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Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Gene References into Functions
Knockdown of exportins 4, 5, and 7 altered thyroid hormone receptor shuttling dynamics, and when exportins 5 and 7 were overexpressed, TR distribution shifted toward the cytosol. PMID: 25911113
Knockdown of XPO7 reduced the amount of nuclear p65 following TNF stimulation. XPO7 binding to p65 is NLS independent PMID: 23906023
These biochemical and functional data reveal RANBP16 and RANBP17 as novel regulators of E2A protein action, and demonstrate specific interaction of E12 with RANBP17. PMID: 20503194
Exportin 7-dependent nuclear export signals differ fundamentally from the leucine-rich, CRM1-dependent ones PMID: 15282546
STRADalpha facilitates nuclear export of LKB1 by serving as an adaptor between LKB1 and exportins CRM1 and exportin7. PMID: 18256292
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Subcellular Location
Cytoplasm. Nucleus.
Protein Families
Exportin family
Tissue Specificity
Strong expression in testis, thyroid and bone marrow, low expression in lung, liver and small intestine, no expression in thymus, and remaining tissues studied have moderate expression. Expressed in red blood cells; overexpressed in red blood cells (cytop