Analytical Data
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Gene name
FGF-1
- Application
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Alternative Names
ECGF; AFGF; ECGFA; ECGFB; FGF-Alpha; FGFA; HBGF1; ECGFB; HBGF1; Acidic Fibroblast Growth Factor; heparin-binding growth factor 1; Endothelial Cell Growth Factor, Beta
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Species
Human
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 85% as determined by SDS-PAGE.
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Uniprot
P05230
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Expression Region
Phe16~Asp155
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Protein Length
Partial
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Molecular Weight
30kDa
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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
Fibroblast growth factor 1 (FGF-1), also known as acidic fibroblast growth factor (aFGF), is a key member of the fibroblast growth factor family, which is involved in various biological processes such as cell proliferation, differentiation, and tissue repair. The significance of FGF-1 in the regulation of angiogenesis, wound healing, and neuronal survival has made it a focal point of research in regenerative medicine and developmental biology. Given its broad biological activities, FGF-1 has potential therapeutic applications in conditions like ischemic diseases, nerve injuries, and various types of cancer. The recombinant production of FGF-1 has allowed for more detailed studies of its functional properties and interactions at the molecular level. Moreover, advancements in biotechnology have facilitated the application of FGF-1 in drug development, especially in terms of designing targeted therapies. Researchers are increasingly exploring its mechanism of action, signaling pathways, and potential side effects to optimize its clinical use. Understanding and manipulating FGF-1's activity could lead to innovative strategies for enhancing tissue repair and regeneration, making it a pivotal target in contemporary biomedical research.
