Mouse FGF-8 Biotinylated Antibody Summary
Gln23-Arg215
Accession # NP_006110
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 (1‑3). 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).
- Mattila, M.M. and P.L. Harkonen (2007) Cytokine Growth Factor Rev. 18:257.
- Reuss, B. and O. von Bohlen und Halbach (2003) Cell Tiss. Res. 313:139.
- Tanaka, A. et al. (1992) Proc. Natl. Acad. Sci. USA 89:8928.
- Gemel, J. et al. (1996) Genomics 35:253.
- Olsen, S.K. et al. (2006) Genes Dev. 20:185.
- Crossley, P.H. et al. (1996) Cell, 84:127.
- Heikinheimo, M. et al. (1994) Mech. Dev. 48:129.
- Sun, X. et al. (1999) Genes Dev. 13:1834.
- Ghosh, A.K. et al. (1996) Cell Growth Differ. 7:1425.
- Mattila, M.M. et al. (2001) Oncogene 20:2791.
- Valve, E. et al. (2000) Int. J. Cancer 88:718.
- Valve, E.M. et al. (2001) Lab. Invest. 81:815.
- Nezu, M. et al. (2005) Biochem. Biophys. Res. Commun. 335:843.
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