Human Recombinant FGFR-3 / Fc Chimera, soluble

Recombinant human soluble FGFR-3 alpha (IIIc) was fused via a Xa cleavage site with the Fc part of human IgG1. Human recombinant soluble FGFR-3 alpha (IIIc)/Fc is a disulfide-linked heterodimeric protein. In the reduced form the glycosylated subunits of sFGFR-3 alpha/human Fc chimera display a MW = 80-85kDa. 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 3 Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the beta 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 from a solution of PBS

Lyophilized samples are stable for greater than six months at -20C to -80C. Reconstituted sFGFR-3/Fc should be stored in working aliquots at -20C. Avoid repeated freeze/thaw cycles.