Histone H2B (21-41)-GGK(Biotin)

Product Name: Histone H2B (21-41)-GGK(Biotin)

Sequence One Letter Code: AQKKDGKKRKRSRKESYSIYV-GGK(Biotin)

Sequence Three Letter Code: H-Ala-Gln-Lys-Lys-Asp-Gly-Lys-Lys-Arg-Lys-Arg-Ser-Arg-Lys-Glu-Ser-Tyr-Ser-Ile-Tyr-Val-Gly-Gly-Lys(Biotin)-OH

Chemical Formula:C131H223N43O37S1

Molecular Weight: 3024.7

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: This peptide corresponds to residues 21–41 of histone H2B and contains a C-terminal glycine–glycine (GG) linker followed by a biotinylated lysine residue. The biotin tag enables strong binding to streptavidin-coated surfaces, facilitating affinity purification, pull-down assays, and protein interaction studies. Histone H2B is an important component of the nucleosome core particle and participates in the regulation of chromatin structure and gene expression. By providing a defined histone sequence with a convenient affinity handle, this peptide supports investigations of histone-binding proteins, chromatin remodeling complexes, and epigenetic enzyme activity. It is widely used in chromatin biology research, including studies of transcriptional regulation, nucleosome dynamics, and histone modification–dependent protein interactions.

Current Research: Introduction to Histone-Based Peptide Probes Histone proteins form the structural foundation of chromatin and play essential roles in regulating gene expression and genome organization. Within the nucleosome core particle, histones H2A, H2B, H3, and H4 assemble with DNA to create a dynamic chromatin structure that controls access to genetic information. Short synthetic peptides derived from histone sequences are widely used in biochemical studies to investigate chromatin-binding proteins and epigenetic regulatory mechanisms. The Histone H2B (21–41) peptide with a C-terminal GG linker and biotinylated lysine provides a convenient experimental probe for analyzing protein interactions with histone sequences. The addition of a biotin affinity tag allows the peptide to be easily captured on streptavidin-coated surfaces, enabling a wide range of affinity-based assays. Structural Features of the H2B (21–41) Peptide This peptide corresponds to residues 21–41 of histone H2B, a region within the N-terminal portion of the protein that participates in chromatin regulation and protein interaction. Histone H2B is a core component of the nucleosome, where it pairs with histone H2A to form H2A–H2B dimers that help organize DNA around the nucleosome core. The peptide includes a C-terminal glycine–glycine (GG) linker, followed by a biotinylated lysine residue. The GG linker provides flexibility between the histone-derived sequence and the biotin tag, helping preserve accessibility of the peptide for protein binding studies. Because the peptide reproduces a defined region of the histone tail while incorporating a strong affinity handle, it can be used to mimic histone sequences in controlled biochemical experiments. Role of the Biotin Tag in Affinity-Based Assays The biotin–streptavidin interaction is one of the strongest known non-covalent interactions in biology. By attaching a biotin group to the peptide, researchers can easily immobilize the peptide on streptavidin-coated beads, plates, or biosensor surfaces. This property enables the peptide to be used in a variety of affinity purification and interaction assays, including: Pull-down assays for identifying histone-binding proteins Affinity purification of chromatin-associated complexes Protein–peptide interaction studies Surface-based binding assays The strong and specific binding between biotin and streptavidin ensures stable immobilization of the peptide during experimental procedures. Applications in Histone-Binding Protein Studies The H2B (21–41) peptide is commonly used to investigate proteins that interact with histone sequences. Many regulatory proteins recognize specific regions of histone tails to control chromatin accessibility and transcriptional activity. By immobilizing the peptide on streptavidin-coated matrices, researchers can capture proteins that bind to the H2B sequence. These experiments help identify histone-binding factors, including chromatin-associated proteins and regulatory complexes. Studying these interactions provides insight into how chromatin structure is dynamically regulated within the cell. Investigating Chromatin Remodeling and Epigenetic Enzymes Chromatin structure is continuously modified by enzymes and complexes that regulate nucleosome positioning, histone modifications, and DNA accessibility. The H2B-derived peptide can be used to examine chromatin remodeling complexes and histone-modifying enzymes that interact with specific histone sequences. For example, enzyme assays may use histone peptides to evaluate the activity of proteins that catalyze histone modifications or interact with histone tails during transcriptional regulation. Because the peptide provides a defined substrate sequence, it allows precise analysis of enzyme specificity and protein recognition. These studies are essential for understanding the molecular mechanisms underlying epigenetic regulation of gene expression. Applications in Chromatin Biology Research Biotinylated histone peptides such as H2B (21–41) are widely used in chromatin biology research. By combining a defined histone sequence with a convenient affinity tag, the peptide supports experiments exploring how histone interactions influence chromatin organization and gene regulation. Typical applications include: Characterizing chromatin-binding proteins Investigating nucleosome dynamics Studying transcriptional regulation mechanisms Analyzing histone modification–dependent interactions These studies help clarify how histone sequences function as regulatory platforms within chromatin. Conclusion The biotinylated Histone H2B (21–41) peptide provides a useful tool for investigating protein interactions with histone sequences and studying mechanisms of chromatin regulation. The incorporation of a GG linker and C-terminal biotin tag enables strong binding to streptavidin-coated surfaces, facilitating affinity purification and interaction assays. Widely used in pull-down assays, chromatin-binding studies, and epigenetic enzyme investigations, this peptide supports research exploring transcriptional regulation, nucleosome dynamics, and histone-dependent signaling pathways. Through these applications, it contributes to a deeper understanding of chromatin biology and epigenetic control of gene expression.