FGF 8 Mouse, 194 a.a.

The mouse recombinant FGF8 is a non-glycosylated polypeptide chain consisting of 194 amino acids, with a total molecular mass of approximately 22.5 kDa . It is produced in Escherichia coli (E. coli) and is typically available as a sterile, lyophilized (freeze-dried) powder .

FGF8 plays a crucial role in several developmental processes:

• Embryonic Development: It functions as an embryonic epithelial factor and is involved in midbrain and limb development, organogenesis, embryo gastrulation, and left-right axis determination .
• Tumor Growth and Angiogenesis: FGF8 supports androgen and anchorage-independent growth of mammary tumor cells. Overexpression of FGF8 has been linked to increased tumor growth and angiogenesis .
• Adult Expression: In adults, the expression of the FGF8 gene is primarily restricted to the testes and ovaries .

• Formulation: The lyophilized form of FGF8 is typically reconstituted in sterile water to a concentration of at least 100 µg/ml, which can then be further diluted for various applications .
• Stability: While stable at room temperature for up to three weeks, it is recommended to store the lyophilized form below -18°C. Once reconstituted, it should be stored at 4°C for short-term use (2-7 days) and below -18°C for long-term storage . To prevent degradation, it is advisable to add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) and avoid freeze-thaw cycles .
• Purity: The recombinant FGF8 is typically greater than 97% pure, as determined by SDS-PAGE analysis .

FGF8 is widely used in laboratory research for its ability to induce proliferation in various cell types. For instance, it has been shown to induce proliferation of mouse 3T3 cells at concentrations as low as 20 ng/ml, corresponding to a specific activity of 50,000 units/mg .

FGF8 is intended for laboratory research use only and should not be used as a drug, agricultural or pesticidal product, food additive, or household chemical .