Epigenetic Proteins Product Highlights
- Biologically Relevant - Obtain quantitative cellular compound entry and epigenetic target binding data for more confident drug discovery decisions
- Easy-to-Use & Scalable - Simple, homogeneous, and high-throughput amenable protocol to easily measure compound binding to your epigenetic target with a chemiluminescent readout
- Target Specificity & Selectivity - Ability to screen and differentiate multiple target-selective stereoisomers of BRD4 and determine target specificity
- High Quality Proteins - Access epigenetics-related recombinant proteins produced using optimal expression systems with high quality and purity
Key Resources
Application Note: Automating a Cell-Based Target-Compound Assay for Methyltransferase and Bromodomain.
Scientific Posters & Presentations
Related Topic: InCELL Target Engagement Assays
InCELL Hunter Assay Principle
InCELL Hunter stabilization assays are based on the industry validated Enzyme Fragment Complementation (EFC) technology and built on the principle of protein stabilization related to the protein turnover. Cells expressing a protein of interest is fused to the small EFC enzyme donor of β-galactosidase (β-gal) called ePL (enhanced ProLabel®). Upon addition of a compound that binds the target, protein levels are stabilized or altered in the cell, and this change can be monitored by measuring target protein abundance using chemiluminescent detection. Upon addition of the large EFC enzyme acceptor (EA) fragment and chemiluminescent substrate, EA naturally complements with the ePL tag on the target protein to create an active β-gal enzyme. The resulting active enzyme hydrolyzes the substrate to generate a chemiluminescent signal. The greater the signal, the greater the presence of compound-target engagement in the cell.
InCELL Pulse Assay Principle
InCELL Pulse™ compound-target engagement assays are based on the EFC technology incorporating compound binding detection based on protein thermal stability. Cells expressing a protein of interest is fused to the small EFC β-gal enzyme donor ePL. These cells are treated with test compound and then subjected to elevated temperatures during a pulse denaturation step. The larger EFC enzyme donor (EA) of β-gal is then added with a chemiluminescnet substrate and EFC complementation. Compound binding protects the target protein from thermal denaturation, which enhances complementation between added EA and ePL components and increases the chemiluminescent signal measured using the EFC-based detection system. In the absence of compound binding, the target protein forms denatured aggregates that poorly complement with EA, which results in a low chemiluminescent signal.