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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. Additionally we are shipping NUP214 Kits (18) and and many more products for this protein.
Showing 9 out of 12 products:
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 references for ABIN563519
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
Show all 2 references for ABIN151667
Human Polyclonal NUP214 Primary Antibody for ICC, IF - ABIN4286951
Wen, Zhou, Liu, Wang, Zhang, Liang: Effect of the knockdown of Cabin1 on p53 in glomerular podocyte. in Journal of receptor and signal transduction research 2016
A major function of DNup88 is to anchor DNup214 and CRM1 (show XPO1 Antibodies) on the nuclear envelope and thereby attenuate NES (show NES Antibodies)-mediated nuclear export.
The FG repeats of Nup153 (show NUP153 Antibodies) are necessary for its function in transport, whereas the remainder of the protein maintains pore integrity.
We have identified NUP214, a member of the massive nuclear pore complex, as a novel miR (show MLXIP Antibodies)-133b target.
t(6;9)/DEK (show DEK Antibodies)-NUP214 represents a unique subtype of acute myeloid leukemia (show BCL11A Antibodies) 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 (show ABL1 Antibodies)-mediated cell proliferation in T-cell acute lymphoblastic leukemia is dependent on the LCK (show LCK Antibodies) kinase and various interacting proteins.
the expression of the fusion gene DEK (show DEK Antibodies)-NUP214 leads to increased cellular proliferation. We show that this is dependent on upregulation of the signal transduction protein mTOR (show FRAP1 Antibodies) 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 (show XPO1 Antibodies).
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.
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