Human epidermal growth factor (EGF) stimulates cell proliferation and differentiation. It is used extensively in induced-pluripotent stem cell (iPSC) and embryonic stem cell (ESC) culture systems for the successful expansion and differentiation of epithelial, neural, mesoderm and hematopoietic lineages.
Recombinant EGF protein is a key component of many organoid media, along with other stem cell niche factors, R-spondin 1, Noggin or Gremlin, Wnt3a and FGF10. In addition, recombinant EGF is used for establishing and maintaining intestine, stomach, liver, pancreas, brain and cancer organoids.
Members of the human epidermal growth factor family are synthesized as type I transmembrane precursor proteins, often containing several EGF domains in the extracellular region. Proteolysis yields mature proteins that are released from the cell surface1. The mature form of human EGF protein comprises 53 amino acids2. Epidermal growth factor binds to high-affinity EGF receptors (EGFRs) and promotes receptor dimerization and clustering leading to activation of downstream signalling pathways, including PI3K, ERK1/2, JAK/STAT, β-catenin, and calcium signalling3.