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The nuclear import of the spliceosomal snRNPs U1, U2, U4 and U5, is dependent on the presence of a complex nuclear localization signal. Additionally we are shipping Snurportin 1 Antibodies (52) and Snurportin 1 Proteins (15) and many more products for this protein.
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analysis of interactions between CRM1 and the nuclear pore protein Tpr and snurportin
SPN (show SPN ELISA Kits) construct lacking the importin beta (show KPNB1 ELISA Kits) binding domain (IBB) localizes primarily to the nucleus rather than to the cytoplasm.
There is an interaction between the N- and C-terminal domains of SPN (show SPN ELISA Kits), suggesting an autoregulatory function similar to that of importin-alpha (show KPNA4 ELISA Kits).
study presents the crystal structure of the SPN1 (show SSPN ELISA Kits).CRM1 (show XPO1 ELISA Kits).RanGTP export complex at 2.5 angstrom resolution (where SPN1 (show SSPN ELISA Kits) is snurportin1 and RanGTP is guanosine 5' triphosphate-bound Ran
the binding of dimethylated RNA-caps (show CAPS ELISA Kits) to snurportin 1
The nuclear import of the spliceosomal snRNPs U1, U2, U4 and U5, is dependent on the presence of a complex nuclear localization signal. The latter is composed of the 5'-2,2,7-terminal trimethylguanosine (m3G) cap structure of the U snRNA and the Sm core domain. The protein encoded by this gene interacts specifically with m3G-cap and functions as an snRNP-specific nuclear import receptor. Alternatively spliced transcript variants encoding the same protein have been identified for this gene.
RNA, U transporter 1
, snurportin 1
, RNA U transporter 1