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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. Zusätzlich bieten wir Ihnen Far Upstream Element (FUSE) Binding Protein 1 Proteine (10) und Far Upstream Element (FUSE) Binding Protein 1 Kits (6) und viele weitere Produktgruppen zu diesem Protein an.
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Cow (Bovine) Polyclonal FUBP1 Primary Antibody für 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. ... in Molecular systems biology 2007
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Cow (Bovine) Polyclonal FUBP1 Primary Antibody für 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. in Genes & development 1994
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Human Polyclonal FUBP1 Primary Antibody für ELISA, IHC - ABIN4312771
Ko, Kim, Sriram, Dawson, Dawson: Identification of far upstream element-binding protein-1 as an authentic Parkin substrate. in 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 (zeige TOP1 Antikörper), 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 (zeige GDE1 Antikörper) targets, which mediate miR-16 (zeige GDE1 Antikörper) antiproliferative effects.
FUBP1 acts as a potential oncogene (zeige RAB1A Antikörper) in clear cell renal cell carcinoma (zeige MOK Antikörper) (ccRCC) and may be considered as a novel biomarker or an attractive treatment target of ccRCC.
FBP1 (zeige FBP1 Antikörper) expression in Bcell lymphoma was also associated with poor survival outcomes. Functionally, small interfering RNAmediated silencing of FBP1 (zeige FBP1 Antikörper) was able to inhibit the proliferation of Bcell lymphoma cells, resulting in G0/G1 phase cell cycle arrest.
FUBP1 may potentially stimulate c-Myc (zeige MYC Antikörper) 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 (zeige PIK3CA Antikörper)/AKT (zeige AKT1 Antikörper)/mTOR (zeige FRAP1 Antikörper) signaling pathway, frequently activated in human hepatocarcinogenesis, and the enrichment of oncogenic transcription factors of the FBP (zeige FBP1 Antikörper) family
FBP helps to hold multiple physiologic processes to close tolerances, at least in part by constraining Myc (zeige MYC Antikörper) 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 (zeige FBP2 Antikörper) 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 (zeige PARK2 Antikörper) 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