AnaSpec Includes Citrullinated Histone in GO® Peptides Collection
Product News Sep 07, 2011
AnaSpec, offers 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.
AnaSpec now offers Histone H1, H2A, H2B, H3 and H4 Modifications (with or without biotin), including citrullinated, acetylated, methylated (mono, di, tri) and phosphorylated.
Chromatin exist either as the transcriptionally active euchromatin or as the transcriptionally repressed heterchromatin state.
Post-translational modifications of histone “tails” (amino termini) have been implicated in the conversion between the two states.
Covalent modifications, such as acetylation, methylation, citrullination and phosphorylation, affect chromatin structure and exquisitely regulate gene expression.
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.
Cuthbert, et al. reported that PAD4 deiminates unmodified arginine and monomethyl, but not dimethyl arginine. Wang, et al. found that PAD4 demethyliminates histones in vitro and in vivo, regulating both histone Arg methylation and gene activity.
Histone hypercitrullination catalyzed by PAD4 appears to play a critical role in chromatin decondensation in granulocytes/neutrophils.