PathHunter™ ß-arrestin Assays are revolutionary high-throughput screening assays for monitoring G-protein coupled receptor (GPCR) activation following ligand stimulation, without an imaging instrument, fluorescent protein tag, or radioactivity. Instead, the assays detect GPCR activation through ß-arrestin binding to the expressed GPCR of interest, measuring the interaction of the two proteins using enzyme fragment complementation (EFC)*. The EFC approach offers a range of benefits for screening, including signal amplification, high assay windows, robust performance, and a homogenous, single-addition assay format. The chemiluminescent signal generated can easily be read in 96-, 384- or 1536-well microplates with a standard luminometer, so library screening is simple, fast, and cost effecti...Read more
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Features and Benefits
» Ideally suited for HTS with a single-addition, chemiluminescent detection protocol
» Directly screen broadest range of GPCRs— or deorphanize novel GPCRS
» Using a standard plate reader, the protocol is fast, simple, and reduces operating costs
» Use common cell types
PathHunter™ ß-arrestin Assay Principle
The assay detects binding of an agonist to a GPCR of interest by directly measuring ß-arrestin binding to the GPCR. Once bound, complementation occurs between the two ß-galactosidase components: the ProLink tag is fused to the C-terminus of the GPCR of interest; the Enzyme Acceptor (EA) is attached to ß-arrestin. These components interact only when in close proximity, forming active ß-gal enzyme that converts substrate to detectable signal.*
» ProLink™ Cloning Vector
» PathHunter™ ß-Arrestin CHO-K1, HEK 293, or U2OS Cell Lines
» PathHunter™ Detection Reagents
» Luminometer, Multimode Microplate Reader or CCD Camera
* Covered by issued and pending US and foreign patents.