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Recombinant human FGFbasic Protein

Cat # Size Price Quantity
63230120 μg$100
632302100 μg$275

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostE.coli
Target NameFGFbasic, Fibroblast Growth Factor-basic, FGF2
SpeciesHuman
accession numberNP_001997.5
SourcesA DNA sequence encoding the mature form of human bFGF (NP_001997.5) (Pro143-Ser288) was expressed with an additional Met at the N-terminus.
Molecular WeightThe recombinant human bFGF consists of 147 amino acids and predicts a molecular mass of 16.5 kDa.
Affinity TagNone
Purity≥ 95 % as determined by SDS-PAGE
Regulatory StatusRUO
Endotoxin level< 0.1 EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Background Information

Human FGF-basic (FGF2), also known as basic fibroblast growth factor (bFGF), is a multifunctional growth factor that regulates cell proliferation, survival, migration, differentiation, angiogenesis, wound healing, and tissue repair. FGF2 exerts its effects primarily by binding to fibroblast growth factor receptors (FGFR1–FGFR4), which are receptor tyrosine kinases. Heparan sulfate proteoglycans on the cell surface and extracellular matrix facilitate FGF2–FGFR binding and receptor activation, leading to downstream signaling pathways including MAPK/ERK, PI3K/AKT, and related pathways.



Structurally, human FGF2 is a small, highly conserved protein characterized by a 12-stranded β-trefoil fold. Its positively charged regions, particularly around the β1–β2 loop and β10–β12 region, form an important binding site for heparin and heparan sulfate. Unlike many secreted growth factors, FGF2 lacks a conventional N-terminal signal peptide and can reach the extracellular environment through unconventional secretion mechanisms.



FGF2 is itself a ligand for FGFR1, FGFR2, FGFR3, and FGFR4, although receptor interactions can vary according to receptor isoform and cellular context. Dysregulated FGF2 signaling has been associated with pathological angiogenesis, fibrosis, inflammation, abnormal bone remodeling, and cancer. Increased FGF2 activity can promote tumor-associated blood-vessel formation and support tumor-cell proliferation and survival.



Because FGF2 signaling can be either beneficial or harmful depending on context, it represents a potential therapeutic target as well as a therapeutic molecule. Recombinant FGF2 has been investigated for tissue regeneration and wound healing, whereas strategies that inhibit FGF2 or FGFR signaling—including neutralizing molecules and receptor kinase inhibitors—are being investigated for cancer, bone disease, and other disorders involving excessive FGF signaling.

Data Sheets

Recombinant human FGFbasic Protein TDS

Frequently Asked Questions

What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.
What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.
How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.
Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.
Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

Have a product or application question? Consult our FAQs or contact us.