Analytical Data
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Gene name
FGF2
- Application
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Alternative Names
Fibroblast growth factor 2;FGF-2;Basic fibroblast growth factor;bFGF;Heparin-binding growth factor 2;HBGF-2
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Species
Human
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Source
E. coli
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Tag
N-his
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P09038
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Protein Length
Partial
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Molecular Weight
31.6kDa
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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
Related Products
Identification
Protein Description
Fibroblast growth factor 2 (FGF2), also known as basic FGF (bFGF), is a multifunctional protein involved in various biological processes, including cell proliferation, differentiation, and angiogenesis. Its significance is underscored by its role in embryonic development, wound healing, and tissue repair. FGF2 operates through the interaction with specific FGF receptors, initiating several intracellular signaling pathways that influence cellular behaviors. Given its critical functions, FGF2 has garnered considerable attention in the fields of regenerative medicine and cancer therapy. Researchers have pursued the production of recombinant FGF2 to explore its therapeutic potential in various applications, including tissue engineering and the treatment of ischemic diseases. However, the functional activity of recombinant FGF2 can be influenced by factors such as its glycosylation state and folding. Therefore, optimizing expression systems and purification methods for producing biologically active recombinant FGF2 is essential to harness its therapeutic benefits. As studies progress, the characterization and application of FGF2 recombinant protein promise to advance our understanding of its biological roles and facilitate innovative approaches in medicine.
