In 1988, our laboratory discovered a novel soluble binding-protein for the neurotoxin, saxitoxin, in plasma of the bullfrog, Rana catesbeiana. STX is small cationic molecule produced by toxic dinoflagellates in the ocean and cyanobacteria in freshwater environments. The frog STX-binding protein (named saxiphilin) is homologous to the transferrin family of Fe3+-binding proteins that include serum transferrin, lactoferrin, and melanotransferrin. It has since become clear that saxiphilin is just one example of number of transferrin-related proteins that do not bind Fe3+. However, little is known about the function of such proteins. We are currently working on improved methods for production of recombinant saxiphilin. Saxiphilin will be used to develop a fluorescence-based assay for saxitoxin, which is the toxic principle of paralytic shellfish poisoning in humans. We also plan to clone related saxiphilin genes from other species and study the biological function of this protein.

This website was created by Melissa Bell, Lindsay Schwarting, and Niall Mangan. Updates by Niall Mangan. All information and images on this site are ©Clarkson University Laboratory of Molecular Neuroscience.