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anti-Human KPNA2 Antikörper:
anti-Rat (Rattus) KPNA2 Antikörper:
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Human Polyclonal KPNA2 Primary Antibody für 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 für 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
Human Polyclonal KPNA2 Primary Antibody für 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
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 (zeige POU5F1 Antikörper) 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 (zeige POU5F1 Antikörper) 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 (zeige MLXIP Antikörper)-26b plays an anti-metastatic role and is downregulated in gastric cancer tissues via the KPNA2/c-jun (zeige JUN Antikörper) pathway
our results show for the first time that KPNA2 is transcriptionally and post-translationally regulated by the mTOR (zeige FRAP1 Antikörper) pathway and provide new insights into targeted therapy for non-small cell lung cancer
KPNA2 was associated with tumorigenesis and cancer progression in CRC (zeige CALR Antikörper) 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.
the crystal structure of the nuclear import adaptor importin-alpha1 bound to the nuclear localization signal (NLS (zeige ALDH1A2 Antikörper)) of EBNA-LP that shows EBNA-LP residues 44-RRVRRR-49 binding to the major NLS (zeige ALDH1A2 Antikörper)-binding site at the P0-P5 positions.
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 (zeige HIF1A Antikörper)-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 (zeige TP53 Antikörper) glioblastoma cells and provided evidence for the signaling pathway (MIR517C-KPNA2-cytoplasmic TP53 (zeige TP53 Antikörper)) 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 (zeige RPAIN Antikörper) importin alpha2 can modulate paraspeckle protein 1 (zeige PSPC1 Antikörper) delivery to nuclear paraspeckles.
constitutive expression of Kpna2 during the differentiation culture of ESCs (zeige NR2E3 Antikörper) significantly impairs clock development, and KPNA2 facilitates cytoplasmic localization of PER1 (zeige PER1 Antikörper)/
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 (zeige NUP153 Antikörper)
results collectively reveal that nuclear-localized importin alpha2 influences gene expression and contributes directly to cell fate outcomes including non-apoptotic cell death.
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