EGF (Leu 21) Human

Epidermal Growth Factor (Leu-21) (Human Recombinant) is a single, non-glycosylated polypeptide chain consisting of 53 amino acids. It has a molecular mass of approximately 6205 Daltons . The sequence of the first five N-terminal amino acids is Asn-Ser-Asp-Ser-Glu . This specific variant is known for its high purity, often exceeding 98%, as determined by reverse-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) .

EGF (Leu-21) is a potent mitogenic factor, meaning it stimulates cell division. It has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin . The biological activity of this recombinant protein is measured by its ability to induce the proliferation of MDCK cells, with an effective dose (ED50) of less than 10 ng/ml .

The recombinant EGF (Leu-21) is typically produced in Escherichia coli and purified using proprietary chromatographic techniques . The protein is lyophilized (freeze-dried) to ensure stability and is recommended to be reconstituted in sterile water at a concentration of not less than 100 µg/ml . Once reconstituted, it should be stored at 4°C for short-term use (2-7 days) and below -18°C for long-term storage . It is important to avoid repeated freeze-thaw cycles to maintain its stability and activity .

The therapeutic potential of EGF (Leu-21) lies in its ability to stimulate the growth of various epidermal and epithelial tissues, both in vivo and in vitro . This makes it a promising candidate for applications in wound healing, tissue regeneration, and potentially in the treatment of certain cancers. The specific signaling pathways and cellular responses triggered by this EGF variant are subjects of ongoing research, aiming to uncover novel therapeutic avenues .