Human FGFR-2(IIIc)/Fc Chimera, soluble

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Size50 µg
Price235 €
SourceInsect cells
Purity Confirmation> 90% by SDS-PAGE
Length [aa]602
Molecular Weight67.1kDa
Biological ActivityDetermined by its ability to inhibit human FGF basic-dependent proliferation on HUVE cells. The ED50 for this effect is typically at 15 - 30ng/ml.
Species ReactivityHuman
ReconstitutionThe lyophilized sFGFR-2/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 StorageLyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted sFGFR-2/Fc should be stored in working aliquots at -20°C.
SynonymsFGFR2; BEK; JWS; CEK3; CFD1; ECT1; KGFR; TK14; TK25; BFR-1; CD332; K-SAM
DescriptionRecombinant human soluble FGFR-2 alpha (IIIc) was fused via a Xa cleavage site with the Fc part of human IgG1. Human recombinant soluble FGFR-2 alpha (IIIc) is a disulfide-linked heterodimeric protein. In the reduced form the glycosylated subunits of sFGFR-2 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 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.
Uniprot IDP21802
Protein RefSeqNP_000132
mRNA RefSeqNM_000141


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