dCypher™ assay services reveal the true binding specificity of chromatin readers, enzymes, antibodies, and more. This platform combines EpiCypher’s comprehensive library of recombinant nucleosomes with AlphaScreen® technology, enabling unprecedented throughput and sensitivity. Compared to traditional histone peptide arrays, dCypher also has improved physiological accuracy, requires less protein, and is compatible with full length proteins and domains.
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What are the advantages of dCypher™ assay services?
EpiCypher has considerable experience in developing and optimizing chromatin binding assays, including those for chromatin readers, writer / eraser enzymes, antibodies, and more. dCypher assay services leverage this expertise, combined with our comprehensive library of modified nucleosome and histone peptide substrates, to deliver highly sensitive and customized assays. There are multiple advantages to using dCypher assay services:
- Detect chromatin interactions missed by histone peptide arrays
- Screen against physiologically relevant targets, with access to >80 modified nucleosome substrates
- Assess the binding of histone binding multiple domains in one experiment
- Reduced protein input requirements (average is nM)
- Accommodates full length proteins
- Prior knowledge of histone PTM interactions not necessary
- Have option of profiling against our library of ~300 modified histone peptides, including single and combinatorial histone PTMs
What are the service applications?
applications for dCyhper assay services include:
- Drug target identification and validation
- Reveal novel biological mechanisms
- Determine how modifications impact chromatin enzyme activity
- Examine chromatin reader binding specificity
Publications and Technical Notes
The dCypher platform is starting to make a significant impact in epigenetics research. Learn more about our most recent collaboration, in which the dCypher approach was utilized to support the theorized mechanism of action of NuA4.
- Zukin et al. Structure and Flexibility of the Yeast NuA4 Histone Acetyltransferase Complex. eLife, 2022.
- Weinberg DN, et al. The histone mark H3K36me2 recruits DNMT3A and shapes the intergenic DNA methylation landscape. Nature, 2019.
In another collaboration, the dCypher platform was instrumental in revealing the mechanism of DNMT3A recruitment at intergenic regions.
EpiCypher has also published a series of Technical Notes to help scientists use the dCypher platform in their chromatin research.
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