Recombinant Human FGF-8a Protein, CF

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Recombinant Human FGF-8a (Catalog # 4745-F8) stimulates cell proliferation of the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is 0.25-1.5 μg/mL in the presence of 10 μg/mL heparin.
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 at22 kDa.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human FGF-8a Protein, CF Summary

Details of Functionality
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 0.25-1.5 μg/mL in the presence of 10 µg/mL heparin.
Source
E. coli-derived human FGF-8 protein
Gln23-Arg204, with an N-terminal Met
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
Gene
FGF8
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
21 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.
Publications
Read Publications using
4745-F8 in the following applications:

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, and EDTA.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human FGF-8a Protein, CF

  • 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 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).

  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.

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Publications for FGF-8 (4745-F8)(4)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Bioassay.


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Bioinformatics

Gene Symbol FGF8
Uniprot