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FBXO2 encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. Additionally we are shipping F-Box Protein 2 Antibodies (61) and F-Box Protein 2 Kits (31) and many more products for this protein.
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Structural analysis of a function-associated loop mutant of the substrate-recognition domain of Fbs1 ubiquitin ligase has been presented.
This study provides new knowledge of the CFTR (show CFTR Proteins) biosynthetic pathway. It suggests that SYVN1 (show SYVN1 Proteins) and FBXO2 represent two distinct multiprotein complexes that may degrade DeltaF508-CFTR (show CFTR Proteins) in airway epithelia and identifies a new role for NEDD8 (show NEDD8 Proteins) in regulating DeltaF508-CFTR (show CFTR Proteins) ubiquitination.
Although the overall structure of FBG3 (show FBXO44 Proteins) is similar to that of Fbs1, the residues that form the Fbs1 carbohydrate-binding pocket failed to be superposed with the corresponding residues of FBG3 (show FBXO44 Proteins).
FBG1 degrades A1AT (show SERPINA1 Proteins)-Z through a Beclin1 (show BECN1 Proteins)-dependent arm of autophagy.
FBG1 is unique among known F-box proteins in that it contains a non-canonical D-Box within F-box domain, required for the growth arrest.
interaction of the HSV-1 UL9 protein with NFB42 results in its polyubiquitination and subsequent degradation by the 26S proteasome (show Psmd4 Proteins)
F-box only protein 2 (FBXO2), a substrate recognition component of the Skp1 (show SKP1 Proteins)-Cul1 (show CUL1 Proteins)-F-box protein (show FBXO30 Proteins) (SCF (show KITLG Proteins)) E3 ubiquitin ligase (show MUL1 Proteins) complex, was upregulated in livers of obese mice. Furthermore, using a protein purification approach combined with high-performance liquid chromatography/tandem mass spectrometry, we carried out a system-wide screening of FBXO2 substrates, in which the insulin receptor (IR (show INSR Proteins)) was identified as a substrate
The results of this study suggested that Fbxo2 controls the abundance and localization of specific NMDAR (show GRIN1 Proteins) subunits in the brain and may influence synapse formation and maintenance.
these results suggest that Fbxo2 regulates APP (show APP Proteins) levels and processing in the brain and may play a role in modulating Alzheimer disease pathogenesis.
our studies support a non-essential role for FBG1 on the degradation of torsinA (show TOR1A Proteins) and uncover a novel link of FBG1 to the autophagy pathway.
When expressed in hippocampal neurons, the Fbx2 dominant-negative mutant augmented NR1 subunit levels and NMDA receptor-mediated currents in an activity-dependent fashion
Fbs1 assists clearance of aberrant glycoproteins in neuronal cells by suppressing aggregates formation, independent of ubiquitin ligase activity, and thus functions as a unique chaperone for those proteins.
Our findings demonstrate that components of protein quality control are essential for inner ear homeostasis and implicate Fbx2 and Skp1 (show SKP1 Proteins) as potential genetic modifiers in age-related hearing loss.
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. This protein is highly similar to the rat NFB42 (neural F Box 42 kDa) protein which is enriched in the nervous system and may play a role in maintaining neurons in a postmitotic state.
F-box only protein 2
, F-box gene 1
, organ of Corti protein 1
, prion protein ligand 4
, neural F box protein NFB42