EpCAM Rabbit Monoclonal Antibody (Clone 28)

Epithelial cell adhesion molecule (EpCAM) is a transmembrane glycoprotein.¹ It is composed of an extracellular domain (EpEX) that contains an N-domain, a thyroglobulin type-IA domain, and a C-domain, a transmembrane domain, and an intracellular domain (EpIC). EpEX undergoes proteolytic cleavage by disintegrin and metalloproteinase domain-containing protein 17 (ADAM17/TACE) to release soluble EpEX, and γ-secretase cleaves EpCAM at two sites to release a soluble extracellular amyloid-β-like fragment and EpIC. EpCAM is ubiquitously expressed in epithelial tissues but is also found in stem and progenitor cells and tight junctions.^2,3 It is involved in cell adhesion, transport, polarity, proliferation, and motility and signals through novel PKC (nPKC), Wnt, and embryonic RAS (ERAS)/Akt pathways.² Knockdown of EPCAM decreases proliferation, migration, and invasion of breast cancer cells in vitro.⁴ Epcam^-/- mice develop congenital tufting enteropathy (CTE), a disease characterized by hemorrhagic diarrhea, colon crypt hyperplasia, intestinal tufts, and villous atrophy.⁵ Increased protein levels of EpCAM are frequently found in tumors from patients with diverse cancer types.⁶ Cayman’s EpCAM Rabbit Monoclonal Antibody (Clone 28) can be used for ELISA, ELISA (detection), flow cytometry (FC), immunocytochemistry (ICC), immunofluorescence (IF), immunohistochemistry paraffin (IHC-P), immunoprecipitation (IP), and Western blot (WB) applications. The antibody recognizes EpCAM at 34 kDa from human samples. However, due to glycosylation the antibody may recognize EpCAM at approximately 38-40 kDa.

WARNING This product is not for human or veterinary use.

1. Keller, L., Werner, S., and Pantel, K. Biology and clinical relevance of EpCAM. Cell Stress 3(6), 165-180 (2019).

2. Huang, L., Yang, Y., Yang, F., et al. Functions of EpCAM in physiological processes and diseases (Review). Int. J. Mol. Med. 42(4), 1771-1785 (2018).

3. Ladwein, M., Pape, U.F., Schmidt, D.-S., et al. The cell‒cell adhesion molecule EpCAM interacts directly with the tight junction protein claudin-7. Exp. Cell Res. 309(2), 345-357 (2005).

4. Osta, W.A., Chen, Y., Mikhitarian, K., et al. EpCAM is overexpressed in breast cancer and is a potential target for breast cancer gene therapy. Cancer Res. 64(16), 5818-5824 (2004).

5. Guerra, E., Lattanzio, R., La Sorda, R., et al. mTrop1/Epcam knockout mice develop congenital tufting enteropathy through dysregulation of intestinal E-cadherin/β-catenin. PLoS One 7(11), e49302 (2012).

6. Went, P.T., Lugli, A., Meier, S., et al. Frequent EpCam protein expression in human carcinomas. Hum. Pathol. 35(1), 122-128 (2004).