Analytical Data
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Gene name
FGF-9
- Application
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Alternative Names
GAF; HBFG9; Glia-Activating Factor; Heparin-Binding Growth Factor 9
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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
P31371
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Expression Region
Met1~Ser208
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Molecular Weight
26&27kDa
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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 9 (FGF-9) is a member of the fibroblast growth factor family, which plays a crucial role in various biological processes, including embryonic development, tissue repair, and cell proliferation. FGF-9 is particularly important in the development of the central nervous system, limb formation, and the regulation of endothelial cells, making it a key factor in angiogenesis. Research has indicated that FGF-9 can influence the proliferation and differentiation of various cell types, including neural progenitor cells and mesenchymal stem cells. The ability of FGF-9 to promote survival and growth in diverse cellular contexts has drawn considerable attention in the fields of regenerative medicine and cancer therapy. Recent studies have highlighted its potential therapeutic applications, including promoting tissue regeneration and serving as a target for cancer therapies, due to its involvement in tumor biology and the microenvironment. Given its multifaceted roles and significant implications in health and disease, the recombinant production of FGF-9 protein has been the focus of extensive research efforts aimed at elucidating its mechanisms of action, as well as exploring its therapeutic potential in regenerative medicine and oncology. Understanding the functional properties of FGF-9 and its signaling pathways could pave the way for novel therapeutic strategies that leverage its regenerative capabilities while minimizing adverse effects in clinical applications. Thus, ongoing investigations into FGF-9 continue to contribute to our understanding of its biological significance and its potential utility in medical science.
