[Lys(Ac)14/18/23/27]-Histone H3 (1-30)-GGK(Biotin)

Product Name: [Lys(Ac)14/18/23/27]-Histone H3 (1-30)-GGK(Biotin)

Sequence One Letter Code: ARTKQTARKSTGG-K(Ac)-APR-K(Ac)-QLAT-K(Ac)-AAR-K(Ac)-SAP-GGK(Biotin)

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

Molecular Weight: 3802.6

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 H3 (1–30) K14/K18/K23/K27Ac-GGK(Biotin) is a synthetic peptide derived from the N-terminal tail of histone H3 and contains multiple acetylation modifications at lysines 14, 18, 23, and 27. Hyperacetylation of histone H3 is strongly associated with relaxed chromatin structure and active transcriptional states, facilitating the recruitment of bromodomain-containing proteins and transcriptional coactivators. The peptide includes a C-terminal GGK linker with a biotin tag that enables efficient enrichment and immobilization in streptavidin-based assays. This design allows convenient use in pull-down experiments and interaction studies aimed at identifying acetylation-recognizing proteins. The peptide is widely used in epigenetics research to study chromatin accessibility, transcriptional activation mechanisms, and the functional roles of acetylation reader domains.

Current Research: Histone acetylation is a key epigenetic modification that regulates chromatin accessibility and gene expression. Acetylation of lysine residues on histone tails reduces the positive charge of histones, weakening their interaction with DNA and promoting a more open chromatin structure. This relaxed configuration allows transcription factors and chromatin-associated proteins to access genomic DNA more easily. Synthetic histone peptides that incorporate defined acetylation patterns provide valuable tools for studying these regulatory mechanisms. Histone H3 (1–30) K14/K18/K23/K27Ac-GGK(Biotin) is a synthetic peptide derived from the N-terminal tail of histone H3, featuring site-specific acetylation at lysines 14, 18, 23, and 27. The peptide also contains a C-terminal GGK linker with a biotin tag, enabling efficient immobilization and capture using streptavidin-based affinity systems. By presenting multiple acetylated lysine residues within the same sequence context, this peptide mimics a hyperacetylated chromatin state associated with active transcription. The Histone H3 N-Terminal Tail in Epigenetic Regulation Histone H3 is one of the four core histone proteins that assemble into nucleosomes, the fundamental structural units of chromatin. DNA wraps around histone octamers composed of two copies each of H2A, H2B, H3, and H4, forming a compact structure that regulates genome accessibility. The N-terminal tail of histone H3, particularly the first 30 amino acids, contains several lysine residues that serve as hotspots for post-translational modifications. These modifications—including acetylation, methylation, phosphorylation, and ubiquitination—act as regulatory signals that influence chromatin organization and transcriptional activity. Residues K14, K18, K23, and K27 are among the most frequently acetylated lysines within the H3 tail. When multiple lysine residues in this region are acetylated simultaneously, the chromatin environment becomes more permissive for transcription. Hyperacetylation and Transcriptional Activation Hyperacetylation of histone H3 is strongly associated with active chromatin and gene expression. The addition of acetyl groups neutralizes the positive charge of lysine residues, weakening electrostatic interactions between histones and the negatively charged DNA backbone. This results in a more relaxed chromatin structure that facilitates transcriptional machinery access. In addition to altering chromatin structure, acetylated lysine residues act as recognition signals for chromatin-binding proteins. Many regulatory proteins contain specialized domains that specifically bind acetylated lysines, allowing them to recognize active chromatin regions. Among these domains, bromodomains are the most well-characterized acetyl-lysine recognition modules. Bromodomain-containing proteins, including transcriptional coactivators and chromatin remodelers, bind to acetylated histone tails and help recruit transcriptional complexes to target genes. By presenting four acetylation marks simultaneously, the H3 (1–30) K14/K18/K23/K27Ac peptide models a chromatin state that strongly favors transcriptional activation and recruitment of acetylation reader proteins. Design of the GGK(Biotin) Peptide The Histone H3 (1–30) K14/K18/K23/K27Ac-GGK(Biotin) peptide is engineered to maintain the biologically relevant histone sequence while incorporating features that facilitate experimental applications. Key structural components include: Histone H3 residues 1–30, representing the regulatory N-terminal tail Acetylation at lysines 14, 18, 23, and 27, mimicking a hyperacetylated chromatin state A C-terminal GGK linker, providing spatial separation between the peptide and the affinity tag Biotin conjugation, enabling capture and immobilization via streptavidin The GGK linker ensures that the biotin tag remains accessible for streptavidin binding without interfering with the histone sequence recognized by chromatin-binding proteins. Advantages of Biotinylated Histone Peptides Biotinylated peptides are widely used in biochemical and molecular biology research because the interaction between biotin and streptavidin is extremely strong and specific. This interaction enables stable immobilization of peptides on experimental platforms such as beads, microplates, or biosensor surfaces. For histone peptides, biotinylation enables: Pull-down assays for identifying acetylation-dependent binding proteins Affinity purification of chromatin-associated complexes Stable immobilization for biochemical and biophysical analysis Compatibility with proteomics workflows, including mass spectrometry These capabilities allow researchers to identify and characterize proteins that recognize specific histone modification patterns. Applications in Epigenetics and Chromatin Biology The Histone H3 (1–30) K14/K18/K23/K27Ac-GGK(Biotin) peptide is widely used in research aimed at understanding how histone acetylation regulates chromatin structure and transcriptional activation. Common research applications include: Protein interaction studies The peptide can be used in pull-down assays to identify proteins that recognize hyperacetylated histone H3 tails. Bromodomain binding assays Researchers frequently use this peptide to analyze interactions between acetylated histone tails and bromodomain-containing proteins. Chromatin accessibility studies The peptide helps investigate how histone acetylation influences chromatin relaxation and transcriptional activation. Epigenetic signaling research Scientists can examine how multiple acetylation marks cooperate to recruit transcriptional regulators and chromatin remodeling complexes. Supporting Research on Acetylation-Dependent Chromatin Activation Histone acetylation plays a fundamental role in shaping chromatin architecture and regulating gene expression. The presence of multiple acetylated lysine residues within histone tails often signals active chromatin regions and promotes the recruitment of transcriptional machinery. The Histone H3 (1–30) K14/K18/K23/K27Ac-GGK(Biotin) peptide provides a practical experimental model for studying these processes. By combining a hyperacetylated histone sequence with a biotin affinity tag, the peptide enables efficient pull-down assays, protein interaction studies, and chromatin signaling investigations. Through these applications, it supports ongoing research into the mechanisms by which acetylation reader proteins interpret histone modification patterns and regulate transcriptional activation.