Anti-Importin subunit alpha-4 KPNA3 Antibody

Karyopherin, a cytosolic and heterodimeric protein complex consisting of alpha and beta subunits, is responsible for targeting proteins with nuclear localization signals to the nuclear pore complex by an energy requiring, Ran-dependent mechanism. The alpha subunit and imported substrate enter the nucleus and accumulate in the nucleoplasm, while the beta subunit accumulates at the NPC. KPNA3, the alpha subunit 3 of karyopherin, is silimar to human KPNA2, suggesting that KPNA3 may be involved in the nuclear transport system. It is ubiquitously expressed and recent studies have shown that human KPNA3 may be associated with schizophrenia.

KPNA3 antibody was raised against a 14 amino acid synthetic peptide near the carboxy end of human KPNA3. The immunogen is located within the last 50 amino acids of KPNA3.

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non- classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9.

KPNA3 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.