EGF Human
Greater than 98.0% as determined by SDS-PAGE.
Description
Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.
Product Specs
Recombinant Human Epidermal Growth Factor, generated using E.Coli as an expression system, is a single-chain polypeptide that lacks glycosylation. It consists of 53 amino acids, resulting in a molecular weight of 6.2kDa. The purification of EGF is achieved through specialized chromatographic methods.
The lyophilization of EGF was carried out from a solution containing PBS at a pH of 7.4, with an EGF concentration of 1mg/ml.
The purity of the Epidermal Growth Factor is determined to be greater than 98.0% based on SDS-PAGE analysis.
The ED50, determined using a cell proliferation assay with murine Balb/c 3T3 cells, is found to be less than 0.1 ng/ml. This corresponds to a specific activity greater than 1.0x107 IU/mg.
Product Science Overview
EGF was first discovered by Stanley Cohen and Rita Levi-Montalcini in the 1950s while they were conducting experiments on nerve growth factor at Washington University in St. Louis . Initially, human EGF was known as urogastrone due to its ability to inhibit gastric acid secretion . The discovery of EGF earned Stanley Cohen the Nobel Prize in Physiology or Medicine in 1986.
Human EGF is a protein consisting of 53 amino acids with a molecular weight of approximately 6 kDa . It contains three intramolecular disulfide bonds that are crucial for its structural stability . The primary function of EGF is to bind to the EGFR on the cell surface, which triggers a cascade of downstream signaling pathways leading to various cellular responses, including proliferation, differentiation, and survival .
The recombinant production of human EGF involves cloning the human EGF gene into a suitable expression vector, which is then introduced into a host organism, typically Escherichia coli (E. coli) . The host organism expresses the EGF protein, which is subsequently purified and used for various applications. Recombinant EGF is widely used in cell culture, wound healing, and as a therapeutic agent in certain medical conditions .
Recombinant EGF has several applications in both research and medicine. In research, it is used to study cell signaling pathways and to culture cells that require EGF for growth and proliferation . In medicine, recombinant EGF is used to promote wound healing and tissue regeneration. It has been shown to accelerate the healing of chronic wounds, such as diabetic ulcers, and to improve the outcomes of skin grafts and other surgical procedures .
