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The Importin beta-dependent nuclear import of TopBP1 (show TOPBP1 Proteins) was required for the mitomycin C -induced Chk1 (show CHEK1 Proteins) phosphorylation.
Data show that importin-beta binds to Apc (show APC Proteins) and negatively regulates the MT-assembly and spindle-promoting activity of Apc (show APC Proteins) in a Ran-regulatable manner.
The initial step of chromatin seeding is negatively regulated by importin beta.
These results showed that BLM enters the nucleus via the importin beta1, RanGDP and NTF2 dependent pathway, demonstrating for the first time the nuclear trafficking mechanism of a DNA helicase.
Karyoppherins constitute integral constituents of the nuclear pore complex whose barrier, transport, and cargo release functionalities establish a continuum under a mechanism of Kap (show CDKN3 Proteins)-centric control.
Therefore, we show for the first time that the nuclear localization of Cat L and its substrate Cux1can be positively regulated by Snail NLS and importin beta1, suggesting that Snail, Cat L and Cux1 all utilize importin beta1 for nuclear import.
KPNB1 might enhance human glioma proliferation via Wnt (show WNT2 Proteins)/beta-Catenin (show CTNNB1 Proteins) Pathway.
Importins, Impbeta, Kapbeta2, Imp4 (show SPPL2B Proteins), Imp5 (show IPO5 Proteins), Imp7 (show IPO7 Proteins), Imp9 (show IPO9 Proteins), and Impalpha, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kapbeta2 and Imp5 (show IPO5 Proteins) with KD values of 77 and 57 nm, respectively, and binds the other five Importins more weakly.
Patients with tumors highly expressing Kpnbeta1 have poorer overall survivals. Kpnbeta1 interacts with p65 (show GORASP1 Proteins) and enhances cell adhesion-mediated drug resistance.
Collectively, these data show that KPNB1 is required for timely nuclear import of PER/CRY (show CRY2 Proteins) in the negative feedback regulation of the circadian clock.
Humanin Peptide Binds to Insulin-Like Growth Factor-Binding Protein 3 (IGFBP3 (show IGFBP3 Proteins)) and Regulates Its Interaction with Importin-beta.
RBBP4 functions as a novel regulatory factor to increase the efficiency of importin alpha/beta-mediated nuclear import
High expression of KPNB1 protein is associated with hepatocellular carcinoma.
KPNb1 acts as a positive regulator in the NF-kappaB (show NFKB1 Proteins) pathway to enhance palmitate-induced inflammation response.
KPNB1 may play a key role in the inflammation process of rheumatoid arthritis via STAT3 (show STAT3 Proteins) signal transduction pathway.
The study revealed a regulatory role of the p97 (show EIF4G2 Proteins)-Npl4-Ufd1 (show UFD1L Proteins) complex in regulating a partial degradation of the NF-kappaB (show NFKB1 Proteins) subunit p100 (show PATL2 Proteins).
Identification of a karyopherin beta1/beta2 proline-tyrosine nuclear localization signal in huntingtin (show HTT Proteins) protein.
translation of Importin beta1 mRNA enables separation of cytoplasmic and nuclear transport functions of importins and is required for efficient retrograde signaling in injured axons.
A critical function of RanBP2 is to capture recycling RanGTP-importin-beta complexes at cytoplasmic fibrils to allow for adequate classical nuclear localization signal-mediated cargo import.
Ap4A hydrolase (show NUDT2 Proteins) was found to translocate into the nuclei of mast cells following immunological activation; found its immunologically dependent association with importin beta
Data show that MRTF-A contains an unusually long bipartite nuclear localisation signal embedded within the RPEL domain, that uses the importin (Imp (show BRAP Proteins))alpha/beta-dependent import pathway, and that import is inhibited by G-actin (show ACTB Proteins).
results show the crystal structure of importin-beta complexed with the active form of SREBP-2 (show SREBF2 Proteins)
Results suggest that the importin alpha/beta system is involved in nuclear entry of mammalian clock components Cry2 (show CRY2 Proteins) and Per2 (show PER2 Proteins), which is indispensable to transcriptional oscillation of clock genes
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. Two transcript variants encoding different isoforms have been found for this gene.
Importin beta-1 subunit
, importin beta-1 subunit
, importin beta 1
, importin 1
, importin 90
, importin subunit beta-1
, karyopherin subunit beta-1
, nuclear factor p97
, pore targeting complex 97 kDa subunit
, importin beta
, Importin beta
, karyopherin,beta 1
, nuclear factor P97