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importin-alpha5, which is a key regulator of interferon (show IFNA ELISA Kits) signaling following Ebola virus infection, as one putative target of miRNA.
The nuclear importin IPO5 was identified as a novel interacting protein of SMAD1 (show GARS ELISA Kits). Overexpression of IPO5 in various cell lines specifically increases nuclear localization of BMP receptor (show BMPR1A ELISA Kits)-activated SMADs (R-SMADs) confirming a functional relationship between IPO5 and BMP but not TGF-beta (show TGFB1 ELISA Kits) R-SMADs.
Importins, Impbeta, Kapbeta2, Imp4, Imp5, Imp7, Imp9, and Impalpha, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kapbeta2 and Imp5 with KD values of 77 and 57 nm, respectively, and binds the other five Importins more weakly.
Single nucleotide polymorphism in IPO5 gene is associated with Peripheral Arterial Disease.
IQGAP1 (show IQGAP1 ELISA Kits) interacts with human importin-beta5 in HEK (show EPHA3 ELISA Kits) 293T cells.
In case of L7, importin beta2 or importin beta3 are preferentially used by clusters with a high import efficiency.
The N-terminal of influenza A virus PB1 mediates its binding to host RanBP5.
The results of this study suggested that abnormal expression and alternative splicing of the IPO5 gene may be involved in the pathophysiology of schizophrenia.
importin beta3 is essential for the nuclear import of RPL7 (show RPL7 ELISA Kits). The import is mediated via the multifaceted basic amino acid clusters present in the NH(2)-region of RPL7 (show RPL7 ELISA Kits), and is RanGTP-dependent
L1 major capsid protein of human papillomavirus type 11 interacts with Kap (show CDKN3 ELISA Kits) beta3 nuclear import receptors
nuclear import protein (show KPNA2 ELISA Kits) IPO5 facilitates the nuclear translocation of MSI1 (show MSI1 ELISA Kits) to the transcriptionally silenced XY chromatin domain in meiotic pachytene spermatocytes, resulting in the release of MSI1 (show MSI1 ELISA Kits) RNA-binding targets
RanBP5 exhibits age- and gender-specific subcellular localization within fetal gonads. At E12.5, RanBP5 protein is cytoplasmic in gonocytes but predominantly nuclear in oogonia, but by E14.5 RanBP5 appears nuclear in gonocytes and cytoplasmic in oogonia
Nucleocytoplasmic transport, a signal- and energy-dependent process, takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. In the presence of nucleoside triphosphates and the small GTP binding protein Ran, the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex. The protein encoded by this gene is a member of the importin beta family.
, RAN binding protein 5
, Ran_GTP binding protein 5
, importin beta-3 subunit
, importin subunit beta-3
, karyopherin (importin) beta 3
, karyopherin beta-3
, ran-binding protein 5