The Nogo receptor is a leucine-rich repeat (LRR) containing protein with a glycosylphosphatidylinositol (GPI) anchored C-terminus. The receptor was identified on the basis of its ability to bind with high affinity to Nogo-A a member of the reticulon family expressed in the cell membrane of oligodendrocytes.1
Nogo-A attracted attention when it was demonstrated that it is a myelin protein capable of inhibiting axonal growth following nerve injury.2,3 Other myelin proteins also identified as axonal growth inhibitors are the myelin-associated glycoprotein (MAG) a sialic-dependent immunoglobulin-like family member lectin (SIGLEC) and the oligodendrocyte myelin glycoprotein (OmgP) which is a GPI-anchored membrane protein. Remarkably, despite their structural diversity, all three axonal growth inhibitors bind to the Nogo receptor with high affinity.4,5
Since the Nogo receptor is a GPI-anchored protein it was expected that it would require another protein component to transduce the Nogo-A binding information into the responding neurons interior. Indeed, it was shown that the neurotrophin receptor p75 (p75NTR) interacts with Nogo receptor and a third protein termed LINGO-1 to mediate axonal growth inhibition signaling.6,7
We are pleased to offer a new antibody directed against a highly conserved epitope situated in the linker region between the LRRs and the GPI anchor. The antibody will work with human, mouse and rat samples and has been tested in western blot, immunocytochemistry and immunohistochemistry techniques.
