The nuclear pore complex (NPC) is a 125 MDa nuclear envelope complex that mediates nucleocytoplasmic shuttling of RNA and protein. NPC is comprised of more than 30 different proteins, including Ran/TC4, importins, and exportins . Exportin-1(hCRM1/XPO1) is the widely expressed human homologue of the yeast CRM1 protein, which functions in the maintenance of chromatin structure and nuclear export. Exportin-1 has an N-terminal CRIME domain that is homologous to yeast CRM1 and importin-β. Intracellular localization of Exportin-1 shows association with the NPC and overexpression of Exportin-1 in Xenopus oocytes stimulates Rev and U snRNA export from the nucleus. Exportin-1 also binds other nuclear transport related proteins, such as RanGTP, snurportin-1, and the nucleoporins CAN/Nup214 and Nup50. Overexpression of CAN leads to sequestration of Exportin-1 in the nucleoplasm, which inhibits cell growth and induces apoptosis. In addition, Exportin-1 may export specific proteins, such as Rev and PKI, via binding to a leucine-rich nuclear export signal (NES). Thus, Exportin-1 is an important protein and RNA nuclear export receptor, which may be required for normal cell growth and survival.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.