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The transport of protein and large RNAs through the nuclear pore complexes (NPC) is an energy-dependent and regulated process. Additionally we are shipping and many more products for this protein.
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These biochemical and functional data reveal RANBP16 (show XPO7 Antibodies) and RANBP17 as novel regulators of E2A (show TCF3 Antibodies) protein action, and demonstrate specific interaction of E12 (show ELSPBP1 Antibodies) with RANBP17.
Interactions between RANBP17 and SPEM1 (show SPEM1 Antibodies), for the first time, point to a potential function of SPEM1 (show SPEM1 Antibodies) in the RANBP17-mediated nucleocytoplasmic transport.
The transport of protein and large RNAs through the nuclear pore complexes (NPC) is an energy-dependent and regulated process. The import of proteins with a nuclear localization signal (NLS) is accomplished by recognition of one or more clusters of basic amino acids by the importin-alpha/beta complex\; see MIM 600685 and MIM 602738. The small GTPase RAN (MIM 601179) plays a key role in NLS-dependent protein import. RAN-binding protein-17 is a member of the importin-beta superfamily of nuclear transport receptors.
ran-binding protein 17
, RAN binding protein 17
, ran-binding protein 17-like