Recombinant Human TRPV3 protein

TRPV3 (Transient Receptor Potential Vanilloid 3) is a temperature-sensitive, calcium-permeable ion channel belonging to the TRP family. It is primarily expressed in epithelial tissues, including skin keratinocytes, oral mucosa, and the gastrointestinal tract, where it functions as a molecular sensor for warm temperatures (33–39°C). Beyond thermosensation, TRPV3 participates in diverse physiological processes such as skin barrier formation, hair growth, itch transduction, and inflammatory responses. Its dysfunction has been linked to skin disorders (e.g., Olmsted syndrome, pruritus), chronic pain, and neurodegenerative conditions.

Recombinant TRPV3 proteins are engineered in heterologous expression systems (e.g., HEK293 cells, Xenopus oocytes) to study channel structure-function relationships, ligand interactions, and regulatory mechanisms. The full-length protein contains six transmembrane domains, cytoplasmic N- and C-termini, and a pore-forming loop between the fifth and sixth domains. Post-translational modifications (e.g., glycosylation) and lipid microenvironment critically influence its gating behavior and thermal sensitivity.

Research on recombinant TRPV3 has accelerated since its cryo-EM structure was resolved (2018), revealing distinct conformational states and potential drug-binding pockets. These proteins enable high-throughput screening of agonists/antagonists for therapeutic development, particularly targeting inflammatory skin diseases and neuropathic pain. However, challenges persist in maintaining native-like channel properties during recombinant expression, as TRPV3 exhibits sensitization upon repeated activation—a hallmark feature complicating in vitro studies. Current efforts focus on optimizing purification protocols and developing membrane mimetics to preserve functional stability.