Histone H3 Antibodies

Structure of Histone H3

Histone H3 is a core histone with a molecular weight of approximately 15.4 kDa. Its molecular weight varies slightly among different species, mainly due to variations in the N-terminal tail of the amino acid sequence. The molecular weight and characteristics of histone H3 in humans and common model organisms are as follows:

This protein is composed of 135 amino acids, forming a typical long N-terminal tail-spherical core structure. Its spherical domain forms histone folding through a helical-ring-helical motif, mediating the assembly of H3-H4 tetramers. The extended N-terminal tail segment presents a disordered conformation, providing a molecular basis for histone modification. In the spatial configuration, this protein forms a triple helix bundle through a helical arrangement of α 1-ring -α2-α3. Among them, the L1 ring and the α2 helix directly participate in the interaction of the DNA phosphate skeleton, while the 116th cysteine reversibly oxidizes and modifies to regulate the higher structure of chromatin. This structural characteristic makes histone H3 a key carrier for epigenetic regulation.

Fig. 1 Structure of histone H3 in the histone octamer.¹

Key structural properties of Histone H3:

• Conserved histone folding domains, linked by three sets of α-helices via short loops
• Distribution of positively charged amino acids
• Flexible N-terminal tail structure, providing binding sites for epigenetic modification

Functions of Histone H3

The core function of histone H3 is to participate in nucleosome assembly and regulate gene expression. Its specific functions include:

Unlike the histone variant H3.3 which replaces the classical H3.1 in the transcriptional active region, the classical subtype of H3 mainly incorporates into chromatin during the DNA replication period. This difference reflects its unique role in maintaining epigenetic memory.

Applications of Histone H3 and Histone H3 Antibody in Literature

1. Lai, Po Man, Xiaoxiang Gong, and Kui Ming Chan. "Roles of Histone H2B, H3 and H4 Variants in cancer development and prognosis." International Journal of Molecular Sciences 25.17 (2024): 9699. https://doi.org/10.3390/ijms25179699

The article indicates that histone H3 variants play a significant role in key biological processes such as DNA damage repair and transcriptional regulation. Recent studies have revealed novel variants of them in various cancers, and their expression levels have significant prognostic assessment value.

2. Collins, Bridget E., et al. "Histone H3 lysine K4 methylation and its role in learning and memory." Epigenetics & chromatin 12.1 (2019): 7. https://doi.org/10.1186/s13072-018-0251-8

The article indicates that the methylation of histone H3 lysine 4 (H3K4) is a key epigenetic mechanism in the formation of learning and memory. The abnormal reading, writing and erasing of this modification are directly related to cognitive disorders such as hippocampus memory function deficiency and human intellectual disability. This review will explore its regulatory mechanism and its association with neurocognitive impairment.

3. Klein, Rachel H., and Paul S. Knoepfler. "Knockout tales: the versatile roles of histone H3. 3 in development and disease." Epigenetics & Chromatin 16.1 (2023): 38. https://doi.org/10.1186/s13072-023-00512-8

The article indicates that the histone variant H3.3 plays a key role in gamete formation, brain-lung development and other processes, and is crucial for maintaining genomic stability. The deletion or mutation of the H3.3 encoding genes H3f3a and H3f3b can damage chromatin organization, leading to developmental defects and being closely related to human diseases such as pediatric tumors and neurodevelopmental syndromes.

4. Hillje, Roman, et al. "Time makes histone H3 modifications drift in mouse liver." Aging (Albany NY) 14.12 (2022): 4959. https://doi.org/10.18632/aging.204107

The article indicates that to detect the drift of epigenetics over time, the study found that the modifications of multiple histone H3 sites in the liver of mice would be redistributed across the entire genome with age, especially in the intergenic regions and near the transcription start sites. Calorie-restricted diets can effectively slow down such H3 modification changes related to aging.

5. Gleason, Ryan J., et al. "Developmentally programmed histone H3 expression regulates cellular plasticity at the parental-to-early embryo transition." Science advances 9.14 (2023): eadh0411. https://doi.org/10.1126/sciadv.adh0411

This study reveals that during embryonic development, the genomic landscape of histone H3 expression undergoes significant changes, that is, it shifts from a state rich in H3.3 to one rich in conventional H3. This transformation is regulated by the differential expression of different histone gene clusters, thereby limiting developmental plasticity and regulating the function of germline chromatin.

Creative Biolabs: Histone H3 Antibodies for Research

Creative Biolabs specializes in the production of high-quality Histone H3 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom Histone H3 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our Histone H3 antibodies, custom preparations, or technical support, contact us at email.