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FUBP1 encodes a ssDNA binding protein that activates the far upstream element (FUSE) of c-myc and stimulates expression of c-myc in undifferentiated cells. De plus, nous expédions Far Upstream Element (FUSE) Binding Protein 1 Protéines (10) et Far Upstream Element (FUSE) Binding Protein 1 Kits (6) et beaucoup plus de produits pour cette protéine.
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Cow (Bovine) Polyclonal FUBP1 Primary Antibody pour IHC, WB - ABIN2776409
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: Large-scale mapping of human protein-protein interactions by mass spectrometry. ... dans Molecular systems biology 2007
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Cow (Bovine) Polyclonal FUBP1 Primary Antibody pour IHC, WB - ABIN2780231
Duncan, Bazar, Michelotti, Tomonaga, Krutzsch, Avigan, Levens: A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif. dans Genes & development 1994
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Human Polyclonal FUBP1 Primary Antibody pour ELISA, IHC - ABIN4312771
Ko, Kim, Sriram, Dawson, Dawson: Identification of far upstream element-binding protein-1 as an authentic Parkin substrate. dans The Journal of biological chemistry 2006
High FUBP1 expression is associated with low Chemosensitivity to Adriamycin in Gastric Cancer.
Low FUBP1 expression is associated with adenovirus infection.
These results suggest that the interference with the FUBP1/FUSE interaction as a further molecular mechanism that, in addition to the inactivation of TOP1 (Montrer TOP1 Anticorps), may contribute to the therapeutic potential of camptothecin/SN-38.
The findings demonstrate an association between FUBP1 levels and chordoma progression and prognosis, suggesting that FUBP1 can be used as a biomarker and a potential therapeutic target.
we identified cyclin J and far upstream element-binding protein 1 (FUBP1) as novel miR-16 (Montrer GDE1 Anticorps) targets, which mediate miR-16 (Montrer GDE1 Anticorps) antiproliferative effects.
FUBP1 acts as a potential oncogene (Montrer RAB1A Anticorps) in clear cell renal cell carcinoma (Montrer MOK Anticorps) (ccRCC) and may be considered as a novel biomarker or an attractive treatment target of ccRCC.
FBP1 (Montrer FBP1 Anticorps) expression in Bcell lymphoma was also associated with poor survival outcomes. Functionally, small interfering RNAmediated silencing of FBP1 (Montrer FBP1 Anticorps) was able to inhibit the proliferation of Bcell lymphoma cells, resulting in G0/G1 phase cell cycle arrest.
FUBP1 may potentially stimulate c-Myc (Montrer MYC Anticorps) expression in ESCC and its expression may promote esophageal squamous cell carcinoma progression.
With the advent of large-scale genome sequencing technology, molecular genetic alterations in FUBP1 promoter have now been identified in the majority of oligodendrogliomas
direct connection between the cellular PI3K (Montrer PIK3CA Anticorps)/AKT (Montrer AKT1 Anticorps)/mTOR (Montrer FRAP1 Anticorps) signaling pathway, frequently activated in human hepatocarcinogenesis, and the enrichment of oncogenic transcription factors of the FBP (Montrer FBP1 Anticorps) family
FBP helps to hold multiple physiologic processes to close tolerances, at least in part by constraining Myc (Montrer MYC Anticorps) expression.
Our data establish FUBP1 and its recognition of single-stranded genomic DNA as an important element in the transcriptional regulation of hematopoietic stem cells self-renewal.
Apoptosis-mediated cleavage of FBP1 (Montrer FBP2 Anticorps) and its decreased expression in epithelial cells induces cell cycle arrest, which may play an important role in colonic epithelial disruption in colitis.
FUBP1 is an authentic substrate of Parkin (Montrer PARK2 Anticorps) that might play an important role in development of Parkinson disease pathology along with aminoacyl-tRNA synthetase interacting multifunctional protein type 2
This gene encodes a ssDNA binding protein that activates the far upstream element (FUSE) of c-myc and stimulates expression of c-myc in undifferentiated cells. Regulation of FUSE by FUBP occurs through single-strand binding of FUBP to the non-coding strand. This protein has been shown to function as an ATP-dependent DNA helicase.
DNA helicase V
, far upstream element-binding protein 1
, hDH V
, far upstream element (FUSE) binding protein 1
, far upstream element-binding protein
, far upstream element-binding protein 1-like
, FUSE-binding protein 1
, far upstream element (FUSE) binding protein 4
, FUSE binding protein 1