Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher toutes les espèces
Afficher tous les synonymes
Sélectionnez vos espèces et l'application
anti-Mouse (Murine) Anticorps:
anti-Rat (Rattus) Anticorps:
Vous arrivez à notre recherche pré-filtrée.
Human Polyclonal NUP98 Primary Antibody pour IP, WB - ABIN408604
Franks, Benner, Narvaiza, Marchetto, Young, Malik, Gage, Hetzer: Evolution of a transcriptional regulator from a transmembrane nucleoporin. dans Genes & development 2016
Show all 3 Pubmed References
Human Monoclonal NUP98 Primary Antibody pour IF, WB - ABIN2452064
Iwamoto, Asakawa, Hiraoka, Haraguchi: Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms. dans Genes to cells : devoted to molecular & cellular mechanisms 2010
Show all 2 Pubmed References
Human Monoclonal NUP98 Primary Antibody pour IF, WB - ABIN2452065
Iwamoto, Asakawa, Ohtsuki, Osakada, Koujin, Hiraoka, Haraguchi: Monoclonal antibodies recognize gly-leu-phe-gly repeat of nucleoporin nup98 of tetrahymena, yeasts, and humans. dans Monoclonal antibodies in immunodiagnosis and immunotherapy 2013
Show all 2 Pubmed References
Human Monoclonal NUP98 Primary Antibody pour DB, ICC - ABIN2452066
Fukuhara, Ozaki, Shikata, Katahira, Yoneda, Ogino, Tachibana: Specific monoclonal antibody against the nuclear pore complex protein, nup98. dans Hybridoma (2005) 2005
Show all 2 Pubmed References
The distribution of Moesin in the nucleus suggests a function in transcription and the depletion of mRNA export factors Nup98 or its interacting partner, Rae1, leads to the nuclear accumulation of Moesin, suggesting that the nuclear function of the protein is linked to mRNA export
Nup98 provides a scaffold for poised genes and mediates Induced enhancer-promoter contacts in genetic transcription.
Nup98 associates and colocalizes with the MBD-R2/NSL and Trx complexes. Nup98 regulates transcription of Trx targets, the Hox genes.
Nup98, a virus-induced gene, was antiviral against a panel of viruses.
Study analyzed genomic interactions of full-length nucleoporins Nup98, Nup50, and Nup62 and found that they predominantly interacted with active genes inside the nucleoplasm, particularly those involved in developmental regulation and the cell cycle.
Nup88 localizes to silent loci, Sec13, Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction.
causes epistatic inviability in hybrids between two fruitfly species, Drosophila melanogaster and D. simulans
We demonstrated that Nup98-TopIIbeta and Nup98-SETBP1 negatively regulate the XPO1-mediated protein export. Our results will contribute to the understanding of the molecular mechanism by which the Nup98-fusion proteins induce tumorigenesis.
The age-associated accumulation of somatic mutations that occurs in the Nup98-HOXD13 (NHD13) mouse model of leukemia progression was significantly elevated by co-expression of a PKR transgene.
Nup50 dynamics are independent of importin alpha, Nup153, and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility.
Data indicate that loss of cyclin-dependent kinase inhibitor p15 (p15Ink4b) collaborates with oncogene fusion protein Nup98-HoxD13 transgene in the development of predominantly myeloid neoplasms.
Homeobox partners create more potent NUP98 fusion oncogenes than do non-homeobox partners.
expression of NHD13 fusion gene resulted in impaired NHEJ-mediated DNA break repair.
findings show that expression of NUP98-HOXD13 impairs class switch recombination and reduces the antibody-mediated immune response, in addition to its role in leukemia
Mice expressing both the FLT3/ITD and Nup98-HoxD13 (NHD13) fusion gene developed acute myeloid leukemia with 100% penetrance
Data show that NUP98-HOXA10HD, a novel, canonical NUP98-Hox fusion, significantly enhances the self-renewal capacity of hematopoietic stem cells.
These results clearly demonstrate that Nup98 functions as a novel shuttling cofactor for Crm1-mediated nuclear export in conjunction with RanBP3.
A mouse model of CML blast crisis induced by cooperation between BCR/ABL and NUP98/HOXA9
results suggest that Rae1 and Nup98 are temporal regulators of APC(Cdh1) that maintain euploidy by preventing unscheduled degradation of securin
NUP98 is dysregulated in myeloid leukemogenesis [review]
The onset of leukemia was accelerated, suggesting a synergistic effect between the NUP98-HOXD13 transgene and the genes neighboring retroviral insertion events.
Nup96 levels regulate differential gene expression in a phase-specific manner, setting the stage for proper cell cycle progression.
The expression of the NUP98-HOXD13 fusion transgene inhibits lymphoid as well as myeloid and erythroid differentiation, results in overexpression of Hoxa cluster genes, and leads to a precursor T cell lymphoblastic leukemia/lymphoma.
data show that a novel nup98 was identified and it serves a role in nucleocytoplasmic trafficking similar to human NUP98.
NUP98-fusion transcripts characterize different biological entities within acute myeloid leukemia: a report from the AIEOP-AML group.
Chimeric NUP98-NSD1 fusion transcripts are associated with acute myeloid leukemia.
NHA9 (NUP98-HOXA9 fusion protein) deregulates the expression of key leukemic genes, including MEIS1-HOXA9-PBX3 complex, through the enhancer binding and the direct interaction of the fusion protein with HDAC and p300 transcriptional regulators
human NUP98-IQCG fusion protein could induce fatal and transplantable acute myelomonocytic leukemia in a mouse model
Importantly, binding of Nup98 to DHX9 stimulates the ATPase activity of DHX9, and a transcriptional reporter assay suggests Nup98 supports DHX9-stimulated transcription.
The second FG repeat domain of the NUP98 moiety of the NUP98-HOXA9 fusion protein is important for its cell immortalization and leukemogenesis activities. NUP98-HOXA9 interacts with mixed lineage leukemia (MLL) via this FG repeat domain and that, in MLL-null mice, NUP98-HOXA9-induced cell immortalization and leukemogenesis are severely inhibited.
DYNLT1 interacts with nucleoporins and plays a role in the dysregulation of gene expression and induction of hematopoietic cell proliferation by the leukemogenic nucleoporin fusion, NUP98-HOXA9
the mutation order in the NUP98-rearranged pediatric AML begins with the NUP98 rearrangement leading to epigenetic dysregulations then followed by mutations of critical hematopoietic transcription factors and finally, activation of the FLT3 signaling pathway.
These results provide novel insight into the mechanisms underlying the aberrant capability of NUP98 oncoproteins to interact with APC/C(Cdc20) and to interfere with its function.
Our results suggest that NA10HD increases the number of gamma-globin-transduced HSCs that engraft, leading to an elevated number of fetal hemoglobin-containing red cells.
NUP98-HOXA9 ability to induce blood cell expansion is evolutionarily conserved.
The study demonstrated the association of NUP98-IQCG with CRM1, and found that NUP98-IQCG expression inhibits the CRM1-mediated nuclear export of p65 and enhances the transcriptional activity of nuclear factor-kappaB. Moreover, IQCG could be entrapped in the nucleus by NUP98-IQCG, and the fusion protein interacts with calmodulin via the IQ motif in a calcium-independent manner.
The results indicate that highly selective targeting of Nup98-fusion proteins to Hox cluster regions via prebound Crm1 induces the formation of higher order chromatin structures that causes aberrant Hox gene regulation.
Despite the difference in localization, all tested Nup98 chimera provoked morphological alterations in the nuclear envelope (NE), in particular affecting the nuclear lamina and the lamina-associated polypeptide 2alpha.
NUP98-HOXA9 expression induces myeloid disease.
Overall, these results demonstrate a novel role for FOXK1 in regulating the expression of antiviral genes via Nup98, from insects to humans.
deregulation of the retinoid/rexinoid signaling pathway has a major role and may represent a potential therapeutic target for NUP98-RARG-mediated transformation
Acute myeloid leukemia can be reproduced in mice by transducing mouse mesenchymal stem cells with the human NUP98-NSD1 fusion and the FLT3-ITD mutated constracts.
These data reveal an emergent Kap-centric barrier mechanism that may underlie mechanistic and kinetic control in the nuclear pore complex.
Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1 * Nup98).
These data support a model in which Nup98 interacts with microtubules and antagonizes MCAK activity, thus promoting bipolar spindle assembly.
Signal-mediated nuclear import and export proceed through the nuclear pore complex (NPC), which is comprised of approximately 50 unique proteins collectively known as nucleoporins. The 98 kDa nucleoporin is generated through a biogenesis pathway that involves synthesis and proteolytic cleavage of a 186 kDa precursor protein. This cleavage results in the 98 kDa nucleoporin as well as a 96 kDa nucleoporin, both of which are localized to the nucleoplasmic side of the NPC. Rat studies show that the 98 kDa nucleoporin functions as one of several docking site nucleoporins of transport substrates. The human gene has been shown to fuse to several genes following chromosome translocations in acute myelogenous leukemia (AML) and T-cell acute lymphocytic leukemia (T-ALL). This gene is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. Alternative splicing of this gene results in several transcript variants\; however, not all variants have been fully described.
, nucleoporin 98
, nucleoporin 98-96
, nucleoporin 98kD
, nucleoporin 98kDa
, nuclear pore complex protein Nup98-Nup96-like
, nuclear pore complex protein Nup98-Nup96
, 98 kDa nucleoporin
, nuclear pore complex protein Nup98
, nucleoporin Nup98
, GLFG-repeat containing nucleoporin