Recombinant Human FGF-8a Protein, CF

(2 citations)   
  • Purity
    >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
  • Endotoxin Level
    <0.01 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is typically 0.4-2 μg/mL in the presence of 10 µg/mL heparin.
  • Source
    E. coli-derived Gln23-Arg204, with an N-terminal Met
  • Accession #
  • N-terminal Sequence
  • Predicted Molecular Mass
    21 kDa
Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, EDTA and DTT.
Reconstitution Reconstitute at 500 μg/mL in sterile PBS.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Data Images
1 μg/lane of Recombinant Human FGF-8a was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at
22 kDa.
Recombinant Human FGF-8a (Catalog # 4745-F8) stimulates cell proliferation of the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is typically 0.4-2 μg/mL in the presence of 10 μg/mL heparin.
Background: FGF-8

FGF-8 is a member of the fibroblast growth factor family that was originally discovered as a growth factor essential for the androgen-dependent growth of mouse mammary carcinoma cells (1-4). Alternate splicing of mouse FGF-8 mRNA generates eight secreted isoforms, designated a-h. Only FGF-8a, b, e and f exist in humans (4). FGF-8 contains a 22 amino acid (aa) signal sequence, an N-terminal domain that varies according to the isoform (20 aa for FGF-8a, which is the shortest), a 125 aa FGF domain and a 37 aa proline-rich C-terminal sequence. The FGF domain of FGF-8 shares the most aa identity with FGF17 (75%) and FGF-18 (67%), and the three form an FGF subfamily (2). Human FGF-8a shares 100% aa identity with mouse, rat and bovine FGF-8a, and 99%, 83%, 83% and 78% aa identity with canine, Xenopus, chicken and zebrafish FGF-8a, respectively. FGF-8 is widely expressed during embryogenesis, and mediates epithelial-mesenchymal transitions. It plays an organizing and inducing role during gastrulation, and regulates patterning of the midbrain/hindbrain, eye, ear, limbs and heart in the embryo (2, 5-8). The isoforms may play different roles in development. For example, FGF-8a expands the midbrain in transgenic mice, while FGF-8b transforms midbrain into cerebellum (5). FGF-8 activates the ‘c’ splice forms of fibroblast growth factor receptors FGF R2, FGF R3, and FGF R4, with differential activity among the FGF-8 isoforms (2, 9). FGF-8b shows the strongest receptor affinity and oncogenic transforming capacity, although FGF-8a and e are also transforming and have been found in human prostate, breast or ovarian tumors (1, 5, 10 - 13). FGF-8 shows limited expression in the normal adult, but low levels are found in the reproductive and genitourinary tract, peripheral leukocytes and bone marrow hematopoietic cells (3, 10, 14).

  • References:
    1. Mattila, M.M. and P.L. Harkonen (2007) Cytokine Growth Factor Rev. 18:257.
    2. Reuss, B. and O. von Bohlen und Halbach (2003) Cell Tissue Res. 313:139.
    3. Payson, R.A. et al. (1996) Oncogene 13:47.
    4. Gemel, J. et al. (1996) Genomics 35:253.
    5. Olsen, S.K. et al. (2006) Genes Dev. 20:185.
    6. Crossley, P.H. et al. (1996) Cell, 84:127.
    7. Heikinheimo, M. et al. (1994) Mech. Dev. 48:129.
    8. Sun, X. et al. (1999) Genes Dev. 13:1834.
    9. Blunt, A.G. et al. (1997) J. Biol. Chem. 272:3733.
    10. Ghosh, A.K. et al. (1996) Cell Growth Differ. 7:1425.
    11. Mattila, M.M. et al. (2001) Oncogene 20:2791.
    12. Valve, E. et al. (2000) Int. J. Cancer 88:718.
    13. Valve, E.M. et al. (2001) Lab. Invest. 81:815.
    14. Nezu, M. et al. (2005) Biochem. Biophys. Res. Commun. 335:843.
  • Long Name:
    Fibroblast Growth Factor 8
  • Entrez Gene IDs:
    2253 (Human); 14179 (Mouse); 29349 (Rat)
  • Alternate Names:
    AIGF; AIGFKAL6; Androgen-induced growth factor; FGF8; FGF-8; fibroblast growth factor 8 (androgen-induced); fibroblast growth factor 8; HBGF-8; Heparin-binding growth factor 8; MGC149376
Related Research Areas

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Sample Type
  1. Altered splicing of FGFR1 is associated with high tumor grade and stage and leads to increased sensitivity to FGF1 in bladder cancer.
    Authors: Tomlinson DC, Knowles MA
    Am. J. Pathol., 2010;177(5):2379-86.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay
  2. Similar expression to FGF (Sef) inhibits fibroblast growth factor-induced tumourigenic behaviour in prostate cancer cells and is downregulated in aggressive clinical disease.
    Authors: Darby S, Murphy T, Thomas H, Robson CN, Leung HY, Mathers ME, Gnanapragasam VJ
    Br. J. Cancer, 2009;101(11):1891-9.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay

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