Citrullinated Histone Peptides are GO

AnaSpec, the world's largest provider of on-demand GO peptides is pleased to offer a wide selection of Histone H1, H2A, H2B, H3 and H4 peptides, especially the H3 peptides. The rapidly expanding Histone GO Peptides now include citrullinated sequences in addition to sequences that are acetylated, mono-, di- or tri-methylated, phosphorylated and biotinylated.

Histone Modifications (with or without biotin):



Methylated (mono, di, tri)


Chromatin exist either as the transcriptionally active euchromatin or as the transcriptionally repressed heterchromatin state.1 Post-translational modifications of histone "tails" (amino termini) have been implicated in the conversion between the two states. 1-2 Covalent modifications, such as acetylation, methylation, citrullination and phosphorylation, affect chromatin structure and exquisitely regulate gene expression.3-6 In histones, citrullination or deimination of arginine to citrulline (Cit), a non-conventional amino acid in protein is mediated by peptidylarginine deiminase type 4 (PAD4 or PADI4) in the presence of Ca2+; with PAD4 being the only PAD with a nuclear localization.7-9 Cuthbert, et al. reported that PAD4 deiminates unmodified arginine and monomethyl, but not dimethyl arginine.9 Wang, et al. found that PAD4 demethyliminates histones in vitro and in vivo, regulating both histone Arg methylation and gene activity.10 Histone hypercitrullination catalyzed by PAD4 appears to play a critical role in chromatin decondensation in granulocytes/neutrophils.11

Table 1. A listing of citrullinated histone peptides.



Catalog #

[Cit2/8/17]-Histone H3 (1-21)-GGK(Biotin), amide

0.25 mg


[Cit17]-Histone H3 (1-21)-GGK(Biotin)

1 mg


[Cit26]-Histone H3 (21-44)-GGK(Biotin)

1 mg


[Cit3]-Histone H4 (1-23)-GGK(Biotin)

1 mg


Click to view entire listing of Histone: Histone peptides.


1. Grunstein, M. et al. J Cell Sci Suppl 19, 29 (1995).
2. Strahl, BR and CD Allis, Nature 403, 41 (2000).
3. Strahl, BD. et al. Proc. Natl Acad Sci 96, 14967 (1999).
4. Jenuwein, T. and CD. Allis, Science 293, 1074 (2001).
5. Sterner, DE. et al. Microbiol Mol Biol Rev 64, 435 (2000).
6. Lachner, M. et al. J Cell Sci 116, 2117 (2003).
7. Vossenaar, ER. et al. Bioassays 25, 1106 (2003).
8. Nakashima, K. et al. J Biol Chem 277, 49562 (2002).
9. Cuthbert, GL. et al. Cell 118, 545 (2004).
10. Wang, Y. et al. Science 306, 279 (2004).
11. Wang, Y. et al. J Cell Bio 184, 205 (2009).