CALIXAR’s Solute carrier family 12 member 5 (hKCC2) facilitates reliable fragment-based drug design (FBDD), structure-based drug discovery (SBDD)and antibody discovery against this specific target.
Unlike Calixar’s hKCC2, other possible methods result in a potassium chloride cotransporter that becomes mutated and truncated (96 amino-acids at the C-terminus). In addition, this mutated version converts to a locked conformation within an antagonist.
As with all co-transporters and ion channels, hKCC2 membrane proteins are unstable targets and are difficult to produce natively with conventional procedures. Traditionally, the Solute carrier family 12 member 5 was never isolated from the membrane without causing aggregates due to its unstable construction.
Contrarily, Calixar’s co-transporters are the only original native and purified K-Cl cotransporter 2 on the market as it has been shown to be active in electrophysiology and thallium assays.
Our purified hKCC2 membrane protein can bind to antagonist compounds using SPR. This preparation permits the first functional architecture of hKCC2 reported up to date (Agez M. et al., 2017, Scientific Reports).
Our K-Cl cotransporter 2 maintains its structural and functional integrity and is purified and stabilized to full length and wild-type (native) protein. This membrane target has the ability to bind to an open and wide range of compounds including agonists, antagonists, and allosteric modulators.
- Antibodies (including nanobodies, scaffold proteins, aptamers)
- Small molecules
- 3D Structures (classical X-ray or XFEL, Cryo-EM, NMR)
- Drug discovery (Screening: HTS, FBDD, SBDD; Hit and lead validation)
- Antibody discovery (Immunization and display technologies)
- Clinical stage (drug validation on reliable native KCC2)