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Recombinant human FGF-1 protein

QK071

Brand: Qkine

Fibroblast Growth Factor 1 (FGF-1) can stimulate growth and differentiation of endothelial and epithelial cells and the development of organoids. FGF-1 can also be used for the maintenance of oligodendrocytes and astroglia as well as bone marrow-derived mesenchymal and hematopoietic stem cells.

Qkine human FGF-1 has a molecular weight of 15.9 kDa. This protein is animal origin-free, carrier-free and tag-free to ensure its purity with exceptional lot-to-lot consistency. Qk071 is suitable for the culture of reproducible mesenchymal, endothelial, haematopoietic, glial, and other relevant cells.

Currency: 

Product name Catalog number Pack size Price Price (USD) Price (GBP) Price (EUR)
Recombinant human FGF-1 protein, 50 µg QK071-0050 50 µg (select above) $ 185.00 £ 140.00 € 164.00
Recombinant human FGF-1 protein, 100 µg QK071-0100 100 µg (select above) $ 280.00 £ 210.00 € 246.00
Recombinant human FGF-1 protein, 500 µg QK071-0500 500 µg (select above) $ 725.00 £ 540.00 € 631.00
Recombinant human FGF-1 protein, 1000 µg QK071-1000 1000 µg (select above) $ 1,050.00 £ 800.00 € 935.00

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
Acidic fibroblast growth factor, aFGF, Endothelial cell growth factor, ECGF, Heparin-binding growth factor 1, HBGF-1
Species reactivity

human

species similarity:
mouse – 96%
rat – 96%
porcine – 97%
bovine – 92%

Frequently used together with:

Summary

  • High purity human protein (Uniprot number: P05230)
  • >98%, by SDS-PAGE quantitative densitometry
  • Source: Expressed in E. coli
  • 15.9 kDa monomer
  • Animal origin-free (AOF) and carrier protein-free
  • Manufactured in Cambridge, UK
  • Lyophilized from Tris/NaCl/CyS
  • 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
Handling and Storage FAQ

Featured applications

  • Maintenance of mesenchymal cells
  • Proliferation of endothelial cells
  • Differentiation of epithelial cells
  • Development of epithelial organoids
  • Maintenance of oligodendrocytes and astroglia
  • Culture of bone marrow-derived mesenchymal and hematopoietic stem cells.

Bioactivity

Qk071-FGF-1-bioactivity

FGF-1 activity is determined using the FGF-1-responsive firefly luciferase reporter assay. HEK293T cells are treated in triplicate with a serial dilution of FGF-1 for 3 hours. Firefly luciferase activity is measured and normalised to the control Renilla luciferase activity. EC50 = 0.81 ng/ml (51 pM). Data from Qk071 lot #204543.

Purity

Qk071-FGF-1-purity

Recombinant FGF-1 migrates as a major band at approximately 15.97 kDa in non-reduced (NR) and reduced (R) conditions. No contaminating protein bands are present. The purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptoethanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250. Data from Qk071 batch #204543.

Further quality assays

  • Mass spectrometry, single species with the expected mass
  • Endotoxin: <0.005 EU/μg protein (below the level of detection)
  • Recovery from stock vial: >95%

Qkine FGF-1 is as biologically active as a comparable alternative supplier protein

HEK293T luciferase reporter cells were treated in triplicate with a serial dilution of Qkine FGF-1 (Qk071, green) or alternative supplier protein (Supplier B, black) for 3 hours. Firefly luciferase activity was measured and normalized to control Renilla luciferase activity. Data from Qk071 lot #204537.

Protein background

Fibroblast Growth Factor 1 (FGF-1) is a member of the FGF family and regulates the proliferation, migration, and differentiation of mesenchymal cells [1–3]. It plays a crucial role in multiple biological processes including embryonic development and tissue regeneration [1,2,4,5]. It is a key regulator of angiogenesis and wound healing as it regulates the proliferation and maintenance of endothelial and epithelial cells [3]. It has neurotrophic properties to protect and repair neurons and lipid metabolism functions to regulate adipocytes [5,6]. FGF-1 can also promote the differentiation of hematopoietic stem cells [7]. Notably, FGF-1 is implicated in the tumour growth and migration [8].

FGF-1 is composed of 155 amino acids, with a molecular weight of approximately 17-18 kDa [2,9]. It consists of 12 anti-parallel β-strands organized into a three-fold symmetric β-sheet [10]. FGF-1 binds to different FGF receptors such as FGFR1 triggering several signaling cascades involved in cell growth, proliferation, migration, survival, and differentiation. These include the Ras/Raf/Mek/Erk, Pi3k/Akt, Jnk/Mapk, and STAT3/Nf-kb pathways [8].

The role of FGF-1 on embryonic development and the regulation of mesenchymal cells makes it a growth factor used for a range of different cultures in vitro. FGF-1 is used to promote the differentiation and proliferation of endothelial cells and epithelial cells [11,12]. As FGF-1 also promotes the branching of epithelial cells, it has been used for embryonic lung epithelium cultures and human iPSC-derived uretic bud organoids13,14. Additionally, its neurotrophic properties make it ideal for the maintenance of neural progenitors as well as supporting cells such as oligodendrocytes, and astroglia [5,15–17]. FGF-1 has also been reported for the culture of bone marrow-derived mesenchymal and hematopoietic stem and progenitor cells [7,18,19].

Because of its diverse roles in cellular processes, FGF-1 is a target of interest in various clinical applications, including regenerative medicine, wound healing therapies, and potential treatments for metabolic disorders and neurodegenerative diseases [3,6,16]. In Type 2 diabetes, FGF-1 injections could lower the glucose level without risk of hypoglycaemia through its effect on glucose-sensing neuronal circuits [6]. In neurodegenerative diseases such as multiple sclerosis, FGF-1 could promote the remyelination of neurons [16]. Its role in angiogenesis could have great potential for novel therapies for myocardial infarction4. Finally, its involvement in cancer progression has led to investigations into targeted therapies to inhibit FGF-1 signaling in cancer cells.

Background references

  1. FGF1 fibroblast growth factor 1 [Homo sapiens (human)] – Gene – NCBI. https://www.ncbi.nlm.nih.gov/gene/2246.
  2. Ornitz, D. M. & Itoh, N. Fibroblast growth factors. Genome Biol. 2, reviews3005.1 (2001).
  3. Zakrzewska, M., Marcinkowska, E. & Wiedlocha, A. FGF-1: From Biology Through Engineering to Potential Medical Applications. Crit. Rev. Clin. Lab. Sci. 45, 91–135 (2008).
  4. Engel, F. B., Hsieh, P. C. H., Lee, R. T. & Keating, M. T. FGF1/p38 MAP kinase inhibitor therapy induces cardiomyocyte mitosis, reduces scarring, and rescues function after myocardial infarction. Proc. Natl. Acad. Sci. 103, 15546–15551 (2006).
  5. Nurcombe, V., Ford, M. D., Wildschut, J. A. & Bartlett, P. F. Developmental Regulation of Neural Response to FGF-1 and FGF-2 by Heparan Sulfate Proteoglycan. Science 260, 103–106 (1993).
  6. Gasser, E., Moutos, C. P., Downes, M. & Evans, R. M. FGF1 — a new weapon to control type 2 diabetes mellitus. Nat. Rev. Endocrinol. 13, 599–609 (2017).
  7. Walenda, T. et al. Synergistic effects of growth factors and mesenchymal stromal cells for expansion of hematopoietic stem and progenitor cells. Exp. Hematol. 39, 617–628 (2011).Raju, R. et al. A Network Map of FGF-1/FGFR Signaling System. J. Signal Transduct. 2014, 962962 (2014).
  8. Liu, Y. et al. Advances in FGFs for diabetes care applications. Life Sci. 310, 121015 (2022).
  9. Zhu, X. et al. Three-Dimensional Structures of Acidic and Basic Fibroblast Growth Factors. Science 251, 90–93 (1991).
  10. Kang, S. S., Gosselin, C., Ren, D. & Greisler, H. P. Selective stimulation of endothelial cell proliferation with inhibition of smooth muscle cell proliferation by fibroblast growth factor-1 plus heparin delivered from fibrin glue suspensions. Surgery 118, 280–287 (1995).
  11. Ramos, C. et al. FGF-1 reverts epithelial-mesenchymal transition induced by TGF-β1 through MAPK/ERK kinase pathway. Am. J. Physiol.-Lung Cell. Mol. Physiol. 299, L222–L231 (2010).
  12. Cardoso, W. V., Itoh, A., Nogawa, H., Mason, I. & Brody, J. S. FGF-1 and FGF-7 induce distinct patterns of growth and differentiation in embryonic lung epithelium. Dev. Dyn. 208, 398–405 (1997).
  13. Mae, S.-I. et al. Expansion of Human iPSC-Derived Ureteric Bud Organoids with Repeated Branching Potential. Cell Rep. 32, 107963 (2020).
  14. Jiang, P. & Deng, W. Regenerating white matter using human iPSC-derived immature astroglia. Neurogenesis 3, e1224453 (2016).
  15. Mohan, H. et al. Transcript profiling of different types of multiple sclerosis lesions yields FGF1 as a promoter of remyelination. Acta Neuropathol. Commun. 2, 178 (2014).
  16. Jiang, P. et al. Human iPSC-Derived Immature Astroglia Promote Oligodendrogenesis by Increasing TIMP-1 Secretion. Cell Rep. 15, 1303–1315 (2016).
  17. Haan, G. de et al. In Vitro Generation of Long-Term Repopulating Hematopoietic Stem Cells by Fibroblast Growth Factor-1. Dev. Cell 4, 241–251 (2003).
  18. Jiang, S. et al. Novel insights into a treatment for aplastic anemia based on the advanced proliferation of bone marrow‑derived mesenchymal stem cells induced by fibroblast growth factor 1. Mol. Med. Rep. 12, 7877–7882 (2015).