Recombinant Rat FGF-10 Protein Summary
| Details of Functionality |
Measured in a cell proliferation assay using 4MBr‑5 rhesus monkey epithelial cells. Rubin, J.S. et al. (1989) Proc. Natl. Acad. Sci. USA 86:802. The ED50 for this effect is 20-120 ng/mL. |
| Source |
E. coli-derived rat FGF-10 protein
Gln37-Ser215, with an N-terminal Met |
| Accession # |
|
| N-terminal Sequence |
Met |
| Structure / Form |
Monomer |
| Protein/Peptide Type |
Recombinant Proteins |
| Gene |
Fgf10 |
| Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
20.2 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. |
| SDS-PAGE |
22 kDa, 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, EDTA and DTT with BSA as a carrier protein. |
| Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Reconstitution Instructions |
Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat FGF-10 Protein
Background
The Fibroblast Growth Factors (FGFs) are heparin binding glycoproteins that exert a variety of biological activities toward cells of mesenchymal, neuronal, and epithelial origin. FGF-10 belongs to the subgroup of FGFs that also includes FGF-3, -7, and -22 (1). Mature rat FGF-10 is an approximately 20 kDa protein that contains a serine-rich region near its N-terminus (2). It shares 96% and 91% amino acid sequence identity with human and mouse FGF-10, respectively. FGF-10 is secreted by mesenchymal cells and associates with extracellular FGF-BP (1, 3). It preferentially binds and activates epithelial cell FGF R2 (IIIb) and interacts more weakly with FGF R1 (IIIb) (4). FGF-10 plays an important role in many tissues during embryogenesis. This includes limb bud initiation (5), palate development (6), branching morphogenesis and directional outgrowth of lung buds (7, 8), formation of the otic vesicle and chochlea (9), adipogenesis (10), folliculogenesis (11), cardiomyocyte differentiation (12), and the development of prostate, mammary, lacrimal, and submandibular salivary glands (13‑16). FGF R2 (IIIb) signaling in these responsive tissues is similarly important during embryogenesis (6, 9, 14‑16). The expression and function of FGF-10 are negatively regulated by Shh and BMP-4 in the developing lung (7, 8). Overlapping expression patterns and activities with FGF-3, -7, and -8 suggest at least a partial redundancy in FGF-10 biology (6, 8, 15, 16). FGF-10 signaling through FGF RIIIb also contributes to the progression of pancreatic cancer (17).
- Beenken, A. and M. Mohammadi (2009) Nat. Rev. Drug Discov. 8:235.
- Yamasaki, M. et al. (1996) J. Biol. Chem. 271:15918.
- Beer, H.-D. et al. (2005) Oncogene 24:5269.
- Zhang, X. et al. (2006) J. Biol. Chem. 281:15694.
- Min, H. et al. (1998) Genes Dev. 12:3156.
- Rice, R. et al. (2004) J. Clin. Invest. 113:1692.
- Bellusci, S. et al. (1997) Development 124:4867.
- Weaver, M. et al. (2000) Development 127:2695.
- Pirvola, U. et al. (2000) J. Neurosci. 20:6125.
- Sakaue, H. et al. (2002) Genes Dev. 16:908.
- Zhang, K. et al. (2010) Reproduction 140:815.
- Chan, S.S.-K. et al. (2010) PLoS ONE 5:e14414.
- Donjacour, A.A. et al. (2003) Dev. Biol. 261:39.
- Mailleux, A.A. et al. (2002) Development 129:53.
- Makarenkova, H.P. et al. (2000) Development 127:2563.
- Jaskoll, T. et al. (2005) BMC Dev. Biol. 5:11.
- Nomura, S. et al. (2008) Br. J. Cancer 99:305.
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