Human Recombinant FGFR-2 / Fc Chimera, soluble

Recombinant human soluble FGFR-2a (IIIc) was fused via a Xa cleavage site with the Fc part of human IgG1. Human recombinant soluble FGFR-2a (IIIc) is a disulfide-linked heterodimeric protein. The reduced form of human FGF-R2a (IIIc)/Fc is a monomer with a calculated molecular mass of approximately 66 kDa. As a result of glycosylation, the recombinant protein has a mass of 95-100 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 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 β, 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.

Lyophilized

The lyophilized sFGF-R2a (IIIc)/Fc is soluble in water and most aqueous buffers. The lyophilized sFGF-R2a (IIIc)/Fc should be reconstituted in PBS or medium to a concentration not lower than 50 ig/ml.