Histone Modification Peptides

For studying proteins that interact with histones and histone modifications

Histone post-translational modifications (PTMs) play crucial roles in chromatin regulation, interacting with a wide array of enzymes, reader proteins, and multi-subunit complexes to coordinate downstream processes.

Histone Methylation Peptides

Histone methylation peptides of histone H3 and H4 include mono-methylated, di-methylated, tri-methylated and biotinylated sequences. Among other applications, these epigenetic peptides are useful to researchers conducting studies in enzyme activity and screening inhibitors for specific histone methyltransferases (HMTs).

Histone Acetylation Peptides

Synthesized histone acetylation peptides of histone H3 and H4 include acetylated biotinylated or non-biotinylated sequences. Among other applications, these epigenetic peptides are useful to researchers conducting studies in enzyme activity and inhibitor screening for specific histone acetyltransferases (HATs).

Histone Phosphorylation Peptides

Synthesized histone phosphorylation peptides consist of biotinylated or non-biotinylated peptides phosphorylated at serine residues such as Ser10 and Ser28. Among other applications, these epigenetic peptides are useful for conducting enzyme activity and histone affinity precipitation assays.

Recombinant Nucleosomes

Historically modified histone peptides have been the favored substrate for in vitro chromatin studies, under the assumption that PTMs are unaffected by higher order nucleosome structure. More recent findings (Marunde et al. 2022; Morgan et al. 2021) suggest however, that nucleosome confirmation plays an integral role in dictating histone PTM interactions and chromatin function.

Therefore the use of nucleosome substrates may be essential to generate accurate and physiologically relevant data. BioCat offers a diverse array of recombinant nucleosomes carrying various histone PTMs, histone variants, oncogenic mutations, and more.