Analytical Data
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Gene name
FGF15
- Application
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Species
Rat
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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
Q8VI81
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Expression Region
Gly25~Lys218
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Molecular Weight
24kDa
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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 15 (FGF15) is a protein primarily produced in the ileum, playing a crucial role in regulating bile acid homeostasis and glucose metabolism. Its discovery has drawn significant attention due to its potential therapeutic implications in metabolic disorders such as obesity and type 2 diabetes. FGF15 functions as an endocrine signal, influencing various metabolic processes by acting on the liver, where it modulates the expression of genes involved in lipid and glucose metabolism. Research has indicated that FGF15 can promote insulin sensitivity and enhance energy expenditure, making it a promising target for developing novel treatments for metabolic diseases. Moreover, studies have revealed that altered FGF15 levels are associated with metabolic dysfunctions, highlighting its importance in maintaining metabolic health. Given these roles, the recombinant expression and characterization of FGF15 are essential for further investigating its function and therapeutic potential. Understanding the structural and functional dynamics of FGF15 via recombinant protein technology can provide insights into its mechanisms of action, pave the way for the development of FGF15-based therapies, and facilitate the exploration of its interactions with other metabolic signaling pathways. As the prevalence of metabolic disorders continues to rise globally, the development of FGF15-based interventions could offer a promising avenue for improving metabolic health and preventing related complications.
