Anosmin Antibody

Mutations in Anosmin-1, an extracellular matrix-associated glycosylated protein, have been linked with Kallmann Syndrome (KS), an X-linked genetic disorder characterized by loss of smell caused by abnormal olfactory bulb development and delayed puberty caused by disrupted migration of the gonadotropin-releasing hormone neuron. Anosmin-1 has been shown to directly bind FGFR1 via its N-terminal cysteine-rich domain, whey-acidic protein-like domain, and its first FnIII repeat with the D2 and D3 ectodomains of FGFR1. It is thought that Anosmin-1 can modulate FGFR1 signaling and have opposing effects on the formation and activation of FGF2-FGFR1-heparing complex.