Recombinant Human Fibroblast Growth Factor 8 (FGF8) is produced in an E. coli expression system and spans the full mature protein length of Isoform FGF-8B, specifically amino acids 23-215. This tag-free protein shows a purity level exceeding 95%, as verified by SDS-PAGE analysis. The protein demonstrates biological activity with an ED50 of 21.87 ng/ml in a cell proliferation assay using BALB/c 3T3 cells. Endotoxin levels remain below 1.0 EU/µg, determined by the LAL method.
Fibroblast Growth Factor 8 (FGF8) belongs to the fibroblast growth factor family and appears to play a critical role in embryonic development and cell growth. It participates in several signaling pathways that influence cell division, differentiation, and survival. FGF8's research value likely stems from its involvement in various developmental processes, which makes it a useful tool for studying cellular growth mechanisms and developmental biology.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Cell Proliferation and Growth Factor Signaling Studies
This recombinant FGF8 protein can be applied to investigate fibroblast growth factor signaling pathways in various cell culture systems. The confirmed biological activity with an ED50 of 21.87 ng/ml in BALB/c 3T3 cells offers a reliable reference point for dose-response experiments. Scientists can apply this protein to study downstream signaling cascades, receptor binding kinetics, and cellular responses to FGF8 stimulation in controlled in vitro environments.
2. Developmental Biology Research
FGF8 plays crucial roles in embryonic development, which may make this recombinant protein valuable for studying developmental processes in model systems. The protein can be added to organoid cultures, tissue explants, or primary cell cultures to investigate morphogenetic processes and cell fate determination. High purity (>95%) and low endotoxin levels suggest it should work well for sensitive developmental assays where contamination could muddy the results.
3. Receptor Binding and Interaction Studies
The tag-free nature of this recombinant FGF8 makes it potentially ideal for studying protein-protein interactions and receptor binding without interference from fusion tags. Scientists can use this protein in surface plasmon resonance, isothermal titration calorimetry, or other biophysical techniques to characterize FGF receptor binding affinities and kinetics. It may also work in competitive binding assays to evaluate the specificity of FGF8-receptor interactions.
4. Antibody Development and Validation
This highly pure recombinant FGF8 protein serves as a promising antigen for generating and validating antibodies against human FGF8. The protein can be used for immunizing animals, screening hybridomas, and validating antibody specificity through ELISA, Western blotting, or immunoprecipitation assays. The confirmed biological activity suggests that antibodies developed against this protein should recognize the native, functional form of FGF8.
5. Biochemical Characterization and Protein Stability Studies
Scientists can apply the recombinant FGF8 protein for comprehensive biochemical analyses including protein folding studies, thermal stability assessments, and structure-function relationship investigations. Researchers can examine the protein's behavior under various buffer conditions, pH ranges, and temperatures to optimize storage and experimental conditions. The high purity level should allow for accurate spectroscopic and analytical measurements for detailed protein characterization.
