Analytical Data
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Gene name
FGF5
- Application
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Alternative Names
FGF5；Fibroblast growth factor 5
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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
P12034
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Expression Region
18-268aa
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AA Sequence
MAWAHGEKRLAPKGQPGPAATDRNPIGSSSRQSSSSAMSSSSASSSPAAS LGSQGSGLEQSSFQWSPSGRRTGSLYCRVGIGFHLQIYPDGKVNGSHEAN MLSVLEIFAVSQGIVGIRGVFSNKFLAMSKKGKLHASAKFTDDCKFRERF QENSYNTYASAIHRTEKTGREWYVALNKRGKAKRGCSPRVKPQHISTHFL PRFKQSEQPELSFTVTVPEKKNPPSPIKSKIPLSAPRKNTNSVKYRLKFR FG
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Molecular Weight
28 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 5 (FGF5) is a crucial protein involved in various biological processes, including cell proliferation, differentiation, and angiogenesis. It is part of the fibroblast growth factor (FGF) family, which plays a significant role in developmental processes and tissue homeostasis. Research into FGF5 has garnered attention due to its implications in hair follicle cycling, with overexpression linked to hair loss disorders and other dermatological conditions. Additionally, FGF5's function in modulating epithelial-mesenchymal interactions highlights its potential in cancer biology, particularly in tumor growth and metastasis. The study of recombinant FGF5 proteins has opened new avenues for therapeutic applications, especially in regenerative medicine and tissue engineering. By harnessing the properties of FGF5, researchers aim to develop innovative strategies for promoting wound healing and tissue repair. Furthermore, understanding FGF5’s molecular mechanisms can facilitate the design of targeted therapies for conditions linked to its dysregulation. As such, recombinant FGF5 proteins serve as valuable tools in both basic research and clinical applications, prompting ongoing studies to elucidate their full therapeutic potential.
