Carna Biosciences, Inc.

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Protein-Protein Interaction Detection Assay

Our split luciferase complementation assay utilizing a unique luciferase derived from Pyrearinus termitilluminans (Emerald Luciferase, E-Luc) is a valuable tool for for your study of Protein-Protein Interactions (PPI). This enables detection of various types of PPIs, including GPCRs, with ease and high-sensitivity.

In addition to established cell lines on the list, we develop custom stable transfected cell lines suitable to detect specific PPIs of your interest!

Split Luciferase Technology

E-Luc is known to emit a brighter and more stable signal than conventional firefly luciferases. The N- and C-terminal domains of luciferase can be separated into two fragments, which can re-associate in cells. When those two fragments of the fused reporter proteins are brought within proximity, they spontaneously refold and generate a detectable signal (patent filed).


Pyrearinus termitilluminans and Bioluminescence
Photo Credit: Courtesy of Dr. Yoshihiro Ohmiya, The National Institute of Advanced Industrial Science and Technology (AIST)
Ligand; DAMGO, 10μM

Ligand; DAMGO, 10μM/
Antagonist; Diprenorphine, 0.1μM

DAMGO stimulation of ORPM1-Eluc-C and ELucN-b-arrstin 1 co-expressing HEK293 cells in the presence or absence of diprenorphine

Application for GPCR

The N-terminal and C-terminal fragments of the split luciferase are fused to β-arrestin and GPCR, respectively. Binding of a ligand to GPCR triggers phosphorylation of the GPCR, thereby inducing its interaction with β-arrestin. This interaction brings the N-terminal luciferase into proximity with the C-terminal luciferase, and bioluminescence activity is measurable.
We can develop transfected cell lines not listed on the Stable Cell Line List upon request.