EpiCypher is an epigenetics company founded in 2012 by Drs. Mark Bedford, Or Gozani, Brian Strahl, and James Bone in response to the growing demand for high-quality reagents and tools to study chromatin regulation and enable epigenetics-focused drug development.
EpiCypher is the global leader in recombinant nucleosome manufacturing and development. Using proprietary methods, we are continuously adding to the world’s largest collection of highly pure modified recombinant “designer” nucleosomes (dNucs™). EpiCypher’s broad dNuc™ diversity is providing a powerful tool to decipher the histone code and accelerate drug development. Shah et al., Wang et al., and Weinberg et al. (see below) are just a few examples of the many benefits of using nucleosome substrates for epigenetics studies.
EpiCypher leverages dNuc™ technology for a wide range of applications, including: SNAP-ChIP® Spike-in Controls (for antibody profiling and quantitative ChIP), EpiDyne® substrates (for characterizing chromatin remodeling enzyme complexes and inhibitors), and dCypher™ assays (for interrogation of epigenetic protein-histone PTM binding interactions). We also offer a suite of high-quality recombinant histone binding proteins, enzymes, peptides, antibodies, and custom assay development services to complement these platforms.
EpiCypher continuously pushes technology boundaries to deliver innovative products, solutions, and services to epigenetics and chromatin biology researchers. Most recently, EpiCypher has been at the leading edge of chromatin mapping technology improvements with the recent launch of the highly sensitive epigenomic mapping CUTANA™ assays for ChIC, CUT&RUN, and CUT&Tag.
From our strong scientific expertise and rigor to our focus on customer success, EpiCypher is proud to be an epigenetics company For Scientists, By Scientists.
Featured Co-Authored Publications
Examining the roles of H3K4 methylation states with systematically characterized antibodies
Histone H1 loss drives lymphoma by disrupting 3D chromatin architecture
Two competing mechanisms of DNMT3A recruitment regulate the dynamics of de novo DNA methylation at PRC1-targeted CpG islands
H3K36me2 recruits DNMT3A and shapes the intergenic DNA methylation landscape
Journal of Thrombosis and Haemostasis
Quantification of citrullinated histones: Development of an improved assay to reliably quantify nucleosomal H3Cit in human plasma
Decoding the Protein Composition of Whole Nucleosomes with Nuc-MS