Temperature Related intensity Chang (TRlC)
TRIC (Temperature-dependent Intensity Change) is a fluorescence-based technique that measures the strength of biomolecular interactions by detecting changes in fluorescence intensity of a labeled target molecule when it binds to a ligand, which are amplified by a brief, precise temperature increase using an infrared laser, essentially allowing for high-throughput screening and affinity determination of various biomolecules like membrane proteins, protein complexes, and cell lysates in a homogeneous microplate format, as facilitated by the NanoTemper Dianthus NT.23 Pico Duo instrument at Biortus.
Benefits：
Do more with less protein.
Measure broad range of interaction, including protein-ion/carbohydrate.
Measure Kd independent of size and mass of binding partners.
Measure in solution, in close to native conditions, no immobilization required.
Applications:
Kd measurement in solution, include cell lysate
Membrane Protein
Fragment screening
Cell lysate
Directly Kd measurement
GPCRs
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Class A
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Class B
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Class C
Cytosolic
Proteins
Other membrane proteins
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SLC
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Transporter
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Ion Channel
Biophysical Assays
