Histone H3 Polyclonal Antibody

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 Histone H3 Polyclonal Antibody can be used for ELISA, flow cytometry (FC), immunoprecipitation (IP), and Western blot (WB) applications. The antibody recognizes histone H3 at 15.5 kDa from human samples.

WARNING This product is not for human or veterinary use.

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).

Zhou, Y., An, L.-L., Chaerkady, R., et al. Evidence for a direct link between PAD4-mediated citrullination and the oxidative burst in human neutrophils. Sci. Rep. 8(1), 15228 (2018).