Host: E. coli • AA: 1-136 (full length) • MW: 15.5 kDa
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Measurement and Detection Target(s)
13781Histone H3 Polyclonal Antibody
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Histone H3 (human, recombinant)

Item No. 10263

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • H3C1
  • Histone H3.1
Purity
≥95% estimated by SDS-PAGE
Source
Recombinant human histone H3 expressed in E. coli
Amino Acids
1-136 (full length)
MW
15.5 kDa
Formulation (Request formulation change)
A solution in water (frozen)
UniProt Accession №
P68431
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

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    100 µg

    $138

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    1 mg

    $690

    Add
    NET Formation Screening & Analysis Services
    Our experts are here to help.
    • Detection of NET formation ex vivo and screening for modulators using:
      • High-content imaging
      • Enzymatic detection
      • Citrullination/carbamylation detection
    • Experienced scientists skilled in neutrophil biology, isolation, and handling
    LEARN MORE
    Product Description

    Histone H3 is a nuclear protein and a component of the nucleosome core, a basic unit of chromatin, that is essential for organizing genomic DNA in eukaryotic nuclei.1 It is a globular protein that contains an unstructured N-terminal tail that extends outside of the nucleosome core and is subject to various post-translational modifications (PTMs), including methylation, phosphorylation, acetylation, and citrullination.1,2 Histone H3 PTMs function as epigenetic regulators of gene transcription by affecting chromatin structure and providing binding sites for many transcription factors, thus regulating several cellular functions including gene expression, cell cycle, and DNA replication and repair.1,3 Differential methylation of histone H3 at various lysine residues is catalyzed by SET domain-containing methyltransferases and marks sites of transcriptional activation or repression.1 Citrullination of histone H3 by protein arginine deiminase 4 (PAD4; Item Nos. 10500 | 25915 | 28910) or PAD2 (Item No. 10785) induces the release of neutrophil extracellular traps (NETs), a network of decondensed DNA and intracellular proteins secreted by neutrophils as a pathogen defense mechanism.4,5 Histone H3 mutations have been found in patients with diffuse intrinsic pontine glioma, leukemia, or chondroblastoma.6

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Hyun, K., Jeon, J., Park, K., et al. Writing, erasing and reading histone lysine methylations. Exp. Mol. Med. 49(4), e324 (2017).

    2. Sharda, A., Amnekar, R.V., Natu, A., et al. Histone posttranslational modifications: Potential role in diagnosis, prognosis, and therapeutics of cancer. Prognostic Epigenetics 15, 351-373 (2019).

    3. Filipescu, D., Müller, S., and Almouzni, G. Histone H3 variants and their chaperones during development and disease: Contributing to epigenetic control. Annu. Rev. Cell Dev. Biol. 30, 615-646 (2014).

    4. Leshner, M., Wang, S., Lewis, C., et al. PAD4 mediated histone hypercitrullination induces heterochromatin decondensation and chromatin unfolding to form neutrophil extracellular trap-like structures. Front. Immunol. 3, 307 (2012).

    5. Liang, Y., Pan, B., Alam, H.B., et al. Inhibition of peptidylarginine deiminase alleviates LPS-induced pulmonary dysfunction and improves survival in a mouse model of lethal endotoxemia. Eur. J. Pharmacol. 833, 432-440 (2018).

    6. Lowe, B.R., Maxham, L.A., Hamey, J.J., et al. Histone H3 mutations: An updated view of their role in chromatin deregulation and cancer. Cancers (Basel) 11(5), 660 (2019).

    Product Citations

    Zaranski, K.J., Yang, M., Scaletta, L.R., et al. NLRP3 inflammasome promotes PAD2/PAD4 release and protein citrullination in rheumatoid arthritis. Commun. Biol. (2026).

    Thålin, C., Aguilera, K., Hall, N.W., et al. Quantification of citrullinated histones: Development of an improved assay to reliably quantify nucleosomal H3Cit in human plasma. J. Thromb. Haemost. 18(10), 2732-2743 (2020).

    Thålin, C., Daleskog, M., Göransson, S.P., et al. Validation of an enzyme-linked immunosorbent assay for the quantification of citrullinated histone H3 as a marker for neutrophil extracellular traps in human plasma. Immunol. Res. 65(3), 706-712 (2017).