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抗Mouse (Murine) NUP214 抗体:
抗Human NUP214 抗体:
Human Polyclonal NUP214 Primary Antibody for IP, WB - ABIN151667
Quentmeier, Schneider, Roehrs, Romani, Zaborski, Macleod, Drexler: SET-NUP214 fusion in acute myeloid leukemia- and T-cell acute lymphoblastic leukemia-derived cell lines. in Journal of hematology & oncology 2009
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Human Polyclonal NUP214 Primary Antibody for ELISA, WB - ABIN563519
Stochaj, Ba?ski, Kodiha, Matusiewicz: The N-terminal domain of the mammalian nucleoporin p62 interacts with other nucleoporins of the FXFG family during interphase. in Experimental cell research 2006
Show all 2 Pubmed References
Human Polyclonal NUP214 Primary Antibody for ICC, IF - ABIN151666
Yu, Boyce, Wands, Bond, Bertozzi, Kohler: Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners. in Proceedings of the National Academy of Sciences of the United States of America 2012
A major function of DNup88 is to anchor DNup214 and CRM1 on the nuclear envelope and thereby attenuate NES-mediated nuclear export.
The FG repeats of Nup153 are necessary for its function in transport, whereas the remainder of the protein maintains pore integrity.
RNA-sequencing proved to be a valuable tool for the detection of a fusion of genes DEK and NUP214 in a leukemia that showed cryptic cytogenetic rearrangement of chromosome band 9q34.
SQSTM1-Nup214, although mostly cytoplasmic, also forms nuclear bodies and inhibits nuclear protein but not poly(A)(+) RNA export.
We have identified NUP214, a member of the massive nuclear pore complex, as a novel miR-133b target.
t(6;9)/DEK-NUP214 represents a unique subtype of acute myeloid leukemia with a high risk of relapse.
Both in vitro hexon binding and in vivo nuclear import of the adenovirus genome were strongly reduced in Nup214-depleted cells suggesting that Nup214 is a major binding site of adenovirus during infection.
NUP214-ABL1-mediated cell proliferation in T-cell acute lymphoblastic leukemia is dependent on the LCK kinase and various interacting proteins.
the expression of the fusion gene DEK-NUP214 leads to increased cellular proliferation. We show that this is dependent on upregulation of the signal transduction protein mTOR with subsequent effects on protein synthesis and glucose metabolism.
When compared with SET-NUP214-negative patients, SET-NUP214-positive patients showed a significantly higher rate of corticosteroid resistance (91% vs 44%; P = .003) and chemotherapy resistance (100% vs 44%; P = .0001).
The expression of endogenous Nup214 is significantly down-regulated by the reverse inserted lentiviral promoter
Several phenylalanine-glycine motives in the nucleoporin Nup214 are essential for binding of the nuclear export receptor CRM1.
Nucleoporin p62 (NUP62) and nucleoporin 214 (NUP214) are differentially distributed between nuclear pore complexes.
Data describe the relatively high incidence of SET-NUP214 rearrangement in adult T-ALLs, and demonstrate comprehensive clinical, phenotypic, and genetic characteristics of this entity.
Used MALDI-TOF MS 40-plex assay for testing 40 loci within 21 high-ranking breast cancer CAN-genes. No mutation could be found in 6 cell lines. A single breast cancer tissue sample showed heterozygosity at locus c.5834G>A within the ZFYVE26 gene.
NUP214-ABL1 positive T-cell acute lymphoblastic leukemia patient shows an initial favorable response to imatinib therapy post relapse
Cell lines LOUCY and MEGAL express the recently described SET-NUP214 fusion gene.
Oxidative stress up-regulated the binding of Crm1 to Ran and affected multiple repeat-containing nucleoporins by changing their localization, phosphorylation, O-glycosylation, or interaction with other transport components.
Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFbeta signaling complexes in the cytoplasm and nucleus.
A surface hydrophobic corridor within the MH2 domain of Smad3 is critical for association with CAN/Nup214 and nuclear import, whereas Smad4 interaction with CAN/Nup214, and nuclear import requires structural elements present only in the full-length Smad4
leukemia SET-CAN fusion protein inhibited proliferation of U937 cells, most likely by interfering with hCRM1, but it also partially blocks differentiation
Nup214 has a role in regulating TTP localization
The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. This gene is a member of the FG-repeat-containing nucleoporins. The protein encoded by this gene is localized to the cytoplasmic face of the nuclear pore complex where it is required for proper cell cycle progression and nucleocytoplasmic transport. The 3' portion of this gene forms a fusion gene with the DEK gene on chromosome 6 in a t(6,9) translocation associated with acute myeloid leukemia and myelodysplastic syndrome.
, nucleoporin 214
, nucleoporin 214kDa
, nuclear pore complex protein Nup214-like
, 214 kDa nucleoporin
, nuclear pore complex protein Nup214
, nucleoporin Nup214
, CAN protein, putative oncogene