Human FGFR-1/Fc Chimera, soluble
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| Cat-Nr. | SFC-015 |
| Size | 10 µg |
| Price | 85 € |
| Source | Insect cells |
| Label | Fc-Tag |
| Formulation | lyophilized |
| Purity Confirmation | > 90% by SDS-PAGE |
| Length [aa] | 601 |
| Molecular Weight | 67.0kDa |
| Biological Activity | Determined by its ability to inhibit human FGF basic-dependent proliferation on HUVE cells |
| Species Reactivity | Human |
| Buffer | PBS |
| Reconstitution | The lyophilized sFGFR-1/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-1/Fc should be stored in working aliquots at -20°C. |
| Synonyms | FGFR1; CEK; FLG; OGD; FLT2; KAL2; BFGFR; CD331; FGFBR; FLT-2; HBGFR; N-SAM; FGFR-1; bFGF-R-1 |
| Description | Recombinant human soluble FGFR-1 alpha (IIIc) was fused via a Xa cleavage site with the Fc part of human IgG1. Human recombinant soluble FGFR-1 alpha (IIIc)/Fc is a disulfide-linked heterodimeric protein. In the reduced form the glycosylated subunits of sFGFR-1 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. 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 of the Ig-like domains IgII and IgIII, referred to as the ß 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. |
| Protein Sequence | RPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEDPRRASIEGRGDPEEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK |
| Uniprot ID | P11362 |
| Protein RefSeq | NP_075598 |
| mRNA RefSeq | NM_023110 |
Figures
SDS-PAGE analysis of recombinant human soluble FGFR-1/Fc produced in insect cells. Sample was loaded in 10% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.
Inhibition of the basic FGF-induced proliferation of HUVE cells by recombinant human sFGFR-1-Fc. HUVECs were stimulated with 10 ng/ml bFGF, the soluble receptor was added with a 50-200X excess.
Reference
- Antiangiogenic and anticancer effect of an orally active low molecular weight heparin conjugates and its application to lung cancer chemoprevention. J.Y. Kim et a., J Control Release. 2015 Feb 10;199:122-31.
- Fibroblast growth factor 2-antagonist activity of a long-pentraxin 3-derived anti-angiogenic pentapeptide. D. Leali et al., J Cell Mol Med. 2010 Aug; 14(8): 2109–2121.
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