic modification A C-terminal GGK linker, providing spatial separation from the affinity tag Biotin conjugation, enabling immobilization through streptavidin binding The GGK linker ensures that the biotin tag remains accessible while minimizing interference with protein recognition of the histone sequence. Advantages of Biotinylated Histone Peptides Biotinylated peptides are widely used in molecular biology due to the exceptionally strong and specific interaction between biotin and streptavidin. This interaction enables stable immobilization of peptides on various experimental platforms. For histone peptides, biotinylation offers several advantages: Efficient pull-down assays to identify histone-binding proteins Affinity purification of chromatin-associated complexes Stable immobilization on streptavidin-coated beads or surfaces Compatibility with proteomic analyses, including mass spectrometry These capabilities make biotinylated histone peptides powerful tools for studying modification-dependent protein interactions. Applications in Epigenetics and Chromatin Biology The [Arg(Me2s)3]-Histone H4 (1–23)-GGK(Biotin) peptide is widely used in experiments aimed at understanding how arginine methylation influences chromatin regulation and transcriptional activity. Typical research applications include: Protein interaction studies The peptide can be used in pull-down assays to identify proteins that selectively recognize the H4R3me2s modification. Histone modification cross-talk analysis Researchers can investigate how arginine methylation influences other histone modifications, such as acetylation. PRMT pathway research The peptide provides a model substrate for studying the activity and regulatory roles of PRMT enzymes involved in arginine methylation. Transcriptional regulation studies Scientists can examine how methylated histone tails contribute to gene expression and chromatin accessibility. Supporting Research on Arginine Methylation Signaling Histone arginine methylation is an important component of epigenetic regulation that links chromatin structure with transcriptional control. Understanding how methylated histone residues are recognized by chromatin-associated proteins is essential for deciphering these regulatory pathways. The [Arg(Me2s)3]-Histone H4 (1–23)-GGK(Biotin) peptide provides a convenient and biologically relevant model for investigating these mechanisms. By combining a defined histone modification with a robust biotin affinity tag, this peptide enables efficient pull-down assays, protein interaction studies, and chromatin signaling analyses that help reveal how arginine methylation contributes to epigenetic regulation and transcriptional control.