EPCAM Human, sf9

Epithelial Cell Adhesion Molecule (EpCAM), also known as CD326, is a transmembrane glycoprotein that plays a crucial role in cell-cell adhesion within epithelial tissues. It is involved in various cellular processes, including signaling, migration, proliferation, and differentiation . EpCAM is particularly significant in the context of cancer research due to its overexpression in many epithelial cancers .

EpCAM is a transmembrane protein that mediates calcium-independent homotypic cell-cell adhesion in epithelial tissues . It is composed of an extracellular domain, a single transmembrane domain, and a short cytoplasmic tail. The extracellular domain is responsible for the adhesion properties, while the cytoplasmic tail is involved in intracellular signaling pathways .

EpCAM is known to upregulate oncogenes such as c-myc and cyclins A and E, contributing to its role in tumorigenesis . Additionally, it has been found to inhibit cathepsin-L (CTSL), a cysteine protease that promotes tumor cell invasion and metastasis . This inhibition is mediated by the thyroglobulin type-1 (TY-1) domain present in EpCAM .

Recombinant EpCAM (Human, Sf9) refers to the human EpCAM protein that has been produced using the Sf9 insect cell expression system. The Sf9 cell line, derived from the fall armyworm (Spodoptera frugiperda), is commonly used for the production of recombinant proteins due to its high expression levels and ability to perform post-translational modifications similar to those in mammalian cells .

The recombinant EpCAM produced in Sf9 cells retains the functional properties of the native protein, making it a valuable tool for research and therapeutic applications. It is used in various studies to understand the role of EpCAM in cancer biology and to develop potential therapeutic strategies targeting EpCAM .

EpCAM is highly overexpressed in many epithelial cancers, including colorectal, breast, gastric, prostate, ovarian, and lung cancers . Its overexpression is associated with poor prognosis and increased tumor aggressiveness. As a result, EpCAM is used as a diagnostic marker for these cancers and as a potential target for immunotherapeutic strategies .

Recent studies have revealed that cancer-associated mutations in EpCAM can affect its function and localization. For example, mutations that prevent EpCAM from being expressed on the cell surface can abrogate its ability to inhibit CTSL activity and tumor cell invasion . These findings highlight the importance of EpCAM in cancer progression and its potential as a therapeutic target.