Est 2011
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New Kit to Enhance Flourescence-Labelling Assays

New Kit to Enhance Flourescence-Labelling Assays

Background

Fluorescence labelling assays are frequently used for a diverse range of applications. These assays are often disadvantaged by fluorescence quenching, which dramatically reduces the fluorescent signal intensity. This fluorescence quenching is frequently caused by the biological matrix of the sample. We have developed a technology that enables the accurate quantification of binding sites per cell and that boosts the fluorescent signal several-fold.

Application

To determine the concentration of any fluorescently-labelled protein(s) or small molecules in cells and a wide range of biological samples.

 

TECHNOLOGY:

  • The kit is a two-reagent system, with ready-to-use formulations. • The first solution contains a proprietary un-quenching reagent that rapidly amplifies the fluorescent signal.
  • The second solution contains a read buffer that enables accurate quantification of the fluorescent signal.
  • The kit also contains a fluorescent standard to enable the concentration of fluorescently-labelled protein to be determined, via serial dilution.

 

EXAMPLES OF APPLICATIONS:

  1. Perform ligand binding assays. Radioligand binding studies have been the gold standard for quantifying cell surface receptors since 1970. Binding studies can be performed using the kit and the number of binding sites per sample may be accurately quantified, with enhanced sensitivity.
  2. Determination of intracellular protein. The fluorescent signal emitted by fluorescently-labelled proteins delivered to cells is frequently strongly quenched. This kit enables the signal to be completely un-quenched and the concentration of fluorescently-labelled protein to be accurately determined.
  3. Determine of specific protein content in blood samples. The fluorescent signal emitted by fluorescently-labelled proteins in biological fluids is frequently strongly quenched. This kit enables the concentration of specific fluorescently-labelled proteins to be accurately determined.

Institution:

Maynooth University

 

Commercial Contact:

Katrina Bradley

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