Product Overview
Histone H3 is one of the five main histones involved in the structure of chromatin. H3 has a main globular domain and a long N-terminal tail, and is critical to maintaining the structure of the 'beads on a string' structure of nucleosomes. Histones are subject to various modifications, including phosphorylation, acetylation, glycosylation, methylation, ubiquitination and citrullination. The N-terminus of H3 protrudes from the globular nucleosome core and is susceptible to post-translational modification. In fact, of the five histones, histone H3 is the one that undergoes the most extensive post-transcriptional modifications. The term “Histone H3” does not distinguish between sequence variants or modification state which play a large role in the dynamics and long-term regulation of genes. Histone H3 is an important protein in the emerging field of epigenetics, where its sequence variants and post-translational modifications play a role in the dynamic and long-term regulation of genes.
Histone citrullination, a posttranscriptional modification catalyzed by peptidyl arginine deiminase (PAD) enzymes, is involved in the formation of neutrophil extracellular traps (NETs) — a unique form of cell death that neutrophils undergo — and in human carcinogenesis. NETs help neutralize pathogens and restore homeostasis. However, uncontrolled NET formation (NETosis) is involved in multiple diseases. Citrullinated histone H3 is a NET-specific biomarker.
References:
Hamam HJ, Palaniyar N. Post-Translational Modifications in NETosis and NETs-Mediated Diseases. Biomolecules. 2019 Aug 14;9(8):369. doi: 10.3390/biom9080369.
Zhu D, Zhang Y, Wang S. Histone citrullination: a new target for tumors. Mol Cancer. 2021 Jun 11;20(1):90. doi: 10.1186/s12943-021-01373-z.
Demers M, Wagner DD. NETosis: a new factor in tumor progression and cancer-associated thrombosis. Semin Thromb Hemost. 2014 Apr;40(3):277-83. doi: 10.1055/s-0034-1370765. Epub 2014 Mar 3.