Citrullinated Histone H3 (Arg2) (F3C9B) Rabbit mAb (IHC Formulated) #26111
- IHC
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Immunohistochemistry (Paraffin) | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Citrullinated Histone H3 (Arg2) (F3C9B) Rabbit mAb (IHC Formulated) recognizes histone H3 citrullinated at residue Arg2. This antibody does not cross-react with any other known citrullinated or methylated arginine residues on histone H3.
Species Reactivity:
Human, Mouse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of histone H3 in which Arg2 is citrullinated.
Background
The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Histone post-translational modifications, such as methylation, acetylation, ubiquitination, and citrullination, influence chromatin accessibility and regulate gene expression (1). Histone citrullination is carried out by protein arginine deiminases (PADs), which convert positively charged arginine residues into neutral citrulline (2). Histone citrullination affects the binding of histone reader proteins to chromatin, and it is associated with both transcriptional activation and repression (3-5). Histone citrullination is also a major marker for NETosis, which is a programmed cell death mechanism carried out by neutrophils (6). Deregulation of NETosis is associated with multiple autoimmune diseases, including rheumatoid arthritis (RA) and lupus (7,8). Histone hypercitrullination via PAD4 may also play a role in the progression of various cancers, including multiple myeloma (MM), acute myeloid leukemia (AML), lung cancer, and hepatocellular carcinoma (HCC) (9-12).
- Shanmugam, M.K. et al. (2018) Oncotarget 9, 11414-11426.
- Fuhrmann, J. and Thompson, P.R. (2016) ACS Chem Biol 11, 654-68.
- Wang, Y. et al. (2004) Science 306, 279-83.
- Cuthbert, G.L. et al. (2004) Cell 118, 545-53.
- Zhang, X. et al. (2012) Proc Natl Acad Sci USA 109, 13331-6.
- Hamam, H.J. and Palaniyar, N. (2019) Biomolecules 9, 369. doi: 10.3390/biom9080369.
- Corsiero, E. et al. (2016) Front Immunol 7, 485.
- Hakkim, A. et al. (2010) Proc Natl Acad Sci U S A 107, 9813-8.
- McNee, G. et al. (2017) Leukemia 31, 373-381.
- Song, G. et al. (2016) Oncotarget 7, 3144-57.
- Tanikawa, C. et al. (2012) Nat Commun 3, 676.
- Lu, M. et al. (2020) J Med Virol 92, 1221-1230.
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