CRMP2 Recombinant Rabbit Monoclonal Antibody [JE31-53]

Members of the CRMP family were discovered independently in different species by several groups working in parallel. Among the five members of the family, CRMP-2 was first identified in 1995. Group of researchers led by Goshima found out that CRMP-2 played a role in the transduction of the extracellular Semaphorin 3A (Sema3A), an inhibitory protein for axonal guidance in chick dorsal root ganglion (DRG). The protein was first named as CRMP-62 having a relative molecular mass of 62 kDa and later referred as CRMP-2. Concurrently, a 64 kDa protein named as TOAD-64 for Turned On After Division, was shown to increase significantly during the development of the cortex of the brain. The cDNA sequence of TOAD-64 corresponded to that of rat CRMP-2. In 1996, mouse CRMP-4, often referred to as Ulip for Unc-33 like phosphoprotein, was discovered by Byk and colleagues, using a rabbit polyclonal antiserum which recognized a 64 kDa mouse brain specific phosphoprotein. In the same year, several other studies cloned CRMPs-1-4 in rat and dihydropyrimidinase (DHPase) homologous sequence of CRMPs-1, -2, and -4 in human fetal brain. Finally, in 2000, CRMP-5 was discovered using two-hybrid screenings of brain libraries or purification from a proteic complex. In following researches, CRMPs were studied as target antigens for autoantibodies in various autoimmune neurodegenerative disorders.