Human FGFR-4/Fc Chimera, soluble
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| Cat-Nr. | SFC-021 |
| Size | 10 µg |
| Price | 85 € |
| Source | Insect cells |
| Label | Fc-Tag |
| Formulation | lyophilized |
| Purity Confirmation | > 90% by SDS-PAGE |
| Length [aa] | 578 |
| Molecular Weight | 64.4kDa |
| Biological Activity | Measured by its ability to bind recombinant human FGF-2 in a functional solid phase binding assay. |
| Species Reactivity | Human |
| Buffer | PBS |
| Reconstitution | The lyophilized sFGFR-4/Fc is soluble in water and most aqueous buffers and should be reconstituted in PBS or medium to a concentration not lower than 50µg/ml. |
| Stability and Storage | Lyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted sFGFR-4/Fc should be stored in working aliquots at -20°C. Avoid repeated freeze-thaw cycles! |
| Synonyms | FGFR4; TKF; JTK2; CD334 |
| Description | Recombinant human soluble FGFR-4 was fused with the Fc-part of human IgG1. Human recombinant soluble FGFR-4/Fc is a disulfide-linked heterodimeric protein. In the reduced form the glycosylated subunits of sFGFR-4 alpha/human Fc chimera display a molecular mass of 80-85 kDa. Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorigenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1 to -4, are known. All four genes for FGF-receptors encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the beta isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation. |
| Protein Sequence | LEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDTRSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK |
| Uniprot ID | P22455 |
| Protein RefSeq | NP_002002 |
| mRNA RefSeq | NM_002011 |
Figures
SDS-PAGE analysis of recombinant human soluble FGFR-4/Fc produced in insect cells. Sample was loaded in 10% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.
Functional ELISA: Binding of recombinant human FGF2 to different recombinant human soluble FGF receptors. FGF2 was coated at 2µg/ml. The soluble receptors were added with 1µg/ml. Detection was performed with a conjugated anti-Fc antibody.
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