No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human FBXL5 Antibodies:
anti-Mouse (Murine) FBXL5 Antibodies:
anti-Rat (Rattus) FBXL5 Antibodies:
Go to our pre-filtered search.
MiR-1306-3p directly targets FBXL5 and modulates FBXL5-meadiated snail protein stability in hepatocellular carcinoma.
this study demonstrated that FBXL5 functioned as an oncogene in the progression of colon cancer through regulating PTEN/PI3K/AKT signaling
Transcriptomic analysis shows downregulation of FBXL5 expression in HSCs of patients with myelodysplastic syndrome.
regulatory circuit involving FBXL5 and CIA acts through both IRPs to control iron metabolism and promote optimal cell growth
analysis of the redox sensing mechanism by which FBXL5 can serve as an iron metabolism regulator within mammalian cells
FBXL5 regulates cortactin through induction of its ubiquitylation, and FBXL5 similarly regulates Snail1.
FBXL5-mediated degradation of CITED2 leads to the activation of HIF-1alpha.
results thus suggest that HERC2 regulates the basal turnover of FBXL5, and that this ubiquitin-dependent degradation pathway contributes to the control of mammalian iron metabolism
F-box and leucine-rich repeat protein 5 (FBXL5) is required for maintenance of cellular and systemic iron homeostasis
Data indicate that F-box and leucine-rich repeat protein 5 (FBXL5)-Hr (hemerythrin-like domain) undergoes substantive structural changes when iron becomes limiting, accounting for its switch-like behavior.
Detailed molecular and structural characterization of the ligand-responsive hemerythrin domain provides insights into the mechanisms by which FBXL5 serves as a unique mammalian metabolic sensor.
iron homeostasis is regulated by a proteolytic pathway that couples IRP2 degradation to intracellular iron levels through the stability and activity of FBXL5
observations suggest a mechanistic link between iron sensing via the FBXL5 hemerythrin domain, IRP2 regulation, and cellular responses to maintain mammalian iron homeostasis
Our findings provide a potential mechanism by which p150(Glued) protein function is regulated by SCFs.
Increased intracellular growth due to compromised expressions of Fpn and FBXL5 by specific siRNAs reveals that Leishmania donovani uses a novel strategy of manipulating IRP2-FBXL5 axis to inhibit host Fpn expression.
Conditional deletion of Fbxl5 in mouse HSCs results in cellular iron overload and a reduced cell number. Bone marrow transplantation reveals that FBXL5-deficient HSCs are unable to reconstitute the hematopoietic system of irradiated recipients as a result of stem cell exhaustion. Transcriptomic analysis shows abnormal activation of oxidative stress responses and the cell cycle in FBXL5-deficient mouse HSCs.
FBXL5 contributes to regulation of neural stem progenitor cell proliferation during mammalian brain development.
we describe the iron and oxygen sensing mechanisms of the FBXL5 Hr-like domain and its role in mediating ROS biology.
The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo.
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 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 Fbls class and, in addition to an F-box, contains several tandem leucine-rich repeats. Alternatively spliced transcript variants have been described for this locus.
F-box and leucine-rich repeat protein 5
, F-box/LRR-repeat protein 5
, F-box/LRR-repeat protein 5-like
, F-box protein FBL4/FBL5
, F-box protein FBL5
, p45SKP2-like protein