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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 5 Pubmed References
Fly (Calliphora) Monoclonal KPNA2 Primary Antibody for IF, IP - ABIN968901
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
Show all 4 Pubmed References
Dog (Canine) Monoclonal KPNA2 Primary Antibody for IF, IP - ABIN967999
Grozinger, Schreiber: Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. in Proceedings of the National Academy of Sciences of the United States of America 2000
Show all 4 Pubmed References
Dog (Canine) Monoclonal KPNA2 Primary Antibody for IF, IP - ABIN967998
Moroianu, Hijikata, Blobel, Radu: Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins. in Proceedings of the National Academy of Sciences of the United States of America 1995
Show all 4 Pubmed References
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
Nuclear import rates correlated with nuclear size, and varying the concentrations of two transport factors, importin alpha and Ntf2 (show NUTF2 Antibodies), was sufficient to account for nuclear scaling between the two species.
a decreased H7N9 influenza A virus polymerase activity when importin-alpha7 was silenced by siRNA, is reported.
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 (show HIF1A Antibodies)-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 (show TP53 Antibodies) glioblastoma cells and provided evidence for the signaling pathway (MIR517C-KPNA2-cytoplasmic TP53 (show TP53 Antibodies)) 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 (show RPAIN Antibodies) importin alpha2 can modulate paraspeckle protein 1 (show PSPC1 Antibodies) delivery to nuclear paraspeckles.
constitutive expression of Kpna2 during the differentiation culture of ESCs (show NR2E3 Antibodies) significantly impairs clock development, and KPNA2 facilitates cytoplasmic localization of PER1 (show PER1 Antibodies)/
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 (show NUP153 Antibodies)
our results show for the first time that KPNA2 is transcriptionally and post-translationally regulated by the mTOR (show FRAP1 Antibodies) pathway and provide new insights into targeted therapy for non-small cell lung cancer
KPNA2 was associated with tumorigenesis and cancer progression in CRC (show CALR Antibodies) 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 (show ALDH1A2 Antibodies)) of EBNA-LP that shows EBNA-LP residues 44-RRVRRR-49 binding to the major NLS (show ALDH1A2 Antibodies)-binding site at the P0-P5 positions.
High serum karyopherin alpha 2 levels (>485 microg/mL) correlated with International Federation of Gynecology and Obstetrics stage ( p < 0.0001), lymphatic metastasis ( p = 0.045), overall survival ( p = 0.001), and disease-free progression ( p = 0.006). Serum karyopherin alpha 2 represents a potential diagnostic biomarker for epithelial ovarian carcinoma.
p53 (show TP53 Antibodies)/p21Cip1/Waf1 (show CDKN1A Antibodies)/p16INK4a (show CDKN2A Antibodies) may be an important pathway involved in the function of KPNA2 in tongue squamous cell carcinoma (TSCC) CAL (show FBLIM1 Antibodies)-27 cells.
These results suggest that the selected aptamers (76 and 72) warrant further study to explore not only their application in cancer diagnosis but also their use as a specific reagent to potentially block KPNA2-dependent nuclear transport of macromolecules across the nuclear membrane.
anti-importin alpha1 antibody treatment suppressed the importin alpha1-FGF1 complex formation and ERK1/2 activation, resulting in decreased cell growth. This study provides novel evidence that functional importin alpha1 is located at the cell surface, where it accelerates the proliferation of cancer cells.
Authors demonstrated that swine importin alpha1 interacts with the M1 protein and transports it to the nucleus.
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
importin subunit alpha-2
, Importin subunit alpha-2
, karyopherin subunit alpha-2
, RAG cohort protein 1
, importin alpha P1
, importin subunit alpha-1
, pore targeting complex 58 kDa subunit
, karyopherin (importin) alpha 2
, nuclear import protein
, RAG cohort 1
, importin alpha 1
, importin alpha 2
, importin subunit alpha-8
, karyopherin subunit alpha-7
, nuclear transport receptor