Mature domain of human FGF10 (residues 64-208, Uniprot: O15520) expressed in E.coli and purified to homogeneity, non-glycosylated protein with a molecular weight of 17 kDa.
Recombinant human FGF-10
£160.00 – £1,200.00
Fibroblast growth factor 10 is part of the fibroblast growth factor (FGF) family. Members of this family are heparin binding glycoproteins involved in a number of different embryo and adult cell and tissue types, including mesenchymal, neuronal and epithelial cells. FGf-10 is expressed in the mesenchyme and functions through interacting with the epithelial FGF Receptor 2b (Fgfr2b) with heparin/heparan sulfate1. It has also been shown to interact weakly with FGF Receptor 1b2. The mature form of human FGF-10 is an approximately 20 kDa protein highly similar to FGF-7 and with a serine-rich region near its N-terminus3. It is secreted by mesenchymal cells and is bound and activated by extracellular FGF-BP4.
FGF-10 is first active in the limb bud mesoderm where it creates and maintains FGF signalling 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 hands5. Lung development is based on the same epithelial-mesenchymal FGF mediations involving FGF-10 from the foregut mesenchyme signalling to FGFR-2 in the foregut epithelium6. Further, FGF-10 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, and has been shown to induce migration and invasion of pancreatic cancer cells, to be associated with breast cancer risk, and patients with FGF-10 haploinsufficiency present symptoms of chronic obstructive pulmonary disease. FGF-10 also drives the differentiation of embryonic stem cells into gut-like structures, cardiomyocytes, and hepatocytes1.
Product: recombinant human FGF10
Mature domain of human FGF10 (residues 64-208, Uniprot: O15520) expressed in E.coli and purified to homogeneity.
Mature protein is a non-glycosylated protein with a molecular weight of 17 kDa.
Protein is provided in PBS without carrier protein at 1 mg/ml.
M G R H V R S Y N H L Q G D V R W R K L F S F T K Y F L K I E K N G K V S G T K K E N C P Y S I L E I T S V E I G V V A V K A I N S N Y Y L A M N K K G K L Y G S K E F N N D C K L K E R I E E N G Y N T Y A S F N W Q H N G R Q M Y V A L N G K G A P R R G Q K T R R K N T S A H F L P M V V H S
Fibroblast Growth Factor-10, FGFA, KGF-2, Keratinocyte growth factor 2
We take the quality of our products very seriously, please see this blog by our founder, Marko Hyvonen to understand why we think improving growth factor quality will save valuable R&D time and expense. All our proteins are produced in-house by our scientists and we understand the potential impact on your work if your growth factors and cytokines are not consistent and of the highest quality. We provide quality control data for each individual batch, please contact us any time if you have any questions.
The biochemical identity of each batch of human recombinant FGF10 is testing by SDS-PAGE and mass spec. Correct recovery from the vial is checked to ensure you will get what you expect.
Stem cell cultures are sensitive to endotoxins, which can be present in media, serum and as a contaminants on plastic ware. We optimise our protein production processes to ensure the lowest possible levels of endotoxin contamination. Endotoxin levels are determined by an external expert microbiological testing services provider and we set our endotoxin pass criteria at the industry leading <0.1 EU per ug protein and aim for <0.01 EU per ug protein. We report the exact endotoxin levels for each batch.
hFGF10 batch #010 endotoxin level = <0.0005 EU/ug protein (below the detection level of the assay)
Our human recombinant FGF10 has been extensively tested by an independent stem cell specialist biotech company, Stemnovate.
Please see the datasheet for full batch-specific quality testing results, customer feedback and additional information.
Please contact us at firstname.lastname@example.org for batch reservation, bulk purchasing arrangements or any other questions.
1. Itoh, N. & Ohta, H. Fgf10: A Paracrine-Signaling Molecule in Development, Disease, and Regenerative Medicine. Curr. Mol. Med. 14, 504–509 (2014).
2. Zhang, X. et al. Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family. J. Biol. Chem. 281, 15694–700 (2006).
3. Igarashi, M., Finch, P. W. & Aaronson, S. A. 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).
4. Beer, H.-D. et al. 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).
5. Ohuchi, H. et al. 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).
6. Min, H. et al. Fgf-10 is required for both limb and lung development and exhibits striking functional similarity to Drosophila branchless. Genes Dev. 12, 3156–61 (1998).
1000 µg, 500 µg, 100 µg, 50 µg
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