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Dyes for Your Near-Infrared Imaging Needs
Product Ordering Information
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Dye Structure
IRDye® 800RS Infrared Dye
IRDye 800RS is an excellent choice for nucleic acid applications.
NHS ester reactive group for labeling primary and secondary amino groups
Labeled nucleic acids easily purified by reverse-phase chromatography
Good water solubility, but low salt tolerance
More hydrophobic than IRDye 800CW
Useful for self-quenching protease assays
IRDye 800RS is not recommended for most protein applications, because of its potential for self-quenching
| Solvent | Ext. Coeff. (M-1cm-1) | Abs Max (nm) | Em Max (nm) | Stokes Shift (nm) |
|---|---|---|---|---|
| Methanol | 300,000 | 770 | 786 | 16 |
| Water | 200,000 | 767 | 786 | 19 |
| 1X PBS | 200,000 | 767 | 786 | 19 |
| PBS: Methanol | 270,000 | 770 | 786 | 16 |
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Dye Structure
IRDye® 800RS for Fluorogenic
Protease Assays
Because IRDye® 800RS will self-quench when dye molecules are close together, fluorogenic protease substrates can be created.
Example:
If casein protein is heavily labeled with IRDye 800RS, the dye becomes self-quenched. When casein is cleaved by a protease, quenching is relieved and fluorescent signal is generated. Labeled casein can be used for general protease assays.
Advantages:
Simple – just mix and read
Sensitivity – near-infrared detection reduces background, light scatter and interference caused by other compounds
Flexible – no stop solution required; easy to monitor reactions over time
Uses less substrate than visible fluorescence kits
Up to 20-fold fluorescence intensity enhancement upon digestion
Can be used for protease inhibitor screening
Self Quenching and Signal Generation
In the heavily labeled substrate, IRDye 800RS fluorophores are self-quenched by interaction of dye molecules that are in close proximity.
After protease cleavage, the fluorophores are separated. Quenching is relieved and fluorescent signal is generated.
[LEFT] IRDye 800RS Casein protease assay. A, B, and C represent replicate samples. Controls: Column 1, buffer only; column 2, trypsin only; column 3, substrate only. Samples (columns 4-12): Two-fold dilution series of trypsin (5 µg/mL - 19.7 ng/mL); substrate concentration is 20 nM.
