Analytical Data
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Gene name
FGF basic/bFGF
- Application
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Biological Activity
1.The ED50 is <0>2.0 × 106 units/mg. 2.Measured in a cell proliferation assay using NIH-3T3 mouse fibroblast cells. The ED50 for this effect is <7>1.3×105 U/mg. Measured in a cell proliferation assay using NIH-3T3 mouse fibroblast cells. The ED50 for this effect is 2.517 ng/mL,corresponding to a specific activity is 3.97×105 U/mg.
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Alternative Names
rMubFGF; HBGF-2; FGF-2; FGF-b; FGF-basic
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Species
Mouse
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 95% as determined by reducing SDS-PAGE.
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Uniprot
P15655
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Expression Region
P10-S154
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Protein Length
Full Length of Mature Protein
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Molecular Weight
17 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples 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.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Basic fibroblast growth factor (bFGF), also known as FGF-2, is a key member of the fibroblast growth factor family, playing a crucial role in various biological processes such as cell proliferation, differentiation, and angiogenesis. The importance of bFGF in wound healing and tissue repair has sparked significant interest in its therapeutic potential. Research has indicated that bFGF can stimulate fibroblast activity, enhance vasculogenesis, and promote collagen synthesis, making it a valuable candidate for regenerative medicine and tissue engineering. Recombinant bFGF has been produced in various expression systems, enabling the study of its biological functions and therapeutic applications. The ability to produce this growth factor in a controlled manner allows for the development of bFGF-based treatments for conditions such as chronic wounds, ischemic diseases, and even certain cancers. Ongoing studies aim to optimize its delivery and efficacy, exploring combinations with biomaterials and other growth factors to maximize its regenerative capabilities. As the understanding of bFGF’s mechanisms of action expands, its integration into clinical practices holds promise for advancing therapeutic strategies in regenerative medicine.
