Recombinant Human FGF-8f Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human FGF-8f Protein Summary

Details of Functionality
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Rizzino, A. et al. (1988) Cancer Res. 48:4266; Thomas, K. et al. (1987) Methods Enzymol. 147:120. The ED50 for this effect is 0.04-0.2 µg/mL in the presence of 10 µg/mL of heparin.
Source
E. coli-derived human FGF-8 protein
Gln23-Arg244, with an N-terminal Met
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
Gene
FGF8
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
25.5 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
29 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, EDTA and DTT with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human FGF-8f Protein

  • 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

Background

FGF-8, a member of the fibroblast growth factor family, is a secreted heparin-binding protein that was originally discovered as a growth factor essential for the androgen-dependent growth of mouse mammary carcinoma cells (1-3). Alternative splicing of mouse FGF-8 mRNA generates eight secreted isoforms, designated a-h, but 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 (84 aa for FGF-8f, the longest form in humans; 20 aa for the shortest, FGF-8a), 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 FGF-17 (75%) and FGF-18 (67%), and these three form an FGF subfamily (2). Human and mouse FGF-8f share 98% aa identity (4), while the human FGF-8a sequence, which is common to all isoforms, 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 transition. 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. FGF-8a, b and e have transforming activities, although FGF-8b shows the strongest receptor affinity and oncogenic capacity (1, 5, 9, 10). 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, 9, 11).

  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. Tanaka, A. et al. (1992) Proc. Natl. Acad. Sci. USA 89:8928.
  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. Ghosh, A.K. et al. (1996) Cell Growth Differ. 7:1425.
  10. Mattila, M.M. et al. (2001) Oncogene 20:2791.
  11. Nezu, M. et al. (2005) Biochem. Biophys. Res. Commun. 335:843.

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Bioinformatics

Gene Symbol FGF8
Uniprot