[pThr11]-Histone H3 (1-21)-GGK(Biotin)-NH2

Product Name: [pThr11]-Histone H3 (1-21)-GGK(Biotin)-NH2

Sequence One Letter Code: ARTKQTARKS-pT-GGKAPRKQLA-GGK(Biotin)-NH2

Sequence Three Letter Code: H-Ala-Arg-Thr-Lys-Gln-Thr-Ala-Arg-Lys-Ser-pThr-Gly-Gly-Lys-Ala-Pro-Arg-Lys-Gln-Leu-Ala-Gly-Gly-Lys(Biotin)-NH2

Molecular Weight: 2802.3

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: [pThr11]-Histone H3 (1–21)-GGK(Biotin)-NH₂ is a synthetic N-terminal histone H3 peptide phosphorylated at threonine 11 and biotinylated at the C-terminus. Phosphorylation at H3T11, catalyzed by kinases such as PRK1 and Chk1, functions as a dynamic chromatin mark involved in transcriptional regulation and DNA damage–associated transcriptional repression. The C-terminal biotin label enables affinity purification and interaction studies with phospho-specific reader proteins. This peptide is widely used in epigenetics research to investigate histone phosphorylation signaling, modification cross-talk, and chromatin-based regulatory mechanisms under physiological and stress conditions.

Current Research: Histone phosphorylation is an important post-translational modification that regulates chromatin dynamics and gene expression in response to cellular signaling and stress. Unlike histone acetylation and methylation, which are often associated with relatively stable chromatin states, histone phosphorylation functions as a rapid and reversible regulatory signal that links extracellular stimuli and intracellular signaling pathways to chromatin regulation. One such modification is phosphorylation at threonine 11 of histone H3 (H3T11ph), a mark that has gained increasing attention for its roles in transcriptional control, cell cycle regulation, and DNA damage responses. Synthetic peptides such as [pThr11]-Histone H3 (1–21)-GGK(Biotin)-NH₂ provide a defined molecular tool for studying this modification and identifying proteins that recognize phosphorylated histone residues. A key focus of current research involves identifying the kinases responsible for catalyzing H3T11 phosphorylation and understanding how this modification integrates with cellular signaling pathways. Studies have shown that kinases such as protein kinase C–related kinase 1 (PRK1) and checkpoint kinase 1 (Chk1) can phosphorylate H3T11 under specific conditions. PRK1-mediated phosphorylation has been linked to transcriptional activation in hormone-responsive genes, particularly in contexts such as androgen receptor signaling. In contrast, Chk1-mediated phosphorylation has been associated with DNA damage responses, where it contributes to transcriptional repression at damaged chromatin regions. Investigating these kinase–substrate interactions is critical for understanding how signaling pathways directly influence chromatin-based gene regulation. Another major research area concerns the interaction of phosphorylated histone residues with chromatin reader proteins. Phosphorylation can alter the binding properties of histone tails, influencing the recruitment or exclusion of regulatory complexes. The biotin tag attached to the peptide enables immobilization on streptavidin-coated matrices, allowing researchers to perform affinity pull-down assays that capture proteins capable of recognizing the H3T11ph modification. These experiments are commonly combined with mass spectrometry–based proteomic analysis to identify chromatin-associated factors that interact with phosphorylated histone marks. H3T11 phosphorylation is also an important component of histone modification cross-talk, where multiple post-translational modifications interact to regulate chromatin structure and gene expression. Phosphorylation events can influence the activity of enzymes responsible for other histone modifications, such as acetylation or methylation. For example, H3T11 phosphorylation has been shown to facilitate the recruitment of histone acetyltransferases that promote transcriptional activation. Synthetic histone peptides containing defined phosphorylation marks enable researchers to systematically analyze how phosphorylation affects the binding of chromatin regulators and how it cooperates with other epigenetic modifications. In addition to transcriptional regulation, H3T11 phosphorylation has been implicated in cellular responses to stress and DNA damage. During genotoxic stress, chromatin undergoes structural changes that facilitate DNA repair and coordinate transcriptional repression near damaged regions. Kinase-mediated phosphorylation of histone residues, including H3T11, contributes to these chromatin remodeling processes. By using defined peptide substrates, researchers can investigate how phosphorylation alters the recruitment of DNA repair proteins and transcriptional regulators. Another growing area of research involves the use of histone phosphorylation peptides in epigenetic drug discovery and inhibitor screening. Because kinases such as PRK1 and Chk1 participate in pathways relevant to cancer progression and stress responses, understanding how they modify chromatin is important for therapeutic development. Peptides representing phosphorylated histone sequences provide valuable tools for studying enzyme activity and for identifying compounds that influence kinase-mediated chromatin signaling. The peptide is also useful in biochemical and structural studies of chromatin-associated protein complexes. By providing a well-defined modification state, synthetic histone fragments allow researchers to analyze the binding preferences of chromatin readers under controlled conditions. These experiments help reveal how specific histone modifications guide the assembly of transcriptional regulatory complexes. In summary, [pThr11]-Histone H3 (1–21)-GGK(Biotin)-NH₂ is an important reagent in epigenetics and chromatin biology research. Its defined phosphorylation mark and biotin affinity tag enable detailed investigation of histone phosphorylation–dependent protein interactions, kinase signaling pathways, and chromatin regulatory mechanisms. Through applications in affinity purification, proteomics, and biochemical assays, this peptide continues to support research aimed at understanding how phosphorylation integrates cellular signaling with chromatin-based gene regulation.