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trFluor™ Eu donkey anti-goat IgG (H+L)
Cross Adsorbed
Many biological compounds present in cells, serum or other biological fluids are naturally fluorescent, and thus the use of conventional, prompt fluorophores leads to serious limitations in assay sensitivity due to the high background caused by the autofluorescence of the biological molecules to be assayed. The use of long-lived fluorophores combined with time-resolved detection (a delay between excitation and emission detection) minimizes prompt fluorescence interferences. Our trFluor™ Eu probes enable time-resolved fluorometry (TRF) for the assays that require high sensitivity. trFluor™ Eu probes have large Stokes shifts and extremely long emission half-lives when compared to more traditional fluorophores such as Alexa Fluor or cyanine dyes. Compared to the other TRF compounds, our trFluor™ Eu probes have relatively high stability, high emission yield and ability to be linked to biomolecules. This trFluor™ Eu donkey anti-goat IgG (H+L) conjugate is commonly used as a second step reagent for indirect immunofluorescent staining, when used in conjunction with primary antibodies.
Time-resolved fluorescence energy transfer&nbsp;(TR-FRET) is the practical combination of&nbsp;time-resolved fluorometry (TRF)&nbsp;combined with&nbsp;F&ouml;rster resonance energy transfer&nbsp;(FRET) that offers a powerful tool for drug discovery researchers. TR-FRET combines the low&nbsp;background&nbsp;aspect of TRF with the&nbsp;homogeneous assay&nbsp;format of FRET. The resulting assay provides an increase in flexibility, reliability and sensitivity in addition to higher throughput and fewer false positive/false negative results. FRET involves two&nbsp;fluorophores, a donor (such as trFluor Eu and trFluor Tb) and an acceptor.&nbsp;Excitation of the donor by an energy source (e.g. flash lamp or laser) produces an energy transfer to the acceptor if the two are within a given proximity to each other. The acceptor in turn emits light at its characteristic wavelength. The FRET aspect of the technology is driven by several factors, including spectral overlap and the proximity of the fluorophores involved, wherein energy transfer occurs only when the distance between the donor and the acceptor is small enough. In practice, FRET systems are characterized by the&nbsp;F&ouml;rster's radius&nbsp;(R<sub>0</sub>): the distance between the fluorophores at which FRET efficiency is 50%. For many FRET parings, R<sub>0</sub>&nbsp;lies between 20 and 90 &Aring;, depending on the acceptor used and the spatial arrangements of the fluorophores within the assay.&nbsp;Through measurement of this energy transfer, interactions between&nbsp;biomolecules&nbsp;can be assessed by coupling each partner with a fluorescent label and detecting the level of energy transfer. Acceptor emission as a measure of energy transfer can be detected without needing to separate bound from unbound assay components (e.g. a filtration or wash step) resulting in reduced assay time and cost.
Time-resolved fluorescence energy transfer&nbsp;(TR-FRET) is the practical combination of&nbsp;time-resolved fluorometry (TRF)&nbsp;combined with&nbsp;F&ouml;rster resonance energy transfer&nbsp;(FRET) that offers a powerful tool for drug discovery researchers. TR-FRET combines the low&nbsp;background&nbsp;aspect of TRF with the&nbsp;homogeneous assay&nbsp;format of FRET. The resulting assay provides an increase in flexibility, reliability and sensitivity in addition to higher throughput and fewer false positive/false negative results. FRET involves two&nbsp;fluorophores, a donor (such as trFluor Eu and trFluor Tb) and an acceptor.&nbsp;Excitation of the donor by an energy source (e.g. flash lamp or laser) produces an energy transfer to the acceptor if the two are within a given proximity to each other. The acceptor in turn emits light at its characteristic wavelength. The FRET aspect of the technology is driven by several factors, including spectral overlap and the proximity of the fluorophores involved, wherein energy transfer occurs only when the distance between the donor and the acceptor is small enough. In practice, FRET systems are characterized by the&nbsp;F&ouml;rster's radius&nbsp;(R<sub>0</sub>): the distance between the fluorophores at which FRET efficiency is 50%. For many FRET parings, R<sub>0</sub>&nbsp;lies between 20 and 90 &Aring;, depending on the acceptor used and the spatial arrangements of the fluorophores within the assay.&nbsp;Through measurement of this energy transfer, interactions between&nbsp;biomolecules&nbsp;can be assessed by coupling each partner with a fluorescent label and detecting the level of energy transfer. Acceptor emission as a measure of energy transfer can be detected without needing to separate bound from unbound assay components (e.g. a filtration or wash step) resulting in reduced assay time and cost.
protocol
Protocol
sds
SDS
COA
CatalogSize
Price
Quantity
6200050 ug
Price
 
Physical properties
Molecular weight~150000
SolventWater
Spectral properties
Correction factor (260 nm)0.911
Correction factor (280 nm)0.777
Extinction coefficient (cm -1 M -1)
21000
Excitation (nm)298
Emission (nm)617
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12171501
Documents
Protocol
Safety Data Sheet
Certificate of Analysis
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Page updated on October 28, 2025