FGF-basic (154aa) protein: A multifunctional regulatory factor in stem cell culture and tissue repair
This article focuses on the molecular characteristics and biological functions of FGF-basic (also known as FGF-2/bFGF), systematically elaborating its key role as a core member of the FGF family in promoting the proliferation of various cells, regulating embryonic development, angiogenesis, and tissue repair. It also analyzes the molecular structure and improved thermal stability properties of its 154aa form.
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FGF-basic (154aa) Protein: A Multifunctional Regulator in Stem Cell Culture and Tissue Repair
Overview
This article systematically elaborates on the molecular characteristics and biological functions of FGF-basic (also known as FGF-2/bFGF), a core member of the FGF family, highlighting its key roles in promoting cell proliferation, regulating embryonic development, angiogenesis, and tissue repair. It also analyzes the molecular structure and thermal stability improvement features of its 154aa form.
This article systematically elaborates on the molecular characteristics and biological functions of FGF-basic (also known as FGF-2/bFGF), a core member of the FGF family, highlighting its key roles in promoting cell proliferation, regulating embryonic development, angiogenesis, and tissue repair. It also analyzes the molecular structure and thermal stability improvement features of its 154aa form.

I. Molecular Characteristics and Sequence Structure of FGF-basic
FGF-basic, also known as basic fibroblast growth factor (bFGF), FGF-2, or HBGF-2, is a member of the FGF superfamily and one of the most extensively studied among the 23 identified related mitogenic proteins. FGF-basic shares 35%-60% amino acid sequence conservation with other FGF family members (e.g., FGF-1) and features a characteristic central β-trefoil structure, but the two are distinguished as "basic" and "acidic" due to their differing isoelectric points.
Human FGF-basic consists of 288 amino acids and includes multiple isoforms. The four isoforms have molecular weights of 34 kDa, 24 kDa, 22.5 kDa, and 22 kDa, respectively, all initiated by CUG codons and primarily localized to the nucleus, featuring nuclear localization signals involved in intracellular signaling regulation. The classical secretory isoform, with a molecular weight of 18 kDa, comprises 155 amino acids and is initiated by an AUG codon. It lacks a conventional signal peptide and is secreted extracellularly via non-classical pathways. The 17 kDa sequence of mouse FGF-basic shares 98% amino acid identity with rat FGF-basic and 95% identity with human, bovine, and ovine FGF-basic. The 154aa form of FGF-basic encompasses its core structural region, including the complete heparin-binding site (amino acids 128–144) and receptor-binding functional domain, representing the smallest functional unit that retains full biological activity in vitro.
II. Receptor Binding and Signal Transduction Mechanisms of FGF-basic
FGF-basic initiates downstream signal transduction by binding to four high-affinity tyrosine kinase receptors (FGFR-1 to FGFR-4). Heparan sulfate proteoglycans (HSPGs) act as co-receptors, playing a critical role in the formation of FGF/FGFR complexes—binding of FGF to heparin or cell-surface HSPGs is a prerequisite for FGFR dimerization and activation. The signaling pathways activated by FGF-basic include the RAS-RAF-MAPK, PLCγ/PKC, and PI3K/AKT pathways, which collectively regulate cell proliferation, differentiation, and migration. FGF-basic exhibits mitogenic activity toward mesoderm-derived cells (fibroblasts, endothelial cells, osteoblasts, smooth muscle cells) as well as cells of neuroectodermal, ectodermal, and endodermal origin (e.g., astrocytes, oligodendrocytes, keratinocytes, neuroblasts).
III. Biological Functions and Applications of FGF-basic
FGF-basic is a key regulator of diverse physiological and pathological processes. In embryonic development and differentiation, it governs early embryogenesis and nervous system formation and serves as a core additive in embryonic stem cell culture media to maintain pluripotency without inducing differentiation. In angiogenesis, FGF-basic is a potent angiogenic factor, exhibiting chemotactic and mitogenic activity toward vascular endothelial cells and participating in tumor angiogenesis and neovascularization during tissue repair. In tissue repair and regeneration, FGF-basic promotes wound healing and tissue repair, stimulating the proliferation of various cells involved in tissue regeneration. Additionally, FGF-basic facilitates neuronal differentiation, survival, and regeneration, playing a vital role in nervous system development and neurodegenerative diseases. However, transgenic overexpression of FGF-basic, leading to excessive proliferation and angiogenesis, is associated with various pathological states, highlighting its "double-edged sword" nature.
IV. Conclusion
As one of the most functionally versatile members of the FGF family, FGF-basic plays an irreplaceable central role in embryonic development, tissue repair, and stem cell culture due to its multifaceted biological functions, including mitogenesis, angiogenesis, and differentiation regulation. Recombinant mouse FGF-basic (154aa) provides essential support for related basic research and application development.
In stem cell culture and tissue regeneration research, recombinant mouse FGF-basic is a critical tool for achieving cell proliferation, differentiation, and functional regulation. To meet these research needs, Uni offers FGF-basic (154aa) Protein, Mouse. This product is prepared using an E. coli expression system, with a molecular weight of approximately 16–17 kDa and purity verified by SDS-PAGE to exceed 95%. Its endotoxin level is below 0.01 EU/μg, making it suitable for experiments sensitive to endotoxins. The product is supplied as lyophilized powder and remains stable for one year when stored below -20°C. The protein has been validated to exhibit biological activity in BALB/c 3T3 cell proliferation assays, with an ED50 range of 0.3–1.8 ng/mL. It is suitable for maintaining pluripotency in mouse embryonic stem cells, studying the proliferation and differentiation of mouse mesenchymal stem cells, and conducting experiments related to tissue repair and regeneration.
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