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Recombinant human/ rat/ bovine/ porcine FGF-10 protein

QK003

Brand: Qkine

Human epidermal growth factor (EGF) protein is a potent EGF-family growth factor used in many human and mouse organoid and stem cell culture systems including intestinal and tumor organoid culture. EGF is also used in epithelial cell culture.

Qkine human EGF (Qk011) is a highly pure, animal origin-free, bioactive 6.3 kDa recombinant protein, making it ideal for use in chemically defined induced pluripotent stem cell (iPSC), embryonic stem cell (ESC) and organoid culture media.

Currency: 

Product name Catalog number Pack size Price Price (USD) Price (GBP) Price (EUR)
Recombinant human/rat/bovine/porcine FGF-10 protein, 25 µg QK003-0025 25 µg (select above) $ 170.00 £ 125.00 € 146.00
Recombinant human/rat/bovine/porcine FGF-10 protein, 50 µg QK003-0050 50 µg (select above) $ 270.00 £ 200.00 € 234.00
Recombinant human/rat/bovine/porcine FGF-10 protein, 100 µg QK003-0100 100 µg (select above) $ 395.00 £ 280.00 € 328.00
Recombinant human/rat/bovine/porcine FGF-10 protein, 500 µg QK003-0500 500 µg (select above) $ 1,275.00 £ 910.00 € 1,063.00
Recombinant human/rat/bovine/porcine FGF-10 protein, 1000 µg QK003-1000 1000 µg (select above) $ 1,900.00 £ 1,400.00 € 1,636.00

Note: prices shown do not include shipping and handling charges.

Qkine company name and logo are the property of Qkine Ltd. UK.

Alternative protein names
Fibroblast Growth Factor 10, FGFA, KGF2, Keratinocyte growth factor 2
Species reactivity

human

species similarity:
mouse – 94%
rat – 100%
porcine – 99%
bovine – 99%

Frequently used together:

Summary

  • High purity human FGF-10 protein (residues 64-208, Uniprot: O15520)
  • >98%, by SDS-PAGE quantitative densitometry
  • 17 kDa
  • Expressed in E. coli
  • Animal origin-free (AOF) and carrier protein-free
  • Manufactured in Qkine's Cambridge, UK laboratories
  • Lyophilized from HEPES/NaCl/mannitol
  • Resuspend in water at >100 µg/ml, prepare single use aliquots, add carrier protein if desired and store frozen at -20oC or -80oC
Handling and Storage FAQ
  • Differentiation of embryonic stem cells into gut-like structures, cardiomyocytes and hepatocytes
  • Epithelial to mesenchymal transition

Bioactivity

Human FGF-10 Qk003 bioactivity EMT immunofluorescence lot #010

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 = 21.1 pM (0.36 ng/mL).Data from Qk003 lot #104403.

Purity

Human FGF-10 Qk003 protein purity SDS-PAGE lot #010

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 (+β-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250. Data from Qk003 lot #010.

Further quality assays

  • Mass spectrometry: single species with expected mass

  • Endotoxin: <0.005 EU/μg protein (below level of detection)

  • Recovery from stock vial:  >95%

Qkine FGF-10 is as biologically active as a comparable alternative supplier protein

Quantitative luciferase assay with Qkine FGF-10 (Qk003, green) and alternative supplier FGF-10 (Supplier B, black). Cells were treated in triplicate with a serial dilution of FGF-10 for 4 hours. Firefly luciferase activity was measured and normalized to control Renilla luciferase activity.

Protein background

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 (+β-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250. Data from Qk003 lot #010.

The mature form of human FGF-10 protein is an approximately 20 kDa protein highly similar to FGF-7 and with a serine-rich region near its N-terminus [1]. It is secreted by mesenchymal cells and is bound and activated by extracellular FGF-BP [2]. Human FGF10 protein is expressed in the mesenchyme and functions through interacting with the epithelial FGF Receptor 2b (FGFR 2b) [3]. It has also been shown to interact weakly with FGFR 1b [4].

Human fibroblast growth factor 10 is first active in the limb bud mesoderm where it creates and maintains FGF signaling with epithelial FGF-8, then drives a positive feedback loop accumulating mesenchyme in the growing bud, and finally induces the apical ectodermal ridge which ultimately gives rise to feet and hands [5]. Lung development is based on the same epithelial-mesenchymal FGF mediations involving FGF-10 from the foregut mesenchyme signaling to FGFR2 in the foregut epithelium [6]. Furthermore, FGF-10 protein is involved in the development of white adipose tissue, heart, liver, brain, kidney, thymus, inner ear, tongue, trachea, eye, prostate, salivary gland and mammary gland. It has been shown to induce migration and invasion of pancreatic cancer cells and to be associated with breast cancer risk, and patients with FGF-10 haploinsufficiency present symptoms of chronic obstructive pulmonary disease [3].

FGF-10 is involved in a number of different embryo and adult cell and tissue types, including mesenchymal, neuronal and epithelial cells. Human recombinant FGF-10 protein drives the differentiation of embryonic stem cells (ESC) into gut-like structures, cardiomyocytes and hepatocytes [3]. It is also a potent factor in the development of organoids, increasing organoid size and branching phenotype compared to other FGFs [7].

Background References

  1. M. Igarashi, P. W. Finch & S. A. Aaronson. Characterization of recombinant human fibroblast growth factor (FGF)-10 reveals functional similarities with keratinocyte growth factor (FGF-7). J. Biol. Chem. 273, 13230–5 (1998). doi.org/10.1074/jbc.273.21.13230
  2. H-D. Beer, M. Bittner, G. Niklaus, C. Munding, N. Max, A. Goppelt & S. Werner. The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair. Oncogene 24, 5269–77 (2005). doi.org/10.1038/sj.onc.1208560
  3. N. Itoh & H. Ohta. Fgf10: A Paracrine-Signaling Molecule in Development, Disease, and Regenerative Medicine. Curr. Mol. Med. 14, 504–509 (2014). doi: 10.2174/1566524014666140414204829
  4. X. Zhang, O. A. Ibrahimi, S. K. Olsen, H. Umemori, M. Mohammadi and D. M. Ornitz. Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family. J. Biol. Chem. 281, 15694–700 (2006). doi.org/10.1074/jbc.M601252200
  5. H. Ohuchi, T. Nakagawa, A. Yamamoto, A. Araga, T. Ohata, Y. Ishimaru, H. Yoshioka, T. Kuwana, T. Nohno, M. Yamasaki, N. Itoh and S. Noji. The mesenchymal factor, FGF10, initiates and maintains the outgrowth of the chick limb bud through interaction with FGF8, an apical ectodermal factor. Development 124, 2235–44 (1997). doi.org/10.1242/dev.124.11.2235
  6. H. Min, D. M. Danilenko, S. A. Scully, B. Bolon, B. D. Ring, J. E. Tarpley, M. DeRose, and W. S. Simonet. Fgf-10 is required for both limb and lung development and exhibits striking functional similarity to Drosophila branchless. Genes Dev. 12, 3156–61 (1998). doi: 10.1101/gad.12.20.3156
  7. A. Rabata, R. Fedr, K. Soucek, A. Hampl, Z. Koledova. 3D Cell Culture Models Demonstrate a Role for FGF and WNT Signaling in Regulation of Lung Epithelial Cell Fate and Morphogenesis. Front Cell Dev Biol. 2020 Jul 21;8:574. doi:10.3389/fcell.2020.00574.

Publications using recombinant human FGF-10 protein (Qk003)

Human epidermis organotypic cultures, a reproducible system recapitulating the epidermis in vitro
In Experimental Dermatology on 28 April 2023 by Agarwal, R. et al.
View publication

Generation of human iPSC-derived pancreatic organoids to study pancreas development and disease
bioRxiv preprint on 25 October 2024 by Darrigrand, J. et al.
View publication 

mTOR activity paces human blastocyst stage developmental progression
In Cell on 26 September 2024 by Lyer, D. P., Khoei, H. H. et al.
View publication