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Recombinant Human FGF-8b Heat Stable Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human FGF-8b Heat Stable Protein, CF Summary

Details of Functionality
Measured by its ability to activate SRE-SEAP reporter in HEK293 human embryonic kidney cells. The ED50 for this effect is 0.800-8.00 ng/mL.
Source
E. coli-derived human FGF-8 protein
Proprietary, engineered based on P55075
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
SDS-PAGE
22-27 kDa, under reducing conditions.

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and Brij-35 with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 100 μg/mL in water.

Notes

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

Alternate Names for Recombinant Human FGF-8b Heat Stable 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 (1-3). Alternate 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 (30 aa for FGF-8b; 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 FGF17 (75%) and FGF-18 (67%), and the three form an FGF subfamily (2). Mouse FGF-8b shares 100% aa identity with human FGF-8b. 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. FGF-8b shows the strongest receptor affinity and oncogenic transforming capacity although FGF-8a and FGF-8e are also transforming and have been found in human prostate, breast or ovarian tumors (1, 5, 9-12). 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, 13). Our proprietary Heat Stable FGF-8b (HS) is engineered for superior thermostability compared to the wild-type protein. Additionally, FGF-8b HS retains full bioactivity under heat-challenge conditions in a functional reporter assay.

  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 Tiss. 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. Valve, E. et al. (2000) Int. J. Cancer 88:718.
  12. Valve, E.M. et al. (2001) Lab. Invest. 81:815.
  13. Nezu, M. et al. (2005) Biochem. Biophys. Res. Commun. 335:843.

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