Recombinant Human STATH protein

Statherin (STATH) is a low-molecular-weight phosphoprotein predominantly secreted by salivary glands in humans and other mammals. It plays a critical role in maintaining oral homeostasis by regulating calcium and phosphate ion saturation in saliva, thereby preventing unwanted precipitation of these minerals on tooth surfaces (anticryptic activity) and inhibiting pathological mineralization like dental calculus formation. Its structure features an N-terminal phosphorylated region that enables strong binding to hydroxyapatite, the mineral component of teeth, and a C-terminal domain rich in proline and tyrosine residues linked to antimicrobial functions.

Recombinant STATH protein is produced using genetic engineering techniques, typically through heterologous expression in bacterial (e.g., E. coli) or eukaryotic systems. While bacterial systems offer cost-effective production, they may lack proper post-translational modifications like phosphorylation critical to STATH's mineral-binding capacity. Advanced expression systems utilizing mammalian cells or modified bacterial strains address this limitation, enabling the generation of functionally active recombinant STATH with preserved bioactivity.

Research applications of recombinant STATH span oral biology and biomaterial science. It serves as a tool to investigate protein-mineral interactions, microbial adhesion mechanisms, and enamel remineralization processes. In translational studies, recombinant STATH has been explored as a bioactive component in dental care products for caries prevention and as a coating agent for dental implants to reduce bacterial colonization. Recent studies also suggest potential roles in wound healing and modulating inflammatory responses, expanding its therapeutic relevance beyond oral health. The development of recombinant variants with enhanced stability or modified functional domains continues to drive innovation in both basic research and clinical applications.