The ThunderTM TR-FRET assay platform is based on the use of donor-acceptor fluorophores showing exceptional spectral compatibility and TR-FRET signal:
A long-lifetime and highly stable Europium chelate (Eu) as the donor fluorophore
A small, unique far-red fluorophore (FR) as the acceptor
In a sandwich immunoassay application, one antibody is labeled with the Eu chelate and the second antibody is labeled with the FR fluorophore. The binding of the two labeled antibodies to distinct epitopes on the target protein takes place in solution and brings the two fluorophores into close proximity. Excitation of the donor Eu triggers a FRET to the acceptor FR, which in turn emits a specific TR-FRET signal at 665 nm. Residual (non-transferred) energy from the Eu generates light at 615 nm. These long-lived fluorescent signals are read in a time-resolved manner to minimize assay interference, which increases assay performance and specificity.
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Why choose TR-FRET assays from BioAuxilium?
Better components
Carefully valdiated antibodies
Optimal donor/acceptor fluorophores
Optimized assay components (e.g. buffers)
Rigorous validation
All kits are validated on lysates from activated cells
Technical datasheets contain validation data
Lot-to-lot consistency
Kits are developed and validated in-house
New lots are measured against existing lots to ensure lot-to-lot consistency
Affordability
A superior, cost-effective alternative to ELISA kits
30% cheaper than TR-FRET kits from big suppliers
The Thunder TR-FRET assay platform
The ThunderTM TR-FRET assay platform is based on the use of donor-acceptor fluorophores showing exceptional spectral compatibility and TR-FRET signal:
A long-lifetime and highly stable Europium chelate (Eu) as the donor fluorophore
A small, unique far-red fluorophore (FR) as the acceptor
In a sandwich immunoassay application, one antibody is labeled with the Eu chelate and the second antibody is labeled with the FR fluorophore. The binding of the two labeled antibodies to distinct epitopes on the target protein takes place in solution and brings the two fluorophores into close proximity. Excitation of the donor Eu triggers a FRET to the acceptor FR, which in turn emits a specific TR-FRET signal at 665 nm. Residual (non-transferred) energy from the Eu generates light at 615 nm. These long-lived fluorescent signals are read in a time-resolved manner to minimize assay interference, which increases assay performance and specificity.