Reelin is a 400kD, extracellular matrix glycoprotein secreted by several neurons.
It is a serine protease that degrades fibronectin and laminin.
Reelin also binds lipoprotein receptor superfamily members APOER2 and VLDLR which transduce signals important for neuronal positioning during brain development and synaptic plasticity in the adult brain.
In vivo, Reelin undergoes proteolytic processing at two sites, generating three Reelin fragments.
The N-terminal domain binds integrin alpha3/beta1, leading to a disruption of neuronal glial cell interactions and inhibition of neuronal migration.
Mouse Reelin shares 94% and 96% amino acid identity with human and rat Reelin, respectively in the region immunized.
Applications:Suitable for use in Direct ELISA, Immunohistochemistry and Western Blot.