Recombinant Human CLDN16 protein

Claudin-16 (CLDN16) is a key member of the claudin family, a group of transmembrane proteins essential for forming tight junctions in epithelial and endothelial cells. These junctions regulate paracellular permeability, maintaining cellular polarity and selective ion transport. CLDN16 is predominantly expressed in the thick ascending limb of the kidney's loop of Henle, where it plays a critical role in paracellular reabsorption of magnesium (Mg²⁺) and calcium (Ca²⁺). Mutations in the CLDN16 gene are linked to familial hypomagnesemia with hypercalciuria and nephrocalcinosis (FHHNC), a rare autosomal recessive disorder characterized by severe electrolyte imbalances, kidney stones, and progressive renal failure.

Recombinant CLDN16 protein is engineered using biotechnological platforms (e.g., bacterial, mammalian, or insect cell systems) to produce purified, functional protein for research and therapeutic exploration. Its production typically involves cloning the CLDN16 gene into expression vectors, followed by transfection, protein purification (e.g., affinity chromatography), and validation via Western blot or mass spectrometry. Recombinant CLDN16 enables studies on structure-function relationships, disease mechanisms (e.g., how mutations disrupt tight junction integrity), and drug screening for corrective therapies. It also serves as a potential tool for developing protein replacement strategies or gene therapies targeting FHHNC. However, challenges remain in mimicking its native membrane-bound conformation and post-translational modifications, necessitating optimized expression systems. Current research focuses on leveraging recombinant CLDN16 to design in vitro models of renal transport and to identify modulators that enhance or restore its function in disease contexts.