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Human Monoclonal NUP98 Primary Antibody for IF, WB - ABIN2452065
Iwamoto, Asakawa, Hiraoka, Haraguchi: Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms. in Genes to cells : devoted to molecular & cellular mechanisms 2010
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Human Monoclonal NUP98 Primary Antibody for 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. in Monoclonal antibodies in immunodiagnosis and immunotherapy 2013
Show all 2 Pubmed References
Human Monoclonal NUP98 Primary Antibody for DB, ICC - ABIN2452066
Fukuhara, Ozaki, Shikata, Katahira, Yoneda, Ogino, Tachibana: Specific monoclonal antibody against the nuclear pore complex protein, nup98. in Hybridoma (2005) 2005
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Human Polyclonal NUP98 Primary Antibody for IP, WB - ABIN408604
Franks, Benner, Narvaiza, Marchetto, Young, Malik, Gage, Hetzer: Evolution of a transcriptional regulator from a transmembrane nucleoporin. in Genes & development 2016
The distribution of Moesin (show MSN Antibodies) in the nucleus suggests a function in transcription and the depletion of mRNA export factors Nup98 or its interacting partner, Rae1 (show RAE1 Antibodies), leads to the nuclear accumulation of Moesin (show MSN Antibodies), 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 (show DPEP1 Antibodies)-R2/NSL and Trx (show GSR Antibodies) complexes. Nup98 regulates transcription of Trx (show GSR Antibodies) targets, the Hox (show MSH2 Antibodies) genes.
Nup98, a virus-induced gene, was antiviral against a panel of viruses.
Study analyzed genomic interactions of full-length nucleoporins Nup98, Nup50 (show NUP50 Antibodies), 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 (show NUP88 Antibodies) localizes to silent loci, Sec13 (show SEC13 Antibodies), Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction.
We demonstrated that Nup98-TopIIbeta and Nup98-SETBP1 (show SETBP1 Antibodies) negatively regulate the XPO1 (show XPO1 Antibodies)-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 (show HOXD13 Antibodies) (NHD13) mouse model of leukemia progression was significantly elevated by co-expression of a PKR (show EIF2AK2 Antibodies) transgene.
Nup50 (show NUP50 Antibodies) dynamics are independent of importin alpha, Nup153 (show NUP153 Antibodies), and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility.
Data indicate that loss of cyclin-dependent kinase inhibitor p15 (p15Ink4b (show CDKN2B Antibodies)) collaborates with oncogene (show RAB1A Antibodies) fusion protein Nup98-HoxD13 (show HOXD13 Antibodies) transgene in the development of predominantly myeloid neoplasms.
Homeobox (show PRRX1 Antibodies) partners create more potent NUP98 fusion oncogenes than do non-homeobox (show PRRX1 Antibodies) partners.
findings show that expression of NUP98-HOXD13 (show HOXD13 Antibodies) impairs class switch recombination and reduces the antibody-mediated immune response, in addition to its role in leukemia
Mice expressing both the FLT3 (show FLT3 Antibodies)/ITD and Nup98-HoxD13 (show HOXD13 Antibodies) (NHD13) fusion gene developed acute myeloid leukemia (show BCL11A Antibodies) with 100% penetrance
Data show that NUP98-HOXA10HD, a novel, canonical NUP98-Hox (show MSH2 Antibodies) 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 (show XPO1 Antibodies)-mediated nuclear export in conjunction with RanBP3 (show RANBP3 Antibodies).
A mouse model of CML blast crisis induced by cooperation between BCR/ABL (show ABL1 Antibodies) and NUP98/HOXA9 (show HOXA9 Antibodies)
data show that a novel nup98 was identified and it serves a role in nucleocytoplasmic trafficking similar to human NUP98.
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 (show HOXA9 Antibodies) fusion protein is important for its cell immortalization and leukemogenesis activities. NUP98-HOXA9 (show HOXA9 Antibodies) interacts with mixed lineage leukemia (MLL (show MLL Antibodies)) via this FG repeat domain and that, in MLL (show MLL Antibodies)-null mice, NUP98-HOXA9 (show HOXA9 Antibodies)-induced cell immortalization and leukemogenesis are severely inhibited.
DYNLT1 (show DYNLT1 Antibodies) interacts with nucleoporins and plays a role in the dysregulation of gene expression and induction of hematopoietic cell proliferation by the leukemogenic nucleoporin (show AGFG2 Antibodies) fusion, NUP98-HOXA9 (show HOXA9 Antibodies)
the mutation order in the NUP98-rearranged pediatric AML (show RUNX1 Antibodies) begins with the NUP98 rearrangement leading to epigenetic dysregulations then followed by mutations of critical hematopoietic transcription factors and finally, activation of the FLT3 (show FLT3 Antibodies) signaling pathway.
These results provide novel insight into the mechanisms underlying the aberrant capability of NUP98 oncoproteins to interact with APC (show APC Antibodies)/C(Cdc20 (show CDC20 Antibodies)) 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 (show HOXA9 Antibodies) 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 (show MSH2 Antibodies) cluster regions via prebound Crm1 (show XPO1 Antibodies) induces the formation of higher order chromatin structures that causes aberrant Hox (show MSH2 Antibodies) 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.
These data support a model in which Nup98 interacts with microtubules and antagonizes MCAK (show KIF2C Antibodies) 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