Analytical Data
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Gene name
FGFB
- Application
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Alternative Names
Basic fibroblast growth factor Short name: bFGF Heparin-binding growth factor 2 Short name: 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 90% as determined by SDS-PAGE.
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Uniprot
P09038
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Expression Region
143-288aa
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Molecular Weight
20.4 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
FGFB (Fibroblast Growth Factor-Basic), a member of the fibroblast growth factor family, plays a crucial role in various biological processes, including cell proliferation, differentiation, and angiogenesis. Research on FGFB has gained significant attention due to its potential applications in regenerative medicine and cancer therapy. The ability of FGFB to stimulate cell growth and tissue repair makes it a target for developing treatments for chronic wounds and degenerative diseases. Moreover, its involvement in tumor growth and metastasis has led scientists to explore FGFB as a biomarker for cancer progression and a potential therapeutic target. Understanding the structure-function relationship of FGFB is essential for designing effective FGFB-based therapies, necessitating the development of recombinant FGFB proteins for both basic research and clinical applications. Advances in recombinant DNA technology have enabled the production of FGFB in various expression systems, allowing researchers to study its functional properties and interactions with other cellular components. As a result, FGFB research continues to evolve, contributing to our understanding of its biological significance and paving the way for innovative treatment strategies in medicine.
