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Epithelial Cadherin (E-Cadherin), also known as Cadherin-1 or Uvomorulin (in mouse and rat) is a single-pass transmembrane protein that facilitates calcium dependent cell adhesion. A member of the Cadherin family, E-Cadherin utilizes five extracellular EC domains to form cis-clusters between adjacent epithelial cells and trans-clusters within the same cell. Cleavage of the N-terminal domain by a number of proteases is critical for cell motility and EGFR-dependent survival. The intracellular domain of E-cadherin interacts with many proteins including β-catenin, α-catenin, vinculin, and plakoglobin. Lack of binding to any of these proteins has been indicated in cancer metastasis.
AlphaLISA technology allows the detection of molecules of interest in a no-wash, highly sensitive, quantitative assay. In an AlphaLISA assay, a biotinylated anti-analyte antibody binds to the Streptavidin-coated Donor beads while another anti-analyte antibody is conjugated to AlphaLISA Acceptor beads. In the presence of the analyte, the beads come into close proximity. The excitation of the Donor beads causes the release of singlet oxygen molecules that triggers a cascade of energy transfer in the Acceptor beads, resulting in a sharp peak of light emission at 615 nm.
|Assay Target Class||Protein|
|Experimental Type||In vitro|
|Product Brand Name||AlphaLISA|
|Shipping Condition||Blue Ice|
|Unit Size||100 assay points|
The introduction of enzyme-linked immunosorbent assays (ELISAs) in the early 1970’s offered researchers a non-radiometric immunoassay platform without compromising sensitivity. Over the last 50 years scientists have made huge strides in disease research and drug discovery and a demand for greater assay throughput and sensitivity has evolved. In response, more robust immunoassays have been developed to address some of the limitations of the standard, colorimetric ELISA.
Find out about the most common limitations of traditional ELISAs and how different ELISA alternative technologies address these limitations.