Histone H4 (1-23)-GGK(Biotin)-NH2

Product Name: Histone H4 (1-23)-GGK(Biotin)-NH2

Sequence One Letter Code: SGRGKGGKGLGKGGAKRHRKVLR-GGK(Biotin)-NH2

Sequence Three Letter Code: H-Ser-Gly-Arg-Gly-Lys-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val-Leu-Arg-Gly-Gly-Lys(Biotin)-NH2

Molecular Weight: 2828.5

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)-GGK(Biotin)-NH₂ is a biotinylated peptide corresponding to the N-terminal tail of histone H4, extended with a C-terminal GGK linker for biotin conjugation. The N-terminal region of histone H4 plays a crucial role in nucleosome stability, chromatin organization, and epigenetic signaling through various post-translational modifications. Incorporation of the biotin tag enables efficient immobilization and detection using streptavidin-based affinity systems, making the peptide suitable for pull-down assays and interaction studies. This peptide is widely used as a model substrate for investigating histone-binding proteins, chromatin remodeling complexes, and factors involved in nucleosome assembly. It also supports research into the mechanisms that regulate transcription, chromatin structure, and epigenetic control.

Current Research: The regulation of chromatin structure is fundamental to gene expression, DNA replication, and genome stability. Histone proteins, which package DNA into nucleosomes, play a central role in these processes through their ability to undergo diverse post-translational modifications and interact with chromatin-associated proteins. Synthetic histone peptides that replicate specific regions of histone proteins are widely used to investigate these mechanisms. Histone H4 (1–23)-GGK(Biotin)-NH₂ is a synthetic peptide corresponding to the N-terminal tail of histone H4, extended with a C-terminal GGK linker that carries a biotin tag. This design preserves the biologically important histone sequence while enabling efficient immobilization and detection in streptavidin-based experimental systems. As a result, the peptide serves as a valuable tool for studying histone–protein interactions, chromatin remodeling, and epigenetic regulatory mechanisms. The Importance of the Histone H4 N-Terminal Tail Histone H4 is one of the four core histone proteins that form the nucleosome, the fundamental structural unit of chromatin. Within nucleosomes, DNA wraps around an octamer composed of two copies each of histones H2A, H2B, H3, and H4. While the histone core provides structural stability, the N-terminal tails of histones extend outward from the nucleosome surface and serve as important regulatory platforms. The first 20–25 amino acids of histone H4 contain several residues that undergo post-translational modifications such as: Acetylation Methylation Phosphorylation These modifications influence chromatin organization by altering histone–DNA interactions and by recruiting proteins that regulate transcription, DNA repair, and chromatin remodeling. Because of its regulatory significance, the H4 N-terminal region is frequently used in experimental systems designed to study chromatin dynamics and epigenetic signaling. Structural Features of the H4 (1–23)-GGK(Biotin)-NH₂ Peptide The Histone H4 (1–23)-GGK(Biotin)-NH₂ peptide reproduces the native histone sequence while incorporating structural features that facilitate biochemical applications. Key design elements include: Residues 1–23 of histone H4, representing the regulatory N-terminal tail A C-terminal GGK linker, which provides spatial separation from the histone sequence Biotin conjugation at the lysine residue, enabling affinity capture An amide cap (-NH₂) at the C-terminus to stabilize the peptide structure The GGK linker helps ensure that the biotin tag does not interfere with protein recognition of the histone sequence. This configuration preserves the biological relevance of the peptide while enabling efficient use in affinity-based assays. Advantages of Biotinylated Histone Peptides Biotinylated peptides are widely used in molecular biology because the interaction between biotin and streptavidin is extremely strong and highly specific. This property allows peptides to be immobilized securely on experimental platforms such as beads, microplates, or biosensor surfaces. For histone peptides, biotinylation provides several advantages: Efficient pull-down assays to identify histone-binding proteins Affinity purification of chromatin-associated complexes Stable immobilization for biochemical and biophysical studies Compatibility with proteomics workflows, including mass spectrometry These features make biotinylated histone peptides powerful tools for analyzing protein–histone interactions and chromatin regulatory mechanisms. Applications in Chromatin and Epigenetics Research The Histone H4 (1–23)-GGK(Biotin)-NH₂ peptide is widely used in experiments investigating chromatin structure and histone-dependent signaling pathways. Because it contains the unmodified histone H4 N-terminal sequence, it provides a useful baseline substrate for studying how proteins interact with histone tails. Typical research applications include: Protein interaction studies Researchers use the peptide in pull-down assays to identify proteins that bind to the histone H4 N-terminal tail. Chromatin remodeling research The peptide can help analyze how chromatin remodeling complexes recognize and interact with histone substrates. Nucleosome assembly studies The histone H4 tail plays a role in nucleosome formation and stability, making the peptide useful for investigating assembly mechanisms. Epigenetic regulation research Scientists can use the peptide to examine how chromatin-associated proteins interact with histone tails before or after specific modifications are introduced. Supporting Studies of Chromatin Structure and Gene Regulation Understanding how histone tails interact with regulatory proteins is essential for deciphering the mechanisms that control chromatin organization and gene expression. Synthetic peptides that reproduce histone sequences provide simplified experimental systems for analyzing these interactions. The Histone H4 (1–23)-GGK(Biotin)-NH₂ peptide offers a versatile platform for studying histone recognition and chromatin regulatory pathways. By combining the biologically relevant histone H4 N-terminal sequence with a robust biotin affinity tag, the peptide enables efficient biochemical assays and interaction studies. Through its applications in pull-down experiments, chromatin remodeling research, and nucleosome assembly studies, this peptide contributes to ongoing efforts to understand how histone proteins regulate chromatin structure, transcriptional control, and epigenetic signaling.