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- Table of Contents
1 Citations
Facts about Importin subunit beta-1.
Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re- exported from the nucleus into the cytoplasm where GTP hydrolysis releases Ran from importin.
Human | |
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Gene Name: | KPNB1 |
Uniprot: | Q14974 |
Entrez: | 3837 |
Belongs to: |
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importin beta family |
IMB1; Impnb; Importin 1; importin 90; Importin beta; importin beta-1 subunit; importin subunit beta-1; importin-90; IPO1; IPOB; karyopherin (importin) beta 1; Karyopherin subunit beta-1; KPNB1; MGC2155; MGC2156; MGC2157; NTF97; NTF97Pore targeting complex 97 kDa subunit; Nuclear factor p97; PTAC97
Mass (kDA):
97.17 kDA
Human | |
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Location: | 17q21.32 |
Sequence: | 17; NC_000017.11 (47649919..47685505) |
Cytoplasm. Nucleus envelope.
There are a variety of applications for flow cytometry in science, including the study of cells and particles. Boster offers a wide variety of monoclonal and polyclonal antibodies with high affinity to this marker. For more than 25 years, these antibodies have received widespread citations in the scientific literature. Boster antibodies are ideal for this type of analysis, and many of their products are highly cited in scientific journals and textbooks.
The KPNB1 marker is a highly specific antibody that reacts with the human protein DR5. The antibody was tested in ELISA, WB, IP, and IHC. It is also available in a Liquid form. This antibody was developed by Steven Boster, a Chinese scientist. He earned a nickname "he who converts science in the lavatory" for his work.
In cancer cells, KPNB1 inhibitors and the lysosome inhibitor TRAIL have shown promising results. Together, the two agents inhibit lysosome formation and uncouple pro-survival autophagy. This combination was shown to increase the cell death rate. However, Boster Bio did not publish the results of this study. In glioblastoma multiforme, KPNB1 inhibitors inhibited the growth of the tumors, whereas the combination of TRAIL and KPNB1 inhibition significantly reduced the survival of cancer cells.
In glioblastoma cancer cells, KPNB1 inhibition upregulates the expression of DR5 on cell surfaces. This enables TRAIL-triggered apoptosis. Additionally, inhibition of KPNB1 enhances the production of DR5 at the cell surface. This upregulation also enhances the activity of the death receptor ATF4, which is involved in the response to TRAIL.
The KPNB1 inhibitor and TRAIL combination increased cleaved caspase-8 levels. The combination increased LC3-dependent apoptosis and stabilized procaspase-8. Moreover, inhibiting autophagy prevented cleaved caspase-8 from clearing autophagic vesic acid. This combination improved the synergism of the KPNB1 inhibitor/TRAIL treatment.
Inhibition of KPNB1 reduces ER stress by activating UPR. UPR is the protective mechanism that protects cells from chronic stress by inducing apoptosis. Inhibition of KPNB1 increases the expression of DR5 and DR4 in tumor cells. It also prevents the translation initiation of Mcl-1, which inhibits death receptor signaling.
PMID: 7615630 by Chi N.C., et al. Sequence and characterization of cytoplasmic nuclear protein import factor p97.
PMID: 7627554 by Goerlich D., et al. Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope.
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