Recombinant Human FGF R2/Fc Chimera


FGFR2/Fc Chimera


GFGR2, Fibroblast growth factor receptor 2, CD332



Cat. No.:

CRF017B pdf (datasheet)


50 μg


$450.00 BUY


Recombinant human soluble FGFR-2a (IIIc) was fused via an Xa cleavage site with the Fc part of human IgG1. Human recombinant soluble FGFR-2a (IIIc) is a disulfide-linked heterodimeric protein.

Fibroblast Growth Factors 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 tumorgenesis. The biological activities of the FGFs are mediated by a family if 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 IIIα 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.

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Data PDF:



Insect cells

Molecular Weight:

170 kDa (Dimer, Glycosylated)


Lyophilized from a sterile filtered solution in PBS without additives.


>90% by SDS-PAGE analysis.

Biological Activity:

ED50: 15-30 ng/ml (Determined by its ability to inhibit human FGF acidic-dependent proliferation on R1 cells).

Endotoxin Level:

< 1 EU/µg


Stable for up to 1 year at -20°C to -80°C.