Recombinant Mouse FGF-8c Protein Summary
Product Specifications
Gln23-Arg268 (Ala35Pro), with an N-terminal Met
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
424-FC
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 25 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
424-FC/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
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 (84 aa for FGF-8c; 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). Unique portions of FGF-8c are reported only for mouse, but the mouse FGF-8a sequence, which is common to all isoforms, shares 100% aa identity with human, 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. FGF-8b shows the strongest receptor affinity and oncogenic transforming capacity; while FGF-8c shows little transforming capacity (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.
- MacArthur, C.A. et al. (1995) J. Virol. 69:2501.
- 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.
Citations for Recombinant Mouse FGF-8c Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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FGFs, Wnts and BMPs mediate induction of VEGFR-2 (Quek-1) expression during avian somite development.
Authors: Nimmagadda S, Geetha-Loganathan P, Scaal M, Christ B, Huang R
Dev. Biol., 2007-03-01;305(2):421-9.
Species: Avian - Quail
Sample Types: In Vivo
Applications: In Vivo -
Retinoic acid signalling specifies intermediate character in the developing telencephalon.
Authors: Marklund M, Sjodal M, Beehler BC, Jessell TM, Edlund T, Gunhaga L
Development, 2004-08-04;131(17):4323-32.
Species: Chicken
Sample Types: Whole Tissue
Applications: Bioassay -
FGF8 dose-dependent regulation of embryonic submandibular salivary gland morphogenesis.
Authors: Jaskoll T, Witcher D, Toreno L, Bringas P, Moon AM, Melnick M
Dev. Biol., 2004-04-15;268(2):457-69.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay
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