Analytical Data
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Gene name
FGF10
- Application
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Alternative Names
FGF10;Fibroblast growth factor 10
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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
O15520
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Expression Region
40-208aa
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AA Sequence
MLGQDMVSPEATNSSSSSFSSPSSAGRHVRSYNHLQGDVRWRKLFSFTKY FLKIEKNGKVSGTKKENCPYSILEITSVEIGVVAVKAINSNYYLAMNKKG KLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRR GQKTRRKNTSAHFLPMVVHS
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Molecular Weight
19 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 10 (FGF10) is a member of the fibroblast growth factor family, which plays a crucial role in various biological processes, including embryonic development, tissue repair, and the regulation of cell proliferation and differentiation. Research on FGF10 has garnered significant interest due to its involvement in the formation and maintenance of multiple organ systems, particularly the lungs, pancreas, and salivary glands. Disruptions in FGF10 signaling pathways have been implicated in a variety of pathologies, such as congenital disorders, cancer, and pulmonary diseases. The recombinant form of FGF10 has been explored for its therapeutic potential, especially in regenerative medicine and tissue engineering, where it may promote wound healing and enhance tissue regeneration through its angiogenic properties. Furthermore, studies have demonstrated that FGF10 can induce the proliferation of epithelial cells and the formation of new structures, making it a promising candidate for treating conditions related to tissue damage. By producing FGF10 as a recombinant protein, researchers aim to elucidate its biological functions and develop novel therapeutic strategies, thus advancing our understanding of its roles in both health and disease. Continuous investigations into the mechanisms of action and potential clinical applications of FGF10 hold the promise of significant breakthroughs in regenerative therapies and targeted treatment approaches.
