GMP-Ready Recombinant Human FGF-2 (145 aa) Protein

FGF-2 (145 aa)

FGF-2

Support stem and progenitor cell maintenance, proliferation and expansion with highly pure FGF-2, complete with regulatory documents

FGF-2 is a key growth factor that regulates cell proliferation and survival. It supports the expansion and maintenance of stem and progenitor cells, including mesenchymal and pluripotent stem cells, making it widely used in stem cell culture and regenerative medicine applications.

This highly pure and bioactive 17 kDA FGF-2 protein is AOF certified, CF, and comprised of the core structured region (145 aa), sufficient for robust and reproducible bioactivity.

  • Neural stem cell (NSC) therapy
  • Regenerative stem cell therapy
  • Pluripotent stem cell therapy
  • Expressed in E. coli
  • Animal origin-free (AOF) and carrier protein-free (CF)
  • Manufactured under a certified ISO 9001:2015 Quality Management System
  • 17 kDa monomer
  • >98%, by SDS-PAGE quantitative densitometry
  • Lyophilized from Tris, NaCl, CyS, mannitol
  • Reconstitute 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).
  • Qk025-0050 = 50 µg
  • Qk025-0100 = 100 µg
  • Qk025-0500 = 500 µg
  • Qk025-CTG-0500= 500 µg
Please download FGF-2 (145 aa) resources here:

Applications

iPSC
MAINTENANCE

ESC
MAINTENANCE

Cells - MSC Proliferation

MSC
PROLIFERATION

Cells - CAR-NK

ORGANOID
GROWTH

Recommended for iPSC/ESC maintenance and MSC proliferation and differentiation.

High Purity FGF-2
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High Purity

FGF-2 migrates as major band at 17 kDa in non-reducing (-βME) conditions and upon reduction (+βME). The higher molecular mass band at 35 kDa is a dimer that we always see in our highly purified human FGF-2, the presence of this does not affect biological activity. 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 Qk025 lot #014.

Bioactivity FGF-2
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Bioactivity

FGF-2 (145 aa) was more bioactive than the WHO (NIBSC) standard FGF-2. FGF-2 activity was determined using the Promega serum response element luciferase reporter assay in transfected HEK293T cells. Cells were treated in triplicate with a serial dilution of FGF-2 for 3 hours. Firefly luciferase activity was measured and normalized to the control Renilla luciferase activity. Qk025 #204697, EC50 = 0.39 ng/ml, WHO (NIBSC) EC50 = 1.02 ng/ml.

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Product Background

Fibroblast growth factors (FGFs) are a family of growth factors which regulate a wide range of essential biological functions including cell proliferation and survival, migration and differentiation [1]. The human FGF family has 18-22 members grouped into 6-7 subfamilies based on sequence homology and phylogeny [2]. The FGF family of growth factors have critical roles during both vertebrate and invertebrate embryonic development, in adult cells they modulate tissue maintenance, wound healing and angiogenesis [1,2].

The FGF ligands bind to 4 receptors (FGFR1-4), transmembrane receptors with intracellular tyrosine kinase activity [2, 3]. Once activated FGFRs recruit Src homology-2 (SH2) or phosphotyrosine binding (PTB) domain-containing signaling proteins leading to activation of intracellular signaling pathways [1]. The main signaling pathways activated by FGF binding are the RAS/MAP kinase pathway, PI3 kinase/Akt pathway, and PLCγ pathways [1-3].

Fibroblast growth factor 2 (FGF-2) also known as basic fibroblast growth factor (bFGF) has a broad range of physiological roles including regulation of cell growth, survival and proliferation. FGF-2 is one of the FGFs which binds to and signals through all four of the FGFRs [4].

FGF-2 is an essential growth factor for the maintenance of pluripotency in human embryonic stem cells (ESCs), induced pluripotent stem cells (iPSCs) [4] and mesenchymal stem cells (MSCs) [5]. FGF-2 preserves pluripotency through interaction with PI3 kinase/Akt, ERK1/2, JAK/STAT and PLCγ pathways by activation of activin A. In feeder culture systems FGF-2 stimulates production of essential growth factors and cytokines from the feeder layer [5].

[1] Yun YR, Won JE, Jeon E et al. Fibroblast growth factors: biology, function, and application for tissue regeneration. J. Tissue Eng. vol. 7, pp. 2010:218142, Nov. 2010. doi: 10.4061/2010/218142

[2] Xie Y, Su N, Yang J et al. FGF/FGFR signaling in health and disease. Sig. Transduct. Target. Ther. vol. 5, no. 181, 2020. doi.org/10.1038/s41392-020-00222-7

[3] Beenken A and Mohammadi M. The FGF family: biology, pathophysiology and therapy. Nat. Rev. Drug Discov. vol. 8, no. 3, pp. 235-53. Mar. 2009. doi: 10.1038/nrd2792

[4] Mossahebi-Mohammadi M, Quan M, Zhang JS and Li W. FGF Signaling Pathway: A Key Regulator of Stem Cell Pluripotency. Front. Cell Dev. Biol. vol. 8, pp. 79, 2020. doi: 10.3389/fcell.2020.00079

[5] Lai WT, Krishnappa V and Phinney DG. Fibroblast growth factor 2 (Fgf2) inhibits differentiation of mesenchymal stem cells by inducing Twist2 and Spry4, blocking extracellular regulated kinase activation, and altering Fgf receptor expression levels. Stem Cells, vol. 29, no. 7, pp. 1102-11, Jul. 2011. doi: 10.1002/stem.661

Frequently asked questions

Fibroblast growth factor 2 (FGF-2), also known as basic fibroblast growth factor (bFGF) is a growth factor and signaling protein.
FGF-2 is expressed in a developmental and tissue specific manner. It’s expression is tightly controlled in normal tissues and it can be detected in all major tissues.
FGF-2 is essential for normal embryonic development. It has roles in cell survival and proliferation, angiogenesis, tumorigenesis, wound healing and tissue repair.
FGF-2 binds toand signals though all four of the FGF receptors FGFR1-4.

FGFRs phosphorylate specific tyrosine residues and activate the RAS-MAPK, PI3K-AKT, PLCγ, and STAT intracellular signaling pathways.

FGF-2 is used to maintain the pluripotency of stem cells in culture.

We offer the 145 amino acid form rather than the 146 due to the E. coli processing of the N-terminal. When the 146 form (Pro143-Ser288) is expressed, the proline is either partially or completely removed. To improve expression in E. coli, we chose to start with the alanine (Ala144-Ser288) form. This modification does not affect receptor binding or bioactivity.

Other listings of the 146 amino acid form will often be a mixture of FGF-2 146 and 145, or, in some cases, only the 145 form.

Fibroblast Growth Factor 2 (FGF-2) exists in two main isoforms, distinguished by length: 145 amino acids (aa) and 154 aa. The 154 aa variant contains an additional nine amino acids at the N-terminus. While this extension is not essential for biological activity, it may influence the protein’s localization within cells.

Key differences between the isoforms:

  • FGF-2 (145 aa):
    • The most widely used form, supporting proliferation and survival of stem and progenitor cells.
    • Commonly preferred for organoid culture due to its robust activity and well-established performance.
  • FGF-2 (154 aa):
    • Contains an N-terminal extension that may affect intracellular localization or signaling.
    • Typically, not required for standard organoid or stem cell maintenance, unless specific signaling or localization effects are being investigated.

Recombinant FGF2-G3 (FGF2-STAB®) is a thermostable, engineered form of FGF-2 (bFGF). This modification significantly increases the protein’s functional half-life — from <10 hours for wild-type FGF-2 to >7 days for FGF2-G3 — improving stability and consistency in culture systems.

Disclaimer

For use in manufacturing of cellular or gene therapy products.
Not intended for in vivo applications.

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