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The LANCE® Ultra Human Frataxin Detection Kit is designed for detection and quantitation of human frataxin 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.
Frataxin is expressed as a 210 AA, 23 kDA protein from the FXN gene located on chromosome 9. Upon expression, the FXN protein is directed to the mitochondrion by its 41 AA N-terminal mitochondrial targeting sequence. In the mitochondrion, the protein is cleaved by the mitochondrial processing peptidase (MPP) to its intermediate form of 42 – 210 AA. Later on, MPP cleaves the protein to its mature form of 81-210 AA. Although the function of the FXN protein is not clearly defined, it is thought to be vitally important for Iron-Sulfur cluster biogenesis, heme biosynthesis, and chelation and transportation of iron specifically involved with the mitochondria. The Frataxin protein is the primary culprit for a debilitating neurodegenerative disease called Friedreich’s Ataxia. Due to similarities in the diseases, there is some evidence to suggest that FXN may be involved in other neurodegenerative diseases such as Parkinson’s, Multiple Sclerosis, and Amyotrophic Lateral Sclerosis. This kit has been designed for the detection and quantification of FXN from cell and tissue lysates.
|Assay Target Class||Protein|
|Detection Method||Time-Resolved Fluorescence (TRF), TR-FRET|
|Experimental Type||In vitro|
|Product Brand Name||LANCE Ultra|
|Shipping Condition||Blue Ice|
|Unit Size||10,000 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.