Epiregulin (EREG) is a member of the epidermal growth factor (EGF) family, which plays a crucial role in various cellular processes, including proliferation, differentiation, and survival. Epiregulin functions as a ligand for the epidermal growth factor receptor (EGFR) and other members of the ERBB family of tyrosine-kinase receptors .
Human recombinant epiregulin is typically produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain. The recombinant protein contains 69 amino acids (63-108 a.a) and has a molecular mass of approximately 7.7 kDa . It is fused to a 23 amino acid His-tag at the N-terminus, which facilitates purification using chromatographic techniques .
The recombinant epiregulin is provided as a sterile, filtered, colorless solution. It is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0) and 10% glycerol . The protein solution is stable when stored at 4°C for short-term use (2-4 weeks) and at -20°C for long-term storage. To prevent degradation, it is recommended to avoid multiple freeze-thaw cycles and to add a carrier protein (0.1% HSA or BSA) for extended storage .
Epiregulin is expressed in various tissues, including the placenta and peripheral blood leukocytes. It is also found in specific carcinomas of the bladder, lung, kidney, and colon . Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts, and vascular smooth muscle cells. Interestingly, it inhibits the growth of several tumor-derived epithelial cell lines .