The purity of recombinant hFGF9 was determined by SDS-PAGE of 6 µg reduced (+) and nonreduced (-) recombinant hFGF9 and staining overnight with Coomassie Blue.Learn more about how we get our images
The proliferation of NIH/3T3 cells treated with increasing concentrations of hFGF9 was assessed. After 24 hr treatment, cells were labeled with BrdU for 4 hrs. BrdU incorporation was determined by ELISA and the OD450 was determined.Learn more about how we get our images
Recombinant human FGF9 (hFGF9) Leu4-Ser208 (Accession #NP_31371) was expressed in E.coli at Cell Signaling Technology.
>95% as determined by SDS-PAGE of 6 μg reduced (+) and nonreduced (-) recombinant hFGF9. All lots are greater than 95% pure.
Recombinant hFGF9 has a calculated MW of 23,141 Da. DTT-reduced and nonreduced protein migrates as a 23 kDa polypeptide. The expected amino terminus of recombinant hFGF9 was verified by amino acid sequencing.
The bioactivity of hFGF9 was determined in an NIH/3T3 cell proliferation assay. The ED50 of each lot is between 0.05-0.80 ng/ml.
Less than 0.01 ng endotoxin/1 μg hFGF9.
With carrier: Lyophilized from a 0.22 μm filtered solution of hFGF9 in 20 mM Tris, pH 7.2 containing 20 μg BSA per 1 μg hFGF9. Carrier free: Lyophilized from a 0.22 μm filtered solution of hFGF9 in 20 mM Tris, pH 7.2.
Stable in lyophilized state at 4°C for 1 year after receipt. Sterile stock solutions reconstituted with carrier protein are stable at 4°C for 2 months and at -20°C for 6 months. Avoid repeated freeze-thaw cycles. Maintain sterility. Storage at -20°C should be in a manual defrost freezer.
Fibroblast growth factor (FGF) 9 is a member of the larger FGF family of proteins that play key roles in development, cancer, and metabolism. Binding of FGF9 to its receptor requires interaction with heparin and induces receptor dimerization, subsequent transphosphorylation, and downstream activation of Erk, Akt, and PLCγ pathways (1). FGF9 is important for organ development and bone repair (2-4).
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