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anti-Human KPNA2 Antibodies:
anti-Rat (Rattus) KPNA2 Antibodies:
anti-Mouse (Murine) KPNA2 Antibodies:
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Human Polyclonal KPNA2 Primary Antibody for ICC, IF - ABIN256679
Sato, Maquat: Remodeling of the pioneer translation initiation complex involves translation and the karyopherin importin beta. in Genes & development 2009
Show all 6 Pubmed References
Human Polyclonal KPNA2 Primary Antibody for ICC, IF - ABIN250131
Cuomo, Kirch, Gyuris, Brent, Oettinger: Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein. in Proceedings of the National Academy of Sciences of the United States of America 1994
Mouse (Murine) Polyclonal KPNA2 Primary Antibody for IHC, WB - ABIN3022267
Ye, Chen, Li, Zhao, He, Zohaib, Song, Deng, Zhang, Chen, Cao: Japanese Encephalitis Virus NS5 Inhibits Type I Interferon (IFN) Production by Blocking the Nuclear Translocation of IFN Regulatory Factor 3 and NF-κB. in Journal of virology 2017
Human Polyclonal KPNA2 Primary Antibody for ICC, IF - ABIN4325749
Sun, van Koningsbruggen, Long, Straasheijm, Klooster, Jones, Bellini, Levesque, Brieher, van der Maarel, Jones: Facioscapulohumeral muscular dystrophy region gene 1 is a dynamic RNA-associated and actin-bundling protein. in Journal of molecular biology 2011
KPNA2 overexpression is associated with extranodal extension and poor disease-specific survival in patients with oral cavity squamous cell carcinoma. Patients have elevated salivary KPNA2 and KPNA2 knockdown reduced cell migration and invasion.
analysis of recognition of the 53BP1 nuclear localization signal by importin-alpha
these data revealed the essential roles of the miR-139/KPNA2 axis in hepatocellular carcinoma.
KPNA2 might affect hepatocellular carcinoma cell proliferation and migration by mediating cell cycle and DNA replication pathway.
high KPNA2 protein expression is associated with Clear-Cell and Papillary Renal-Cell Carcinoma.
USP1-mediated deubiquitination and stabilization of KPNA2 are revealed as the downstream events crucial for USP1-pro-metastatic function.
Findings suggested that KPNA2, a potential tumor oncogene, performs its function in part via regulating cellular metabolism through c-myc signaling axis. It would provide a possible explanation for Warburg effect and thus offer a new perspective to the roles of KPNA2 in gliomagenesis.
KPNA2 mediated nuclear localization of E2F1 and E2F7, where they in turn controlled KPNA2 expression. Taken together, our data provided mechanistic insights into divergently transcriptional regulation of KPNA2, thus pointing to KPNA2 as a potential target for cancer therapy.
We have therefore modeled the structure of the complex of the whole Oct4 POU domain and importin alpha2 using protein-protein docking and molecular dynamics. The model explains how the Ebola virus VP24 protein has a negative effect on the nuclear import of STAT1 by importin alpha but not on Oct4, and how Nup 50 facilitates cargo release from importin alpha
Development of a pipeline for automated, high-throughput analysis of PSPC1 paraspeckle protein isoforms reveals specific roles for KPNA2, KPNA4 and KPNA6 proteins.
the present study demonstrated that the function of KPNA2 in the process of autophagy may be p53dependent, and by regulating the translocation of p53, KPNA2 can support autophagy to promote the chemoresistance and metastasis of oral squamous cell carcinoma (OSCC) cells.
KPNA2 expression may be a useful prognostic and predictive marker of gemcitabine sensitivity and survival.
KPNA2 was an essential factor promoting hepatocellular carcinoma and unraveled potential molecular pathways and networks underlying KPNA2-induced hepatocellular carcinogenesis.
we confirmed that up-regulated KPNA2 and OCT4 expression is a common feature of bladder cancer that is correlated with increased aggressive tumor behavior. Also, we propose that KPNA2 regulates the process of OCT4 nuclear transportation in bladder cancer.
KPNA2 overexpression was associated with poor OS in East-Asian patients and European patients, as well as patients with gastric and colorectal cancer.[meta-analysis]
miR-26b plays an anti-metastatic role and is downregulated in gastric cancer tissues via the KPNA2/c-jun pathway
our results show for the first time that KPNA2 is transcriptionally and post-translationally regulated by the mTOR pathway and provide new insights into targeted therapy for non-small cell lung cancer
KPNA2 was associated with tumorigenesis and cancer progression in CRC cells; high KPNA2 expression was associated with increased cell proliferation, migration, invasion, and semisolid agar colony formation.
that the interactions observed between TNRC6A and importin-alpha are conserved between mouse and human complexes. Our results highlight the ability of monopartite cNLS sequences to maximise contacts at the importin-alpha major binding site, as well as regions outside the main binding cavities.
The authors identified Importin-alpha1 to bind to Coxiella burnetii AnkG and concluded that binding of AnkG to p32 and Importin-alpha1 is essential for its migration into the nucleus.
Results demonstrated that radiation-induced dying colorectal cancer cells released considerable amounts of KPNA2 that induce the maturation and activation of DCs for synergistic antitumor effect of radiation.
mTORC1 positively regulated the importer protein KPNA2, which participated in glycolysis regulation downstream of mTORC1 in a HIF1alpha-independent manner, indicating that mTORC1 regulates glycolysis through multiple ways.
provided support for a link between autophagy and epithelial-to-mesenchymal (-like) transition status in WT TP53 glioblastoma cells and provided evidence for the signaling pathway (MIR517C-KPNA2-cytoplasmic TP53) involved in attenuating autophagy
Structure of importin-alpha bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein has been reported.
Specific interaction with the nuclear transporter importin alpha2 can modulate paraspeckle protein 1 delivery to nuclear paraspeckles.
constitutive expression of Kpna2 during the differentiation culture of ESCs significantly impairs clock development, and KPNA2 facilitates cytoplasmic localization of PER1/
a significant correlation of KPNA2 expression and tumour aggressiveness in a large variety of other solid tumour entities
study reports a cell-fate determination mechanism in which importin alpha2 negatively regulates the nuclear import of certain transcription factors to maintain embryonic stem cell properties
importin alpha binds to Nup153
results collectively reveal that nuclear-localized importin alpha2 influences gene expression and contributes directly to cell fate outcomes including non-apoptotic cell death.
Chrp, Arip3, and Hop2 are binding partners of IMPalpha2 in the developmental context of germ line development.
Overexpression of a dominant-negative IMPalpha2 isoform, when assessed against adjacent untransfected or IMPalpha2 transfected cells, led to both a significant reduction in endogenous Oct3/4 protein levels and inhibition of Oct3/4 nuclear localization.
knockdown of KPNA2 decreased myotube growth.
The results suggest that Klf2 and Klf4 function redundantly to drive high level of Kpna2 expression in ES cells.
Data show that MRTF-A contains an unusually long bipartite nuclear localisation signal embedded within the RPEL domain, that uses the importin (Imp)alpha/beta-dependent import pathway, and that import is inhibited by G-actin.
Study identified the sequences KKKRR, KKKRK, and KKRKK as the optimal sequences for binding to this site for mouse importin-alpha2, human importin-alpha1, and human importin-alpha5, respectively.
Karyopherin alpha2: a control step of glucose-sensitive gene expression in hepatic cells
Results suggest that the importin alpha/beta system is involved in nuclear entry of mammalian clock components Cry2 and Per2, which is indispensable to transcriptional oscillation of clock genes
Authors demonstrated that swine importin alpha1 interacts with the M1 protein and transports it to the nucleus.
analysis of binding of the mitotic regulator TPX2 (target protein for Xenopus kinesin-like protein 2) to importin-alpha
The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J recombination
RAG cohort 1
, RAG cohort protein 1
, importin alpha 1
, importin alpha 2
, importin subunit alpha-1
, importin subunit alpha-2
, karyopherin subunit alpha-2
, Importin subunit alpha-2
, karyopherin (importin) alpha 2
, nuclear import protein
, importin alpha P1
, pore targeting complex 58 kDa subunit
, karyopherin alpha 2 (RAG cohort 1, importin alpha 1)
, karyopherin alpha-2 subunit like L homeolog