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Fig. 1 | Experimental Hematology & Oncology

Fig. 1

From: Understanding the versatile roles and applications of EpCAM in cancers: from bench to bedside

Fig. 1

Schematic illustration of EpCAM structure. The premature EpCAM molecule is comprised of 314 amino acids (AA), including a signal peptide, which is cleaved during maturation. The mature membrane-bound EpCAM protein consists of an extracellular domain (EpEX), a transmembrane domain (TM) and an intracellular domain (EpICD). EpEX contains an N-terminal domain (ND), thyroglobulin-domain (TY) and C-terminal domain (CD), including three N-glycosylation sites. Four cleavage sites (α, β, γ, ε-sites) locate on EpCAM molecule, in which can be cleaved into soluble EpEX, TM and free EpICD. Human EpCAM contains two α-sites for ADAM protases, a β-site for BACE1 cleavage, and γ-secretase mediated cleavage on γ-sites and ε-sites

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