Analytical Data
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Gene name
FGF9
- Application
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Alternative Names
FGF9；Fibroblast growth factor 9
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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
P31371
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Expression Region
3-208aa
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AA Sequence
MPLGEVGNYFGVQDAVPFGNVPVLPVDSPVLLSDHLGQSEAGGLPRGPAV TDLDHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIA VGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSN LYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPDKVPELY KDILSQS
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Molecular Weight
23 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
FGF9 (Fibroblast Growth Factor 9) is a member of the fibroblast growth factor family, which plays a crucial role in various biological processes, including cell proliferation, differentiation, and survival. Research on FGF9 has gained significance due to its involvement in developmental biology and pathological conditions, such as cancer and tissue regeneration. It is particularly notable for its role in the development of the male reproductive system and its potential implications in promoting neural regeneration and repairing damaged tissues. The study of recombinant FGF9 proteins has become a focus for researchers aiming to explore therapeutic applications, especially in tissue engineering and regenerative medicine. By producing FGF9 in a recombinant form, scientists can investigate its signaling pathways, biological functions, and interactions with other cellular factors, which may provide insights into developing new treatment strategies for diseases associated with impaired cell growth and differentiation. Moreover, understanding the structure-function relationships of FGF9 can aid in eluding its therapeutic potential and optimizing its application in clinical settings. As a result, recombinant FGF9 not only serves as a vital tool for fundamental research but also holds promise for translational advancements in regenerative therapies.
