Fluidic Analytics Launches Rapid Protein Labeling Kit
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Fluidic Analytics Ltd has launched fluidiphore rapid amine 503, a protein labeling kit designed to be time-saving and affordable. Absorbing at 503 nm, the new kit can be used with a multitude of techniques including the company’s Fluidity One-W instrument for protein interaction analysis.
Fluorescent labeling of proteins such as antibodies, DNA and lipids is widely used to investigate and better understand protein structure and function. There are various fluorescent dyes available on the market, most of which require a long labeling process over several hours and a purification step to remove excess dye.
Fluidic Analytics’ fluidiphore labeling kit is extremely rapid, taking just 30 minutes to bind proteins. In addition, the fluidiphore kit uniquely does not require a purification step. This is due to a “triple-lock” against background effects. Firstly, the absorbance of the dye shifts from 612 nm (free) to 503 nm when conjugated, meaning that unbound dye will not fluoresce at the same excitation wavelength. Quantum yield (the ratio of fluorescence emission to absorption) also increases upon conjugation meaning that unbound dye will have a much weaker signal than bound. Thirdly, any unused dye hydrolyses during the labeling process becoming inactive and unable to bind, therefore preventing the shift in absorbance and increase in quantum yield.
In addition, there is also a useful observable color change from blue to red/yellow which confirms that labeling is taking place, giving researchers additional confidence in the process.
The fluidiphore rapid amine 503 labeling kit is suitable for use with Fluidic Analytics’ Fluidity One-W instrument to study proteins such as membrane proteins, multi-protein complexes, and intrinsically disordered proteins. The Fluidity One-W enables researchers to accurately assess on-target protein interactions in solution, even in complex, unpurified backgrounds such as crude lysates or blood plasma. The instrument reports absolute size of bound and unbound species, stoichiometry and the nature of binding can be assessed at the same time as binding affinity, giving a complete picture of binding events.