Analytical Data
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Gene name
FGF3
- Application
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Alternative Names
HBGF3; INT2; Heparin-binding growth factor 3; Murine Mammary Tumor Virus Integration Site(v-int-2)Oncogene Homolog; INT-2 Proto-Oncogene Protein; Proto-oncogene Int-2
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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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
Tyr154~Ser232
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Protein Length
Partial
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Molecular Weight
44kDa
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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 fibroblast growth factor family, which plays a critical role in various biological processes, including cell proliferation, differentiation, and survival. FGF3 is particularly important in embryonic development, particularly in the formation of the inner ear and skeletal systems. Abnormal expression of FGF3 has been implicated in several diseases, including cancer, as it can influence tumor growth and metastasis. In recent years, research has increasingly focused on recombinant FGF3 protein due to its potential therapeutic applications. By producing FGF3 in a recombinant form, scientists can study its functional properties in detail, develop targeted therapies, and investigate its role in pathology. The ability to generate recombinant FGF3 allows for the exploration of its signaling pathways, interaction with receptors, and effects on cellular behavior. Moreover, these studies may lead to advances in regenerative medicine and targeted therapies aimed at mitigating the adverse effects associated with its dysregulation. Overall, the research on recombinant FGF3 protein is at the intersection of developmental biology and therapeutic innovation, highlighting its significant potential in both understanding fundamental biological processes and developing new treatment strategies for FGF3-related disorders.
