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There are five classes of mammalian immunoglobulins: IgA, IgD, IgE, IgM, and IgG. IgG is the most abundant immunoglobulin and is equally distributed in blood and tissue. The general immunoglobulin structure is composed of four polypeptide chains, two heavy and two light chains linked together and to each other by disulfide bonds, creating a tetrameric quaternary structure. IgE has two main immune functions, it is the main driver in the immune resonse to parasites and it also is the main cause of allergic reactions. IgE is typically the least abundant immunoglobulin in serum but is capable of triggering the most powerful inflammation reations of all the isotypes. Typically mouse serum and plasma samples contain less than 75 ng/mL of IgE.
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||Antibody|
|Experimental Type||In vitro|
|Product Brand Name||AlphaLISA|
|Shipping Condition||Blue Ice|
|Unit Size||500 assay points|