The human recombinant FGF17 protein, tagged with a polyhistidine (His) tag, is typically expressed in E. coli cells . The His tag facilitates purification and detection of the protein. The recombinant protein contains amino acids 23 to 216 of the native FGF17 sequence, with a calculated molecular weight of approximately 24.5 kDa . When analyzed under non-reducing conditions using SDS-PAGE, the protein migrates as a 28-30 kDa band .
The recombinant FGF17 protein is highly purified, with a purity greater than 95% as determined by SDS-PAGE and greater than 90% as determined by size-exclusion chromatography (SEC-HPLC) . The endotoxin level is less than 0.1 EU per microgram, ensuring minimal contamination . Additionally, the protein is tested for host cell protein and DNA contamination, with levels below 0.5 ng/µg and 0.02 ng/µg, respectively .
FGF17 is known to stimulate the proliferation of NIH-3T3 cells, with an EC50 value ranging from 1.495 to 1.639 µg/mL . This bioactivity is crucial for its role in various cellular processes and developmental stages. FGF17, along with FGF8, is a key factor in the patterning of the mid-hindbrain region during cerebellar development .
Recombinant FGF17 protein is widely used in research to study its role in cellular processes and development. It is also used in various assays to investigate its interactions with other proteins and receptors. The His tag allows for easy purification and detection, making it a valuable tool in biochemical and cell biology research .
For long-term storage, the lyophilized FGF17 protein should be kept at -20°C or lower to maintain its stability . After reconstitution, the protein can be stored at -70°C for up to three months under sterile conditions . It is important to avoid repeated freeze-thaw cycles to preserve the protein’s integrity .