Recombinant human FGF-1 protein

Summary

• High purity human protein (Uniprot number: P05230)
• 15.9 kDa (monomer)
• >98%, by SDS-PAGE quantitative densitometry
• Expressed in E. coli
• Animal origin-free (AOF) and carrier protein-free
• Manufactured in our Cambridge, UK laboratories
• Lyophilized from Tris, NaCl, CyS
• Resuspend in sterile-filtered water at >50 µg/ml, add carrier protein if desired, prepare single use aliquots and store frozen at -20 °C (short-term) or -80 °C (long-term).

Featured applications

• Epithelial organoid culture
• Differentiation of iPSCs into epithelial cells
• Mesenchymal stem cell research
• Organoid growth and proliferation
• Differentiation of neural progenitor cells into oligodendrocyte precursor cells
• Maintenance and differentiation of hematopoietic stem cells

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.

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