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The LANCE® Ultra Mouse IgG Detection Kit is designed for detection and quantitation of Mouse IgG in cell culture media using a homogeneous TR-FRET (no-wash steps, no separation steps) assay.
LANCE® and LANCE® (Lanthanide chelate excite) Ultra are our TR-FRET (time-resolved fluorescence resonance energy transfer), homogeneous (no wash) technologies. One antibody of interest is labeled with a donor fluorophore (a LANCE Europium chelate) and the second molecule is labeled with an acceptor fluorophore (ULight™ dye). Upon excitation at 320 or 340 nm, energy can be transferred from the donor Europium chelate to the acceptor fluorophore if sufficiently close for FRET (~10 nm). This results in the emission of light at 665 nm.
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. In mice, the IgG class is further divided into four subclasses: IgG, IgG2a/ IgG2c (strain specific), IgG2b, and IgG3. 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. IgG is involved in response to a foreign antigen. The presence of IgG usually signifies a mature antibody response. IgG has a molecular weight of about 150 kDa, it can bind to many pathogens and also plays an important role in antibody-dependent cell-mediated cytotoxicity. Typically mouse serum and plasma samples contain about 7 to 10 mg/ml of IgG. The present kit permits detection of mouse IgG (i.e. analyte) in different sample matrices, including different cell culture media.
| Assay Target | IgG |
|---|---|
| Assay Target Class | Antibody |
| Automation Compatible | Yes |
| Detection Method | Time-Resolved Fluorescence (TRF), TR-FRET |
| Experimental Type | In vitro |
| Product Brand Name | LANCE Ultra |
| Shipping Condition | Blue Ice |
| Therapeutic Area | Biologics/Bioprocess |
| Unit Size | 500 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.
