HBEGF (E5L5T) Rabbit mAb #27450

Heparin-binding EGF-like growth factor (HBEGF), also known as HB-EGF, belongs to the epidermal growth factor (EGF) family (1). The newly synthesized proHBEGF (about 27 kDa) has an N-terminal prodomain, a heparin-binding EGF domain, and a C-terminal transmembrane fragment (CTF). The heparin-binding region of HBEGF interacts with heparin residues in the extracellular matrix (ECM) and anchors the protein in the ECM. The proHBEGF is activated by the extracellular ADAM and MMP metalloproteases, shedding off its N-terminal prodomain and/or CTF, resulting in a 14-22 kDa product depending on different proteolytic processes. The mature HBEGF acts as a ligand for EGFR or ErbB4 receptors to activate downstream signaling pathways (2,3). The remaining membrane bound CTF is further internalized and binds to Bcl6 to regulate the related nuclear function (3). HBEGF has been shown to be involved in many physiological processes, such as placenta formation (4), heart development and function (5), and hematopoietic cell proliferation (6). The growth factor plays important roles in tissue inflammation, wound healing, and cancer development. Therefore, HBEGF is proposed as a therapeutic target in related diseases (7-10).