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Human Monoclonal NUP98 Primary Antibody pour IF, WB - ABIN2452065
Iwamoto, Asakawa, Hiraoka, Haraguchi: Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms. dans Genes to cells : devoted to molecular & cellular mechanisms 2010
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Human Monoclonal NUP98 Primary Antibody pour IF, WB - ABIN2452064
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
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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
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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
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The distribution of Moesin (Montrer MSN Anticorps) in the nucleus suggests a function in transcription and the depletion of mRNA export factors Nup98 or its interacting partner, Rae1 (Montrer RAE1 Anticorps), leads to the nuclear accumulation of Moesin (Montrer MSN Anticorps), 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 (Montrer NUP50 Anticorps), 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 (Montrer NUP88 Anticorps) localizes to silent loci, Sec13 (Montrer SEC13 Anticorps), Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction.
We demonstrated that Nup98-TopIIbeta and Nup98-SETBP1 (Montrer SETBP1 Anticorps) negatively regulate the XPO1 (Montrer XPO1 Anticorps)-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 (Montrer HOXD13 Anticorps) (NHD13) mouse model of leukemia progression was significantly elevated by co-expression of a PKR (Montrer EIF2AK2 Anticorps) transgene.
Nup50 (Montrer NUP50 Anticorps) dynamics are independent of importin alpha, Nup153 (Montrer NUP153 Anticorps), and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility.
Data indicate that loss of cyclin-dependent kinase inhibitor p15 (p15Ink4b (Montrer CDKN2B Anticorps)) collaborates with oncogene (Montrer RAB1A Anticorps) fusion protein Nup98-HoxD13 (Montrer HOXD13 Anticorps) transgene in the development of predominantly myeloid neoplasms.
Homeobox (Montrer PRRX1 Anticorps) partners create more potent NUP98 fusion oncogenes than do non-homeobox (Montrer PRRX1 Anticorps) partners.
findings show that expression of NUP98-HOXD13 (Montrer HOXD13 Anticorps) impairs class switch recombination and reduces the antibody-mediated immune response, in addition to its role in leukemia
Mice expressing both the FLT3 (Montrer FLT3 Anticorps)/ITD and Nup98-HoxD13 (Montrer HOXD13 Anticorps) (NHD13) fusion gene developed acute myeloid leukemia (Montrer BCL11A Anticorps) 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 (Montrer XPO1 Anticorps)-mediated nuclear export in conjunction with RanBP3 (Montrer RANBP3 Anticorps).
A mouse model of CML blast crisis induced by cooperation between BCR/ABL (Montrer ABL1 Anticorps) and NUP98/HOXA9 (Montrer HOXA9 Anticorps)
data show that a novel nup98 was identified and it serves a role in nucleocytoplasmic trafficking similar to human NUP98.
NHA9 (NUP98-HOXA9 (Montrer HOXA9 Anticorps) fusion protein) deregulates the expression of key leukemic genes, including MEIS1 (Montrer MEIS1 Anticorps)-HOXA9 (Montrer HOXA9 Anticorps)-PBX3 complex, through the enhancer binding and the direct interaction of the fusion protein with HDAC (Montrer HDAC3 Anticorps) and p300 (Montrer EP300 Anticorps) 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 (Montrer DHX9 Anticorps) stimulates the ATPase (Montrer DNAH8 Anticorps) activity of DHX9 (Montrer DHX9 Anticorps), and a transcriptional reporter assay suggests Nup98 supports DHX9 (Montrer DHX9 Anticorps)-stimulated transcription.
The second FG repeat domain of the NUP98 moiety of the NUP98-HOXA9 (Montrer HOXA9 Anticorps) fusion protein is important for its cell immortalization and leukemogenesis activities. NUP98-HOXA9 (Montrer HOXA9 Anticorps) interacts with mixed lineage leukemia (MLL (Montrer MLL Anticorps)) via this FG repeat domain and that, in MLL (Montrer MLL Anticorps)-null mice, NUP98-HOXA9 (Montrer HOXA9 Anticorps)-induced cell immortalization and leukemogenesis are severely inhibited.
DYNLT1 (Montrer DYNLT1 Anticorps) interacts with nucleoporins and plays a role in the dysregulation of gene expression and induction of hematopoietic cell proliferation by the leukemogenic nucleoporin (Montrer AGFG2 Anticorps) fusion, NUP98-HOXA9 (Montrer HOXA9 Anticorps)
the mutation order in the NUP98-rearranged pediatric AML (Montrer RUNX1 Anticorps) begins with the NUP98 rearrangement leading to epigenetic dysregulations then followed by mutations of critical hematopoietic transcription factors and finally, activation of the FLT3 (Montrer FLT3 Anticorps) signaling pathway.
These results provide novel insight into the mechanisms underlying the aberrant capability of NUP98 oncoproteins to interact with APC (Montrer APC Anticorps)/C(Cdc20 (Montrer CDC20 Anticorps)) 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 (Montrer HOXA9 Anticorps) 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.
These data support a model in which Nup98 interacts with microtubules and antagonizes MCAK (Montrer KIF2C Anticorps) 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