Epidermal Growth Factor (EGF) is a potent mitogenic factor that plays a crucial role in the regulation of cell growth, proliferation, and differentiation. Initially discovered by Stanley Cohen and Rita Levi-Montalcini, EGF has since been extensively studied for its biological significance and therapeutic potential . The recombinant form of EGF derived from rats (Rat Recombinant EGF) has been widely used in research to understand its molecular attributes and signaling pathways.
Rat Recombinant EGF is a non-glycosylated polypeptide chain consisting of 53 amino acids with a molecular mass of approximately 6.3 kDa . It is produced in Escherichia coli (E. coli) using recombinant DNA technology, which involves inserting the gene encoding EGF into the bacterial cells. The bacteria then express the EGF protein, which is subsequently purified using chromatographic techniques .
EGF exerts its effects by binding to the Epidermal Growth Factor Receptor (EGFR), a receptor tyrosine kinase on the cell surface. This binding triggers a cascade of downstream signaling pathways that promote cell proliferation and differentiation . The biological activity of Rat Recombinant EGF is determined by its ability to stimulate the proliferation of mouse BALB/c 3T3 cells, with an effective dose (ED50) of less than 0.1 ng/mL .
Rat Recombinant EGF has been instrumental in various research applications, including:
Lyophilized Rat Recombinant EGF is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term storage . Upon reconstitution, it should be stored at 4°C for short-term use and below -18°C for long-term use, with the addition of a carrier protein to prevent freeze-thaw cycles .