Recombinant human FGFR4 (mutated V550E) protein (Active)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant human FGFR4 (mutated V550E) protein (Active) is a Human Fragment protein, in the 460 to 802 aa range, expressed in Baculovirus infected Sf9 cells, with >75%, suitable for SDS-PAGE, FuncS.
View Alternative Names
CD334, JTK2, TKF, FGFR4, Fibroblast growth factor receptor 4, FGFR-4
- FuncS
Supplier Data
Functional Studies - Recombinant human FGFR4 (mutated V550E) protein (Active) (AB268576)
The specific activity of ab268576 was 85 nmol/min/mg in a kinase assay using Poly (4 : 1 Glu, Tyr) synthetic peptide as substrate.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human FGFR4 (mutated V550E) protein (Active) (AB268576)
SDS-PAGE analysis of ab268576.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
FGFR4 influences various developmental and metabolic processes. It is important in limb and skeletal development epithelial cell morphogenesis and muscle fiber regeneration. FGFR4 often partners with heparan sulfate proteoglycans to form a signaling complex which defines the specificity and regulation of fibroblast growth factor signaling. The receptor's interaction with other proteins like FRFR4 and 5b5 further modulates its biological activity.
Pathways
FGFR4 participates in the MAPK and PI3K-Akt signaling pathways both important for regulating cell survival and growth. These pathways allow FGFR4 to connect with several other proteins such as FGFR1 and BLU-554. FGFR4's activation within these pathways helps determine cellular responses to hormonal and mitogenic signals further influencing tissue homeostasis and repair mechanisms.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling.
Sequence similarities
Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.
Post-translational modifications
N-glycosylated. Full maturation of the glycan chains in the Golgi is essential for high affinity interaction with FGF19.. Ubiquitinated. Subject to proteasomal degradation when not fully glycosylated.. Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer.
Subcellular localisation
Endosome
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com