Analytical Data
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Gene name
FGF-6
- Application
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Alternative Names
HBGF6; HST2; HST2 Oncogene; Heparin Secretory-Transforming Protein 2; Heparin-Binding Growth Factor 6
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Species
Zebrafish
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Source
E. coli
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Tag
N-His
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Purity
Greater than 97% as determined by SDS-PAGE.
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Uniprot
Q5TLE1
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Expression Region
Arg85~Ile209
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Protein Length
Partial
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Molecular Weight
18kDa
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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 6 (FGF-6) is a member of the fibroblast growth factor family, known for its role in various biological processes such as cell proliferation, differentiation, and survival. Initially identified for its involvement in muscle development and repair, FGF-6 has garnered attention in regenerative medicine and tissue engineering. Research has shown that FGF-6 plays a crucial role in myogenesis, where it promotes the proliferation and differentiation of myoblasts, making it a potential therapeutic target for muscle degenerative diseases. Additionally, FGF-6's role in angiogenesis and wound healing has sparked interest in its application for enhancing tissue regeneration. The recombinant protein form of FGF-6 allows for detailed studies of its biological functions and mechanisms. Furthermore, engineers and biologists are exploring its potential in drug delivery systems and biomaterial scaffolds to improve healing processes. Despite these advancements, the precise signaling pathways and molecular mechanisms through which FGF-6 exerts its effects remain to be fully elucidated, prompting ongoing investigations into its biological activities and therapeutic potentials. Understanding FGF-6's interactions and functions will not only advance our knowledge of muscle biology but may also lead to innovative treatments for a variety of conditions linked to tissue damage and regeneration. Thus, the study of recombinant FGF-6 represents a significant field of inquiry with promising prospects for future therapeutic applications.
