Analytical Data
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Gene name
FGF3
- Application
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Alternative Names
FGF3；INT2；Fibroblast growth factor 3
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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
P11487
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Expression Region
18-239aa
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AA Sequence
AAGPGARLRRDAGGRGGVYEHLGGAPRRRKLYCATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGIVAIRGLFSGRYLAMNKRGRLYASEHYSAECEFVERIHELGYNTYASRLYRTVSSTPGARRQPSAERLWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVLDHRDHEMVRQLQSGLPRPPGKGVQPRRRRQKQSPDNLEPSHVQASRLGSQLEASAH
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Molecular Weight
32.4 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
Related Products
Protein Description
Fibroblast Growth Factor 3 (FGF3) is a member of the FGF family, which plays a critical role in various biological processes, including cell growth, differentiation, and tissue repair. Initially identified for its involvement in embryonic development, FGF3 has garnered significant attention due to its implications in cancer biology and regenerative medicine. Research has shown that FGF3 is often overexpressed in several malignancies, which contributes to tumorigenesis by promoting angiogenesis, cell proliferation, and metastasis. The recombinant FGF3 protein has been produced for various studies to explore its molecular mechanisms and potential therapeutic applications. Investigations into FGF3 have focused on its signaling pathways, including interactions with FGF receptors and downstream effectors, to elucidate its role in both normal physiology and pathological conditions. Additionally, recombinant FGF3 is being evaluated in preclinical models for its potential to enhance wound healing and tissue regeneration, highlighting its versatility in biomedical research. Understanding the function and mechanisms of FGF3 through recombinant protein studies could pave the way for novel therapeutic strategies targeting FGF3-related pathways in cancer and regenerative medicine.
