Human FGFR-2(IIIb)/Fc Chimera, soluble
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| Cat-Nr. | SFC-041S |
| Size | 10 µg |
| Price | 85 € |
| Source | Insect cells |
| Label | Fc-Tag |
| Formulation | lyophilized |
| Purity Confirmation | > 90% by SDS-PAGE |
| Length [aa] | 603 |
| Molecular Weight | 67.2kDa |
| Biological Activity | (1) The activity of sFGFR-2(IIIb)/Fc was determined by its ability to inhibit the FGF10-induced proliferation of 4MBr-5 cells. (2) Measured by its binding ability in a functional ELISA. Recombinant human soluble FGFR-2(IIIb)/Fc Chimera bind to immobilized recombinant human FGF-10 (Catalog #100-022). |
| Species Reactivity | Human |
| Buffer | PBS |
| Reconstitution | The lyophilized sFGFR-2(IIIb)/Fc is soluble in water and most aqueous buffers and should be reconstituted 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-2(IIIb)/Fc should be stored in working aliquots at -20°C. |
| Synonyms | FGFR2; BEK; JWS; CEK3; CFD1; ECT1; KGFR; TK14; TK25; BFR-1; CD332; K-SAM |
| Description | Recombinant human soluble FGFR-2 (IIIb) was fused via a Xa cleavage site with the Fc part of human IgG1. Human recombinant soluble FGFR-2 (IIIb) is a disulfide-linked homodimeric protein. In the reduced form the glycosylated subunits of sFGFR-2 (IIIb)/human Fc chimera display a molecular mass of about 90 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 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 | RPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGINSSNAEVLALFNVTEADAGEYICKVSNYIGQANQSAWLTVLPKQQAPGREKEITASPDYLEDPRRASIEGRGDPEEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK |
| Uniprot ID | P21802-3 |
| Protein RefSeq | NP_075259.4 |
| mRNA RefSeq | NM_000141 |
Figures
SDS-PAGE analysis of recombinant human soluble FGFR-2(IIIb)/Fc produced in insect cells. Sample was loaded in 10% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.
Functional ELISA with recombinant human sFGFR-2(IIIb)/Fc Chimera. Recombinant human FGF-10 (Catalog #100-022) was coated with 2µg/ml and sFGFR2(IIIb)/Fc and sFGFR2(IIIc)/Fc were added [1µg/ml each]. FGF-10 binds only to FGFR2(IIIb) and not to FGFR2(IIIc).
Inhibition of FGF10-induced proliferation of 4MBr-5 cells by recombinant human soluble FGFR-2(IIIb)/Fc. sFGFR-2(IIIc)/Fc which do not bind FGF10 showed no effect.
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