Technical Data
F4212-05B
Fibroblast Growth Factor 10, Recombinant, Mouse (FGF10)
25ug
Growth Factors, Cytokines Storage: -20CShipping: Blue Ice
The Fibroblast Growth Factors (FGFs) are heparin binding glycoproteins that exert a variety of
biological activities toward cells of mesenchymal, neuronal, and epithelial origin. FGF10 belongs to the subgroup of FGFs that also includes FGF3, 7, and 22 (1). Mature mouse FGF10 is an approximately 20kD protein that contains a serinerich region near its Nterminus (2, 3). C terminal to this region (aa 62 209), it shares 94% and 100% amino acid sequence identity with human and rat FGF10, respectively. FGF10 is secreted by mesenchymal cells and associates with extracellular FGFBP (1, 4). It preferentially binds and activates epithelial cell FGF R2 (IIIb) and interacts more weakly with FGF R1 (IIIb) (5). The mitogenic and chemotactic properties of FGF10 are critical in many tissues during embryogenesis. This includes limb bud initiation (6), palate development (7), branching morphogenesis and directional outgrowth of lung buds (2, 8), formation of the otic vesicle and chochlea (9), adipogenesis (10), and the development of prostate, mammary, lacrimal, and submandibular salivary glands (11 14). FGF R2 (IIIb) signaling in these responsive tissues is similarly important during embryogenesis (7, 9, 12 14).
The expression and function of FGF10 are negatively regulated by Shh and BMP4 in the developing lung (2, 8). Overlapping expression patterns and activities with FGF3, 7, and 8 suggest at least a partial redundancy in FGF10 biology (7, 9, 13, 14). FGF10 induced signaling through FGF R2 (IIIb) also contributes to the progression of pancreatic cancer (15).

Source:
Recombinant corresponding to Ser62-Thr209 from mouse Fibroblast Growth Factors expressed in E. coli.

Molecular Weight:
~17.1kD

Biological Activity:
Measured in a cell proliferation assay using 4MBr5 monkey epithelial cells. Rubin, J.S. et al. (1989) Proc. Natl. Acad. Sci. USA 86:802. The ED50 for this effect is typically 20-120ng/ml.

Endotoxin Level:
<1EU/ug (LAL method)

Storage and Stability:
Lyophilized powder may be stored at -20C. Stable for 12 months at -20C. Reconstitute with BSA. Aliquot to avoid repeated freezing and thawing. Store at -20C. Reconstituted product is stable for 6 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Source: E.coli
Purity: ~95% (SDS-PAGE)
Concentration: Not determined
Form: Supplied as a lyophilized powder in MOPS, Na2SO4, EDTA and DTT with BSA as a carrier protein. Reconstitute with 100ug/ml in PBS containing at least 0.1% human or bovine serum albumin.

Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
1. Beenken, A. and M. Mohammadi (2009) Nat. Rev. Drug Discov. 8:235. 2. Bellusci, S. et al. (1997) Development 124:4867. 3. Tagashira, S. et al. (1997) Gene 197:399. 4. Beer, H.D. et al. (2005) Oncogene 24:5269. 5. Zhang, X. et al. (2006) J. Biol. Chem. 281:15694. 6. Min, H. et al. (1998) Genes Dev. 12:3156. 7. Rice, R. et al. (2004) J. Clin. Invest. 113:1692. 8. Weaver, M. et al. (2000) Development 127:2695. 9. Pirvola, U. et al. (2000) J. Neurosci. 20:6125. 10. Sakaue, H. et al. (2002) Genes Dev. 16:908. 11. Donjacour, A.A. et al. (2003) Dev. Biol. 261:39. 12. Mailleux, A.A. et al. (2002) Development 129:53. 13. Makarenkova, H.P. et al. (2000) Development 127:2563. 14. Jaskoll, T. et al. (2005) BMC Dev. Biol. 5:11. 15. Nomura, S. et al. (2008) Br. J. Cancer 99:305.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.