For immunochemical detection of histone H3
Related Products
Alternative(s)
13781Histone H3 Polyclonal Antibody
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Anti-Histone H3 pan Rabbit Monoclonal Antibody (Clone RM188)

Item No. 20724

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • H3
Immunogen
Peptide corresponding to the C-terminus of human histone H3
Clone Designation
RM188
Formulation (Request formulation change)
100 µg of protein A affinity-purified antibody from an animal origin-free culture supernatant
Storage Buffer
50% glycerol/PBS containing 1% BSA and 0.09% sodium azide
Host
Rabbit
Isotype
IgG
Applications
ELISA, ICC, multiplex-based assays, WB
Cross Reactivity
(+) All histone H3 proteins, independent of post-translational modifications(-) H2A(-) H2B(-) H4
Species Reactivity
(Independent) Species
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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.

Download most recent Certificate of Analysis for this product

    100 µg

    $500

    Add
    Cayman Chemical
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    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.6,7 Cayman's Anti-Histone H3 pan Rabbit Monoclonal Antibody (Clone RM188) can be used for ELISA, immunocytochemistry (ICC), multiplex-based assays, and Western blot (WB) applications. The antibody recognizes all histone H3 proteins independent of post-translational modifications.

    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).

    7. Wan, Y.C.E., Liu, J., and Chan, K.M. Histone H3 mutations in cancer. Curr. Pharmacol. Rep. 4(4), 292-300 (2018).