Histone H4 Antibodies

Histone H4 is an important protein in the structure and function of chromatin, where variable modification states e.g. methylation and acetylation play a role in the dynamic and long term regulation of genes.

Histone methylation has been associated with various cellular functions such as transcription, DNA replication, and DNA damage response including repair, heterochromatin formation, and somatic cell reprogramming. Studies have shown that H4R3 methylation appears to be essential in vivo for the establishment or maintenance of a wide range of transcription promoting chromatin modifications. H4R3 methylation blocks subsequent acetylation on the N-terminal tail. However, acetylation of H4 inhibits its methylation by PRMT1.

Acetylation of histone H4 on lysine 16 (

H4K16ac

) is especially important for chromatin structure and function in a variety of eukaryotes and is catalyzed by specific histone lysine acetyltransferases (HATs). H4K16 is particularly interesting because this is the only acetylatable site of the H4 N-terminal tail, and can influence the formation of a compact higher-order chromatin structure. Browse our table below for antibodies against Histone H4.

Antibodies against Histone H4 Modifications

Histone H4 is one of the slowest evolving proteins, only known sequence variants of histone H4 are 13 K --> A (Impaired methylation by N6AMT1) and 32 K --> R (Abolished ufmylation). among the most highly conserved eukaryotic proteins. H4 also shows high conservation in eukaryotic species. It is assumed that the functions of histone proteins involve nearly all of their amino acids so that any change is deleterious to the cell.

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References

Metzger, Wang, Urban, Willmann, Schmidt, Offermann, Allen, Sum, Obier, Cottard, Ulferts, Preca, Hermann, Maurer, Greschik, Hornung, Einsle, Perner, Imhof, Jung, Schüle: "KMT9 monomethylates histone H4 lysine 12 and controls proliferation of prostate cancer cells." in: Nature structural & molecular biology, Vol. 26, Issue 5, pp. 361-371, (2019) (PubMed).

Qin, Yu, Nowsheen, Wang, Tu, Liu, Li, Wang, Lou: "UFL1 promotes histone H4 ufmylation and ATM activation." in: Nature communications, Vol. 10, Issue 1, pp. 1242, (2019) (PubMed).

Kim, Samaranayake, Pradhan: "Epigenetic mechanisms in mammals." in: Cellular and molecular life sciences : CMLS, Vol. 66, Issue 4, pp. 596-612, (2009) (PubMed).

Huang, Litt, Felsenfeld: "Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications." in: Genes & development, Vol. 19, Issue 16, pp. 1885-93, (2005) (PubMed).