Analytical Data
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Gene name
FGF11
- Application
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Alternative Names
FHF3; Fibroblast Growth Factor Homologous Factor 3
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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
Q92914
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Expression Region
Leu44~His212
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Protein Length
Partial
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Molecular Weight
23kDa
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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 11 (FGF11), a member of the FGF family, plays a critical role in various biological processes, including neuronal differentiation, cardiac development, and tissue repair. Unlike other FGFs that bind to heparan sulfate proteoglycans, FGF11 functions independently of heparin and is primarily localized in the cytoplasm, where it is involved in intracellular signaling pathways. The significance of FGF11 in both normal physiological functions and pathological conditions, such as neurodegenerative diseases and heart failure, has prompted extensive research into its mechanisms of action. Recombinant FGF11 proteins have been produced to better understand its biological functions, as well as to explore its potential therapeutic applications. The study of these recombinant proteins offers insights into the protein's structure-function relationships and interaction with cellular receptors. By elucidating the signaling pathways modulated by FGF11, researchers aim to harness its potential in regenerative medicine and therapeutic development for various conditions. Furthermore, the investigation of FGF11 may uncover novel strategies for tissue engineering and enhance the understanding of growth factor signaling in development and disease.
