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FBXL5 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 FBXL5 Kits (21) and FBXL5 Proteins (4) and many more products for this protein.
Showing 10 out of 59 products:
Human Polyclonal FBXL5 Primary Antibody for FACS, IHC (p) - ABIN952279
Salahudeen, Thompson, Ruiz, Ma, Kinch, Li, Grishin, Bruick: An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis. in Science (New York, N.Y.) 2009
Show all 6 references for ABIN952279
Human Polyclonal FBXL5 Primary Antibody for FACS, IHC (p) - ABIN653358
Vashisht, Zumbrennen, Huang, Powers, Durazo, Sun, Bhaskaran, Persson, Uhlen, Sangfelt, Spruck, Leibold, Wohlschlegel: Control of iron homeostasis by an iron-regulated ubiquitin ligase. in Science (New York, N.Y.) 2009
Show all 4 references for ABIN653358
Cow (Bovine) Polyclonal FBXL5 Primary Antibody for IHC, WB - ABIN2774689
Ilyin, Rialland, Pigeon, Guguen-Guillouzo: cDNA cloning and expression analysis of new members of the mammalian F-box protein family. in Genomics 2000
FBXL5 regulates cortactin (show CTTN Antibodies) through induction of its ubiquitylation, and FBXL5 similarly regulates Snail1 (show SNAI1 Antibodies).
FBXL5-mediated degradation of CITED2 (show CITED2 Antibodies) leads to the activation of HIF-1alpha (show HIF1A Antibodies).
Data suggest a mechanism for the negative regulation of cortactin (show CTTN Antibodies) by FBXL5 protein in gastric cancer cells migration.
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 (show IREB2 Antibodies) 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 (show IREB2 Antibodies) regulation, and cellular responses to maintain mammalian iron homeostasis
Our findings provide a potential mechanism by which p150(Glued (show DCTN1 Antibodies)) protein function is regulated by SCFs.
we describe the iron and oxygen sensing mechanisms of the FBXL5 Hr-like domain and its role in mediating ROS (show ROS1 Antibodies) biology.
The FBXL5-IRP2 (show IREB2 Antibodies) 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