Exportin 2. also known as CSE1L or chromosomal segregation 1-like protein, is a member of the importin-β family of nuclear transport receptors. It plays a critical role in nucleocytoplasmic shuttling, particularly in the recycling of importin-α from the nucleus to the cytoplasm after nuclear import processes. Exportin 2 binds to importin-α in a RanGTP-dependent manner, facilitating its re-export to the cytoplasm for subsequent rounds of nuclear transport. Beyond its transport functions, Exportin 2 has been implicated in mitotic spindle assembly, cell cycle regulation, and signal transduction pathways.
Antibodies targeting Exportin 2 are widely used tools in molecular and cell biology research. These antibodies enable the detection and localization of Exportin 2 in various experimental applications, including Western blotting, immunofluorescence, and immunohistochemistry. They are particularly valuable for studying nuclear transport mechanisms, cellular compartmentalization dynamics, and protein-protein interactions involving transport receptors. Commercially available Exportin 2 antibodies are typically developed using immunogens corresponding to specific epitopes within the human CSE1L protein sequence.
Research utilizing Exportin 2 antibodies has revealed its potential involvement in cancer progression, with studies showing altered expression levels in colorectal, breast, and hepatocellular carcinomas. These antibodies also contribute to investigations of cellular stress responses, as Exportin 2 appears to interact with proteins involved in apoptosis and DNA damage repair pathways. Validation of Exportin 2 antibodies generally includes knockout cell line controls to confirm specificity, given the protein's structural complexity and functional diversity.