E-Cadherin
E-Cadherin (cadherin 1, encoded by CDH1) is a classical cadherin and calcium-dependent cell-cell adhesion glycoprotein. Also known as uvomorulin, CD324 and UVO, it is lost or mutated in several cancers and acts as a bacterial receptor. Browse Assay Genie's current range of E-Cadherin research reagents below, or read on for the biology behind the target.
E-Cadherin is a calcium-dependent cell-cell adhesion protein belonging to the cadherin superfamily. The mature glycoprotein has five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. It is generated from a preproprotein that is proteolytically processed, and alternative splicing of the CDH1 gene produces multiple transcript variants. UniProt records the protein at cell junctions, including adherens junctions and desmosomes, as well as at the cell membrane, endosomes, the trans-Golgi network and the cytoplasm, and also lists a secreted form.
E-Cadherin also has a role in microbial infection. It serves as a receptor for Listeria monocytogenes: the bacterial surface protein internalin A (InlA) binds E-Cadherin and promotes uptake of the bacteria. According to NCBI Gene, the ectodomain mediates bacterial adhesion to mammalian cells, while the cytoplasmic domain is required for internalisation.
HGNC classifies CDH1 (cadherin 1) among the CD molecules and the type I classical cadherins, with CD324 as the CD designation. Earlier names include uvomorulin, UVO and cadherin 1, type 1, E-cadherin (epithelial). The gene sits in a cluster with other cadherin family members on chromosome 16, and mouse and rat each carry a Cdh1 ortholog. Mutations in CDH1 are correlated with gastric, breast, colorectal, thyroid and ovarian cancer. Loss of function is thought to contribute to cancer progression by increasing proliferation, invasion and/or metastasis, which is why E-Cadherin is widely studied as an epithelial adhesion marker.
Loss of E-Cadherin function is thought to promote proliferation, invasion and metastasis, and CDH1 mutations are correlated with several cancer types.
E-Cadherin is a calcium-dependent adhesion protein with five extracellular repeats, making it a core subject in studies of adherens junctions.
E-Cadherin is a receptor for Listeria monocytogenes, with internalin A binding promoting bacterial uptake into cells.
CDH1 mutations are correlated with gastric, breast, colorectal, thyroid and ovarian cancer, supporting its study across epithelial tumours.
E-Cadherin is a calcium-dependent cell-cell adhesion glycoprotein of the classical cadherin group. It localises to adherens junctions and other cell junctions. It also acts as a receptor for Listeria monocytogenes, which binds it through internalin A to enter cells.
The gene symbol is CDH1, and the protein is also called cadherin-1, uvomorulin, CD324 and UVO. An earlier HGNC name was cadherin 1, type 1, E-cadherin (epithelial). Alternative splicing gives multiple transcript variants, and a preproprotein is processed into the mature glycoprotein.
Mutations in CDH1 are correlated with gastric, breast, colorectal, thyroid and ovarian cancer, and loss of function may increase invasion and metastasis. Mouse and rat both have a Cdh1 ortholog; check the datasheet of any product for its validated reactivity.
Other cadherin family members that share the classical cadherin architecture and adhesion functions.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P12830; product specifications from Assay Genie datasheets.