CALIXAR offers the access to cutting-edge technologies and to characterize ligand interaction with any membrane protein targets. Our ligand binding assays services help scientists and researchers who want to obtain accurate ligand binding parameters, compare several ligands in term of binding properties or just identify a specific interaction of their ligands with the membrane target of interest.
With the first Monolith X (Nanotemper) installed in France, CALIXAR increases its analytical capabilities in ligand binding to any type of membrane protein. Scientists and researchers are assured of having access to the latest technologies to characterize membrane targets.
Thanks to the MicroScale Thermophoresis (MST) combined with isothermal spectral shift detection, CALIXAR offers to determine in solution interactions of membrane proteins with unlabeled ligands. Binding measurements can be performed using purified membrane targets or proteins in complex environment such as cell membrane.
Dynamic range: 1nm to mM
Detected molecule range: 101 – 107 Daltons
Samples per run: Up to 24
Ligand binding assays were performed on full-length wild-type A2A adenosine receptor either in cell membrane fractions (A) or purified in solution (B) and with CGS21680 agonist or ZM241385 inverse agonist using a Monolith X (Nanotemper) combining microscale thermophoresis with isothermal spectral shift detection.
A) A2A adenosine receptor in cell membrane
B) Purified full-length wild-type A2A adenosine receptor
CALIXAR offers ligand binding characterization to any membrane protein using radiolabeled [3H]-ligand.
The well-established and robust radioactive method enables high-sensitive detection of membrane protein / ligand interactions. Binding measurements can be performed using purified membrane targets or proteins in complex environment such as cell membrane.
Filtermat-96 Cell Harvester with MicroBeta2 Microplate Counters.
Simple simultaneous analysis of samples from 96- well microplates for filtration-based receptor binding assays. Radiometric 3H-labeled ligands detection is ensured with high efficiency and extremely low background.
A2AR radioligand binding assays.
Saturation radioligand binding assays were performed on purified full-length wild-type A2A adenosine receptor with [3H]-CGS21680 agonist (A) or [3H]-ZM241385 inverse agonist (B).
A) CGS21680 agonist (Kd 200nM)
B) ZM241385 inverse agonist (Kd 4nM)
CALIXAR identifies challenging protein-ligand interactions by using Fluorescence Polarization.
Fluorescence polarization is a method to measure protein-ligand interactions by detection the changes of small molecule rotation. When a fluorescently labeled small ligand is bound to a bigger protein the emitted light is polarized due to the slow movement of the complex .
Purified Multidrug Efflux Pump subunit AcrB
Ligand binding assay was performed on purified full-length wild-type AcrB with Rhodamine G6 ligand using fluorescence polarization.
AcrB: Rhodamin G6
Kd: 6 µM
Purified Voltage-Gated Sodium Channel (Nav1.7)
Ligand binding assay was performed on purified full-length wild-type Nav1.7 ion channel with protoxin-II (Cy5-ProTx-II) using fluorescence polarization.
All of our clients receive access to our proprietary technology and know-how (8 patent families, more than 28 publications).
The CALIXAR® platform uses patented technology only possible for clients under explicit agreements (license, co-development, and services).
You can leverage CALIXAR’s proprietary technology as well as other leading-in-class membrane protein technology that is not found anyplace else on the market.
Gain access to our specific expertise with a strong track record and several types of membrane proteins. We are continuously integrating best-of-the-art membrane protein characterization technology for our clients’ projects. Our clients have access to all assays needed for their projects, all on one platform.
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Starting from native material or recombinant systems, we succeed with all types of membrane proteins: GPCRs, Ions Channels, Transporters, Receptors and Viral Proteins.
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