Histone H2A (1-20)-GGK(Biotin)

Product Name: Histone H2A (1-20)-GGK(Biotin)

Sequence One Letter Code: SGRGKQGGKARAKAKTRSSR-GGK(Biotin)

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

Molecular Weight: 2556.1

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 H2A (1–20)-GGK(Biotin) is a synthetic peptide corresponding to the N-terminal 20 amino acids of human histone H2A, modified with a C-terminal glycine–glycine linker and biotinylated lysine. The H2A N-terminal region contains multiple sites of post-translational modification that regulate nucleosome stability and chromatin architecture. The biotin tag enables efficient capture and detection using streptavidin-based systems, facilitating pull-down and interaction assays. This peptide is well suited for investigating histone–protein interactions, validating modification-specific antibodies, and characterizing chromatin remodeling mechanisms. It serves as a defined reagent for biochemical and cell-free studies in epigenetics and chromatin biology.

Current Research: Epigenetic regulation governs how genetic information is accessed and interpreted without altering the underlying DNA sequence. Among the central players in this regulatory system are histone proteins, which package DNA into nucleosomes and create the structural foundation of chromatin. The N-terminal tails of histones, in particular, function as regulatory platforms where numerous post-translational modifications (PTMs) occur. These modifications influence chromatin architecture, transcriptional activity, and genome stability. To investigate these complex regulatory processes, defined peptide tools that mimic histone tails have become indispensable. One such reagent is Histone H2A (1–20)-GGK(Biotin), a synthetic peptide that reproduces the N-terminal region of human histone H2A and incorporates a biotin tag for biochemical capture and detection. The Regulatory Importance of the Histone H2A N-Terminal Tail Histone H2A is a core component of the nucleosome, forming a heterodimer with histone H2B and contributing to the structural organization of chromatin. Its N-terminal tail extends outward from the nucleosome surface, making it accessible to regulatory proteins and enzymes. This region contains multiple lysine residues and other amino acids that are commonly modified through processes such as acetylation, ubiquitination, and methylation. These PTMs can significantly influence chromatin structure and gene expression. For example, lysine acetylation on histone tails typically reduces electrostatic interactions between histones and DNA, promoting a more open chromatin configuration that favors transcription. Conversely, certain modifications recruit chromatin-binding proteins that reinforce repressive chromatin states. Because the H2A N-terminal domain participates in these regulatory networks, it has become a focal point for studies of nucleosome stability and chromatin remodeling. Synthetic Histone Peptides as Research Tools Studying histone modifications directly in intact chromatin can be challenging due to the complexity of chromatin structure and the presence of multiple overlapping regulatory mechanisms. Synthetic histone peptides offer a controlled alternative. By isolating a defined segment of the histone protein, researchers can examine specific binding interactions and enzymatic activities in simplified biochemical systems. Histone H2A (1–20)-GGK(Biotin) reproduces the first 20 amino acids of the human H2A protein, representing a key regulatory portion of the histone tail. This sequence encompasses several residues frequently targeted by chromatin-modifying enzymes and histone-binding proteins. Because the peptide lacks the structural complexity of the full nucleosome, it provides a convenient model substrate for in vitro assays that probe histone recognition and modification mechanisms. Biotin Tagging for Efficient Capture and Detection A distinguishing feature of this peptide is the C-terminal glycine–glycine linker followed by a biotinylated lysine residue. Biotin is widely used in molecular biology due to its exceptionally strong affinity for streptavidin and avidin proteins. This interaction enables rapid and highly specific capture of biotin-labeled molecules using streptavidin-coated beads, plates, or biosensors. The inclusion of a flexible glycine–glycine linker helps spatially separate the histone sequence from the biotin tag. This design reduces steric interference and ensures that the histone segment remains accessible for interaction with proteins or enzymes under investigation. As a result, the peptide can be immobilized on streptavidin surfaces while still faithfully presenting the H2A tail sequence for binding studies. Applications in Chromatin and Epigenetics Research Biotinylated histone peptides have become valuable reagents across several experimental workflows in epigenetics. One major application is protein pull-down assays, where the peptide is immobilized via streptavidin and incubated with cell lysates or purified proteins. Interacting partners that recognize the H2A N-terminal region can then be isolated and analyzed using mass spectrometry or immunoblotting. Another important use involves validation of modification-specific antibodies. Histone antibodies must distinguish between closely related sequences and modification states. Synthetic peptides representing defined histone segments provide precise standards for testing antibody specificity and binding affinity. In addition, these peptides are useful for studying chromatin remodeling and histone-binding domains. Many chromatin-associated proteins contain modules—such as bromodomains, chromodomains, or plant homeodomain (PHD) fingers—that recognize particular histone sequences or modification patterns. Immobilized histone peptides allow researchers to evaluate these interactions in controlled biochemical assays. Supporting Mechanistic Studies in Epigenetics As the field of epigenetics continues to expand, tools that enable precise dissection of histone-mediated regulatory processes are increasingly important. Defined histone peptides provide a simplified platform for examining the molecular details of chromatin regulation, from enzyme substrate recognition to protein–protein interaction networks. Histone H2A (1–20)-GGK(Biotin) offers a practical reagent for investigating the early segment of the H2A histone tail while leveraging the convenience of biotin-streptavidin capture systems. By enabling efficient pull-down experiments, interaction mapping, and antibody validation, this peptide supports a wide range of studies aimed at understanding how histone modifications influence chromatin function. As research continues to uncover the connections between epigenetic regulation and diseases such as cancer, neurological disorders, and metabolic conditions, well-defined biochemical reagents like this peptide will remain essential for unraveling the molecular mechanisms that shape gene