Epidermal Growth Factor (EGF), also known as urogastrone, is an endogenous peptide growth factor primarily involved in cell growth, proliferation, and differentiation. It was initially isolated from the submandibular glands of mice and is also present in human tissues, including urine, salivary glands, and blood platelets. EGF belongs to the class of growth factors and plays a crucial role in various physiological processes. Researchers have found that EGF stimulates the growth of a variety of tissues and is a potent inhibitor of gastric acid secretion, suggesting its dual role in growth stimulation and digestive regulation. It is implicated in oncogenic transformation, where its pathways are often hijacked by cancer cells to promote tumor growth. EGF acts by binding to the epidermal growth factor receptor (EGFR), a receptor tyrosine kinase. This binding triggers a cascade of intracellular signaling pathways, including the MAPK, PI3K/Akt, and JAK/STAT pathways, leading to cellular proliferation and survival. Mutations in EGFR are associated with various cancers, making it a target for cancer therapies. Pharmacokinetic properties of EGF are not well-documented, with limited data on its half-life and metabolism. It is known to be rapidly cleared from circulation, primarily through renal filtration. EGF's clinical use is primarily in research settings, with therapeutic applications being explored in wound healing and cancer treatment. It is not widely approved for clinical use, and its regulatory status varies by region, with ongoing research into its potential therapeutic benefits.