Epidermal Growth Factor (EGF) is a protein that plays a crucial role in cell growth, proliferation, and differentiation by binding to its receptor, EGFR . The mouse recombinant version of EGF, often biotinylated for various applications, is a significant tool in biological research and biotechnology.
EGF was first identified as a secreted peptide in the submaxillary glands of mice and in human urine . The protein consists of 53 amino acid residues and features three intramolecular disulfide bonds, which are essential for its biological activity . The recombinant version of mouse EGF is produced using E. coli expression systems, ensuring high purity and biological activity .
EGF is a potent growth factor capable of inducing cell proliferation, differentiation, and survival . It stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro, as well as some fibroblasts in cell culture . EGF’s ability to promote cell division and differentiation makes it a valuable component in cell culture media and differentiation studies .
Recombinant mouse EGF, particularly in its biotinylated form, is widely used in research and biotechnology. It is optimized for use in cell culture, differentiation studies, and functional assays . The biotinylation of EGF allows for easy detection and quantification in various assays, enhancing its utility in research applications.
The production of recombinant mouse EGF involves expression in E. coli, followed by purification to achieve high purity levels (>95%) and low endotoxin levels (<0.10 EU per 1 μg of protein) . The biological activity of EGF is tested in appropriate bioassays to ensure its efficacy in stimulating cell proliferation and differentiation .