Recombinant Human/Rat/Bovine FGF-10, Animal-Free Protein

FGF-10 activity is determined using the firefly luciferase reporter assay (*) in stably transfected HEK293T cells. Cells are treated in triplicate with a serial dilution of FGF-10. Firefly luciferase activity is measured and normalized. EC50 = 0.36 ng/ml (21.1 pM).*Promega pGL4.33[luc2P/SRE/Hygro] #E1340

FGF-10 migrates as a single band at 17 kDa in non-reducing (NR) conditions and upon reduction (R). No contaminating protein bands are visible.Purified recombinant human FGF-10 protein (7 µg) was resolved using 15% w/v SDS-PAGE in reduced (+ beta -mercaptoethanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250.

• Reactivity: Hu, Rt, Po, Bv
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human/Rat/Bovine FGF-10, Animal-Free Protein Summary

• Additional Information: Human/Rat/Bovine/Porcine
• Details of Functionality: No significant difference between EC₅₀ of reference and test lots
• Source: E. coli-derived FGF-10 protein
• Accession #: O15520.1
• Protein/Peptide Type: Animal-Free Recombinant Proteins
• Purity: Single species with expected mass
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 17 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: Monomeric FGF-10 protein only

Packaging, Storage & Formulations

• Storage: Store lyophilized protein between -20 °C and -80 °C until the date of expiry. Avoid freeze-thaw cycles.
• Buffer: Lyophilized from HEPES/NaCl/mannitol
• Purity: Single species with expected mass
• Reconstitution Instructions: Resuspend in water at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.

Notes

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.

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

Alternate Names for Recombinant Human/Rat/Bovine FGF-10, Animal-Free Protein

• FGF10
• FGF-10
• fibroblast growth factor 10
• Keratinocyte growth factor 2
• KGF2
• KGF-2
• produced by fibroblasts of urinary bladder lamina propria

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 human FGF-10 is an approximately 20 kDa protein that contains a serine-rich region near its N-terminus (2, 3). It shares 93% and 96% amino acid sequence identity with mouse and rat FGF-10, respectively. FGF-10 is secreted by mesenchymal cells and associates with extracellular FGF-BP (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 FGF-10 are critical in many tissues during embryogenesis. This includes limb bud initiation (6), palate development (7), branching morphogenesis and directional outgrowth of lung buds (8, 9), formation of the otic vesicle and chochlea (10), adipogenesis (11), and the development of prostate, mammary, lacrimal, and submandibular salivary glands (12 - 15). FGF R2 (IIIb) signaling in these responsive tissues is similarly important during embryogenesis (7, 10, 13 ‑ 15). The expression and function of FGF-10 are negatively regulated by Shh and BMP-4 in the developing lung (8, 9). Overlapping expression patterns and activities with FGF-3, -7,  and -8 suggest at least a partial redundancy in FGF‑10 biology (7, 10, 14, 15). FGF-10 induced signaling through FGF R2 (IIIb) also contributes to the progression of pancreatic cancer (16).

1. Beenken, A. and M. Mohammadi (2009) Nat. Rev. Drug Discov. 8:235.
2. Igarashi, M. et al. (1998) J. Biol. Chem. 273:13230.
3. Emoto, H. et al. (1997) J. Biol. Chem. 272:23191.
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. Bellusci, S. et al. (1997) Development 124:4867.
9. Weaver, M. et al. (2000) Development 127:2695.
10. Pirvola, U. et al. (2000) J. Neurosci. 20:6125.
11. Sakaue, H. et al. (2002) Genes Dev. 16:908.
12. Donjacour, A.A. et al. (2003) Dev. Biol. 261:39.
13. Mailleux, A.A. et al. (2002) Development 129:53.
14. Makarenkova, H.P. et al. (2000) Development 127:2563.
15. Jaskoll, T. et al. (2005) BMC Dev. Biol. 5:11.
16. Nomura, S. et al. (2008) Br. J. Cancer 99:305.

Bioinformatics

• Uniprot:
  • O15520.1()