Analytical Data
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Gene name
FGF8
- Application
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Alternative Names
FGF8；AIGF；Fibroblast growth factor 8
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P55075
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Expression Region
23-143aa
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AA Sequence
QEGPGRGPALGRELASLFRAGREPQGVSQQHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGK
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Molecular Weight
44.9 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
Fibroblast growth factor 8 (FGF8) is a member of the fibroblast growth factor family that plays a crucial role in embryonic development, organogenesis, and tissue repair. Its diverse functions are primarily attributed to its ability to stimulate cell proliferation, differentiation, and survival through various signaling pathways, including the FGF receptor-mediated pathways. Research into FGF8 has expanded significantly due to its implications in developmental biology and its potential therapeutic applications in regenerative medicine and cancer treatment. Abnormal expression of FGF8 has been linked to several malignancies, making it a target for cancer therapies. Moreover, FGF8’s role in the development of the central nervous system and limb patterning has drawn attention to its potential in addressing congenital disorders. Recombinant FGF8 proteins are increasingly being utilized in research to elucidate its biological functions and to explore its therapeutic potentials in various fields, including tissue engineering and stem cell biology. By generating purified recombinant FGF8, scientists aim to analyze its interactions with receptors and downstream signaling molecules, thereby providing insights into its mechanisms of action. Understanding the biological roles and therapeutic applications of FGF8 is critical for advancing both basic and applied biomedical research, potentially leading to innovative treatments for diseases where FGF signaling is altered.
