We've updated our Privacy Policy to make it clearer how we use your personal data.

We use cookies to provide you with a better experience. You can read our Cookie Policy here.

Advertisement
AnaSpec Includes Citrullinated Histone in GO® Peptides Collection
Product News

AnaSpec Includes Citrullinated Histone in GO® Peptides Collection

AnaSpec Includes Citrullinated Histone in GO® Peptides Collection
Product News

AnaSpec Includes Citrullinated Histone in GO® Peptides Collection


Want a FREE PDF version of This Product News?

Complete the form below and we will email you a PDF version of "AnaSpec Includes Citrullinated Histone in GO® Peptides Collection"

First Name*
Last Name*
Email Address*
Country*
Company Type*
Job Function*
Would you like to receive further email communication from Technology Networks?

Technology Networks Ltd. needs the contact information you provide to us to contact you about our products and services. You may unsubscribe from these communications at any time. For information on how to unsubscribe, as well as our privacy practices and commitment to protecting your privacy, check out our Privacy Policy

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.

Advertisement