Analytical Data
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Gene name
FGF-4
- Application
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Alternative Names
rHuFGF-4; HBGF-4; HST; HST-1; HSTF1
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08620-1
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Expression Region
A41-L206
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Protein Length
Partial
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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
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Protein Description
Fibroblast Growth Factor 4 (FGF-4) is a crucial member of the fibroblast growth factor family, which plays significant roles in embryonic development, tissue repair, and various physiological processes. Research on FGF-4 has garnered attention due to its involvement in cell proliferation, differentiation, and angiogenesis. Its expression is particularly high during early developmental stages, suggesting a key role in mesodermal and ectodermal patterning. Additionally, FGF-4 has been implicated in tumorigenesis, as abnormally elevated levels are often found in certain cancers. The recombinant protein form of FGF-4 has been developed for both in vitro and in vivo studies, enabling scientists to explore its functional properties and therapeutic potential. Investigations into FGF-4's signaling mechanisms and interactions with specific receptors have revealed insights into its biological activities, which may lead to novel therapeutic strategies for tissue regeneration and cancer treatment. Furthermore, the production of FGF-4 as a recombinant protein facilitates research on its pharmacokinetics and potential use in regenerative medicine, thus highlighting its significance in both basic biological research and clinical applications.
