Recombinant human FGF-4 protein (Qk004)

Human fibroblast growth factor 4 (FGF-4) protein is used for the proliferation and differentiation of embryonic and induced-pluripotent and tissue (mesenchymal) stem cells and promotes neural stem cell proliferation. Recombinant FGF-4 is an important component of cardiac, intestinal and other organoid culture media.

High purity and bioactivity 14 kDa, bioactive domain of human FGF-4, animal origin-free (AOF) and carrier-protein free.

Orders are typically shipped same or next day (except Friday).
Easy world-wide ordering, direct or through our distributors.

1000µg will be despatched as 2 x 500µg

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Buy online with secure credit card or purchase order.
For any questions, please email orders@qkine.com

Summary

  • High purity human FGF-4 protein (residues 79-206, Uniprot: P08620)

  • >98%, by SDS-PAGE quantitative densitometry

  • 14 kDa

  • Expressed in E. coli

  • Animal origin-free (AOF) and carrier protein-free

  • Manufactured in our 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 -20°C or -80°C

Featured applications

  • Hindgut organoids from iPSC-derived human posterior gut endoderm cells

  • Neural stem cell proliferation and neuronal differentiation

Fibroblast Growth Factor-4, Kaposi’s sarcoma-associated FGF, k-FGF, Heparin secretory-transforming protein 1 HST-1, Transforming protein KS3, Heparin-binding growth factor 4, HBGF-4

human

species similarity:
mouse – 91%
rat – 80%
porcine – 91%
bovine – 90%

Bioactivity

Qk004 FGF4-lot-#010-proliferation of iPSC

FGF-4 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-4. Firefly luciferase activity is measured and normalized. EC50 = 306.5 pM (4.3 ng/mL). Data from Qk004 lot #104330.

Purity

human-FGF-4-Qk004-protein-purity-lot-010

Recombinant human FGF-4 protein migrates as a single band at 14 kDa in non-reducing conditions (NR) and upon reduction (R). No contaminating protein bands are visible. Purified recombinant 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 Qk004 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%

We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine.  All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.

Qkine FGF-4 bioactivity is comparable to an alternative supplier protein

Quantitative luciferase assay with Qkine FGF-4 (Qk004, green) and alternative supplier FGF-4 (Supplier B, black). Cells were treated in triplicate with a serial dilution of FGF-4 for 3 hours. Firefly luciferase activity was measured and normalized to control Renilla luciferase activity.

Protein background

Fibroblast growth factor 4 (FGF-4) is a member of the FGF superfamily with a physiological role in the regulation of proliferation and differentiation in embryonic stem cells and tissue stem cells [1-3] .

Recombinant human FGF-4 protein promotes neural stem cell proliferation and neuronal differentiation in the postnatal brain [4], increases the proliferation rate of human adult bone-marrow derived mesenchymal stem cells [5] and supports the maintenance, proliferation and self-renewal properties of human embryonic stem cells [6].

Synergism between FGF-4 and WNT signalling acts to form hindgut organoids from iPSC-derived human posterior gut endoderm cells [7] and recombinant human FGF-4 protein is used to mimic embryonic intestinal development during directed differentiation in culture of pluripotent stem cells into intestinal organoids.

[1] Beenken, A. & Mohammadi, M. The FGF family: biology, pathophysiology and therapy. Nat. Rev. Drug Discov. 8, 235–53 (2009). doi.org/10.1038/nrd2792[2] Coutu, D. L. & Galipeau, J. Roles of FGF signaling in stem cell self-renewal, senescence and aging. Aging (Albany. NY). 3, 920–33 (2011).[3] Kosaka, N., Sakamoto, H., Terada, M. & Ochiya, T. Pleiotropic function of FGF-4: Its role in development and stem cells. Dev. Dyn. 238, 265–276 (2009). doi.org/10.1002/dvdy.21699[4] Kosaka, N. et al. FGF-4 regulates neural progenitor cell proliferation and neuronal differentiation. FASEB J. 20, 1484–1485 (2006). doi:10.1096/fj.05-5293fje[5] Farré, J. et al. FGF-4 increases in vitro expansion rate of human adult bone marrow-derived mesenchymal stem cells. Growth Factors 25, 71–76 (2007). doi.org/10.1080/08977190701345200[6] Mayshar, Y. et al. Fibroblast Growth Factor 4 and Its Novel Splice Isoform Have Opposing Effects on the Maintenance of Human Embryonic Stem Cell Self-Renewal. Stem Cells 26, 767–774 (2008). doi.org/10.1634/stemcells.2007-1037[7] Zhang, R.-R. et al. Human iPSC-Derived Posterior Gut Progenitors Are Expandable and Capable of Forming Gut and Liver Organoids. Stem Cell Reports 10, 780–793 (2018). doi.org/10.1016/j.stemcr.2018.01.006 

Additional resources

Our products are for research use only and not for diagnostic or therapeutic use.  Products are not for resale.

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