rev: January 6, 2002


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Human Cytokine/Growth Factor/Chemokines Sample Spec sheets (subject to change without notice):

Recombinant Human sFGFR-1 (IIIc)/Fc Chimera  (see also sFGFR-2 & sFGFR-3)

Description: Recombinant human soluble FGFR-1á (IIIc) was fused via a Xa cleavage site with the Fc part of human IgG1. Human recombinant soluble FGFR-1á (IIIc)/Fc is a disulfide-linked heterodimeric protein. The reduced form of human FGF -R1á (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 90-95 kDa. Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, 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-1to-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 á isoform, or only IgII and IgIII, referred to as the ß isoform. Only the á 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 IIIá 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.

Source:                          Insect cells

Molecular Weight:        190 kDa

Subunit:                         glycosylated dimer

Purity:                           > 90%, by SDS-PAGE and visualised by silver stain

Endotoxin level:            < 0.1 ng per ug of sFGF-R1á

Stabilizer:                     none

Buffer:                          none

Formulation:                 lyophilized

Biological Activity:    Determined by its ability to inhibit human FGF acidic-dependent proliferation on R1 cells.

                                    The ED50 for this effect is typically at 15.0-30.0 ng/ml.

Reconstitution:           The lyophilised sFGFR-1á (IIIc)/Fc is soluble in water and most aqueous buffers. The

                                   lyophilised sFGF-R1á (IIIc)/Fc should be reconstituted in PBS or medium to a concentration not                                       lower than 50 µg/ml.

Stability:                   Lyophilised samples are stable for greater than six months at –20°C to –70°C. Reconstituted                                             sFGFR-1á (IIIc)/Fc should be stored in working aliquots at -20°C. Avoid repeated freeze-thaw                                        cycles!

Usage:                    sFGFR-1á (IIIc)/Fc is offered for research use. Not for drug use. Not for human use!

Catalogue number:  RDI-SFC-015 Size: 50 µg  $438.00  $375.00/vial 3+  Bulk quotes on Request

Range:                    10-100 ng/ml

Literature: [Eisemann et al., Oncogene 6:1195, 1991; Givol et al., FASEB J 6:3362, 1992]

For In vitro research Use Only. Not for use in or on humans or animals or for diagnostics.  It is the responsibility of the user to comply with all local/state and Federal rules in the use of this product. We are not responsible for any patent infringements that might result with the use of or derivation of this product.

RDI Divison of Fitzgerald Industries Intl

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Concord MA 01742-3049


phone (978) 371-6446 or (800) 370-2222

fax     (978) 371-2266


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