>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.01 EU per 1 μg of the protein by the LAL method.
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 0.4-2 μg/mL in the presence of 10 µg/mL heparin.
E. coli-derived human FGF-8 protein Gln23-Arg204, with an N-terminal Met
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.
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).
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