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Recombinant human FGF-1 protein (Qk071)
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.
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1000µg will be despatched as 2 x 500µg
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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
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.
Acidic fibroblast growth factor, aFGF, Endothelial cell growth factor, ECGF, Heparin-binding growth factor 1, HBGF-1
human
species similarity:
mouse – 96%
rat – 96%
porcine – 97%
bovine – 92%
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
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%
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-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.
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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