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trFluor™ Eu-streptavidin conjugate

Time-resolved fluorescence energy transfer (TR-FRET) is the practical combination of time-resolved fluorometry (TRF) combined with Förster resonance energy transfer (FRET) that offers a powerful tool for drug discovery researchers. TR-FRET combines the low background aspect of TRF with the homogeneous assay 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 fluorophores, a donor (such as trFluor Eu and trFluor Tb) and an acceptor. 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 Förster's radius (R<sub>0</sub>): the distance between the fluorophores at which FRET efficiency is 50%. For many FRET parings, R<sub>0</sub> lies between 20 and 90 Å, depending on the acceptor used and the spatial arrangements of the fluorophores within the assay. Through measurement of this energy transfer, interactions between biomolecules 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 (TR-FRET) is the practical combination of time-resolved fluorometry (TRF) combined with Förster resonance energy transfer (FRET) that offers a powerful tool for drug discovery researchers. TR-FRET combines the low background aspect of TRF with the homogeneous assay 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 fluorophores, a donor (such as trFluor Eu and trFluor Tb) and an acceptor. 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 Förster's radius (R<sub>0</sub>): the distance between the fluorophores at which FRET efficiency is 50%. For many FRET parings, R<sub>0</sub> lies between 20 and 90 Å, depending on the acceptor used and the spatial arrangements of the fluorophores within the assay. Through measurement of this energy transfer, interactions between biomolecules 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.
Ordering information
Price ()
Catalog Number16925
Unit Size
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Additional ordering information
Telephone1-408-733-1055
Fax1-408-733-1304
Emailsales@aatbio.com
InternationalSee distributors
ShippingStandard overnight for United States, inquire for international
Physical properties
Molecular weight52000
SolventWater
Spectral properties
Correction Factor (260 nm)0.911
Correction Factor (280 nm)0.777
Excitation (nm)346
Emission (nm)617
Storage, safety and handling
Certificate of OriginDownload PDF
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12352200
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Show More (43)

OverviewpdfSDSpdfProtocol


Molecular weight
52000
Correction Factor (260 nm)
0.911
Correction Factor (280 nm)
0.777
Excitation (nm)
346
Emission (nm)
617
Streptavidin conjugates are widely used together with a conjugate of biotin for specific detection of a variety of proteins, protein motifs, nucleic acids and other molecules since streptavidin has a very high binding affinity for biotin. This trFluor™ Eu-streptavidin conjugate comprises streptavidin (as the biotin-binding protein) with trFluor™ Eu covalently attached (as the time-resolved red fluorescent europium label). It is commonly used as a second step reagent for indirect immunofluorescent staining, when used in conjunction with biotinylated primary antibodies. It is a very valuable tool for biotin-streptavidin-based biological assays and tests using TR-FRET platform. A variety of the complementary biotinylated reagents are available from numerous commercial vendors.

Calculators


Common stock solution preparation

Table 1. Volume of Water needed to reconstitute specific mass of trFluor™ Eu-streptavidin conjugate to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM1.923 µL9.615 µL19.231 µL96.154 µL192.308 µL
5 mM384.615 nL1.923 µL3.846 µL19.231 µL38.462 µL
10 mM192.308 nL961.538 nL1.923 µL9.615 µL19.231 µL

Molarity calculator

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Spectrum


Open in Advanced Spectrum Viewer
spectrum

Spectral properties

Correction Factor (260 nm)0.911
Correction Factor (280 nm)0.777
Excitation (nm)346
Emission (nm)617

Citations


View all 1 citations: Citation Explorer
Overexpression of MACC1 and the association with hepatocyte growth factor/c-Met in epithelial ovarian cancer
Authors: Li, Hongyu and Zhang, Hui and Zhao, Shujun and Shi, Yun and Yao, Junge and Zhang, Yanyan and Guo, Huanhuan and Liu, Xingsuo
Journal: Oncology letters (2015): 1989--1996

References


View all 47 references: Citation Explorer
A streptavidin paramagnetic-particle based competition assay for the evaluation of the optical selectivity of quadruplex nucleic acid fluorescent probes
Authors: Largy E, Hamon F, Teulade-Fichou MP.
Journal: Methods. (2012)
Biotin-4-fluorescein based fluorescence quenching assay for determination of biotin binding capacity of streptavidin conjugated quantum dots
Authors: Mittal R, Bruchez MP.
Journal: Bioconjug Chem (2011): 362
Iminobiotin binding induces large fluorescent enhancements in avidin and streptavidin fluorescent conjugates and exhibits diverging pH-dependent binding affinities
Authors: Raphael MP, Rappole CA, Kurihara LK, Christodoulides JA, Qadri SN, Byers JM.
Journal: J Fluoresc (2011): 647
Streptavidin-Binding Peptide (SBP)-tagged SMC2 allows single-step affinity fluorescence, blotting or purification of the condensin complex
Authors: Kim JH, Chang TM, Graham AN, Choo KH, Kalitsis P, Hudson DF.
Journal: BMC Biochem (2010): 50
Determination of 17beta-oestradiol by fluorescence immunoassay with streptavidin-conjugated quantum dots as label
Authors: Sun M, Du L, Gao S, Bao Y, Wang S.
Journal: Steroids (2010): 400
Multimodality nuclear and fluorescence tumor imaging in mice using a streptavidin nanoparticle
Authors: Liang M, Liu X, Cheng D, Liu G, Dou S, Wang Y, Rusckowski M, Hnatowich DJ.
Journal: Bioconjug Chem (2010): 1385
Site-dependent excited-state dynamics of a fluorescent probe bound to avidin and streptavidin
Authors: Furstenberg A, Kel O, Gradinaru J, Ward TR, Emery D, Bollot G, Mareda J, Vauthey E.
Journal: Chemphyschem (2009): 1517
Influence of streptavidin on the absorption and fluorescence properties of cyanine dyes
Authors: Luschtinetz F, Dosche C, Kumke MU.
Journal: Bioconjug Chem (2009): 576
Fluorescent nanoscale detection of biotin-streptavidin interaction using near-field scanning optical microscopy
Authors: Park HK, Gokarna A, Hulme JP, Park HG, Chung BH.
Journal: Nanotechnology (2008): 235103
Application of biotin-4-fluorescein in homogeneous fluorescence assays for avidin, streptavidin, and biotin or biotin derivatives
Authors: Ebner A, Marek M, Kaiser K, Kada G, Hahn CD, Lackner B, Gruber HJ.
Journal: Methods Mol Biol (2008): 73