Analytical Data
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Gene name
FGF-9
- Application
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Alternative Names
Fibroblast growth factor 9; FGF-9; GAF; HBGF-9
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Species
Human
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Source
HEK293
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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
P31371
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Expression Region
L4-S208
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Protein Length
Partial
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Molecular Weight
29-30 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 9 (FGF-9) is a crucial member of the FGF family, known for its significant roles in various biological processes, including embryonic development, tissue repair, and regulation of cell proliferation. Research has highlighted FGF-9’s involvement in neurogenesis, indicating its potential therapeutic implications in neurodegenerative diseases and neurological disorders. Additionally, FGF-9 is implicated in angiogenesis and the regulation of bone and cartilage development, making it a subject of interest in regenerative medicine and orthopedic research. The reconstitution of FGF-9 as a recombinant protein allows for in-depth studies of its biological activity, receptor interactions, and signaling pathways. Understanding the molecular mechanisms of FGF-9 can facilitate the development of novel therapeutic strategies for conditions such as traumatic injuries, degenerative diseases, and cancer. The exploration of FGF-9 functions has prompted investigations into its application in tissue engineering and regenerative therapies, with the aim of enhancing healing processes and improving patient outcomes. As the scientific community delves deeper into the potential of FGF-9, ongoing studies continue to unravel its multifaceted roles, providing a promising avenue for innovative treatments and interventions in various fields of medicine.
