|Cy3 NHS ester Catalog No.GC17345|
Sample solution is provided at 25 µL, 10mM.
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|Solubility||very high in water, good in polar organic solvents (DMF, DMSO)||Storage||24 months after receival at -20°C in the dark. Transportation: at room temperature for up to 3 weeks. Avoid prolonged exposure to light. Desiccate.|
|General tips||For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.|
|Shipping Condition||Evaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request
|Excitation max (nm)||584||Emission max (nm)||563|
|Extinction Coefficient (M-1cm-1)||162000||Quantum Yield||0.1|
Sulfonated cyanines are available for the labeling of many targets including:
|• Soluble proteins, which are tolerant to addition of organic co-solvent||• Fluorescence polarization (FP)|
|• Antibodies (with 5-10% of DMSO/DMF)||• Fluorescence resonance energy transfer (FRET)|
|• DNA and oligonucleotides||• Time-resolved fluorescence energy transfer (TR-FRET)|
|• Peptides||• Fluorescence intensity (FI)|
|• Many small molecules|
|• Sensitive proteins which are denatured by DMF or DMSO|
|• Protein conjugation when purification is done by dialysis|
|• Nanoparticles in aqueous solutions|
|• Insoluble or hydrophobic proteins|
Sulfo-Cy3 NHS ester is a sulfonated, hydrophilic and highly water soluble dye. For labeling proteins and peptides, no organic co-solvent is needed. Sulfo-Cy3 NHS ester is ideal for proteins with low solubility and proteins prone to denaturation. Non-sulfonated Cy3 NHS ester is also available. In life science, the sulfonate groups make the Cy dyes soluble in water and also reduce fluorescence-quenching which can arise from dye–dye interactions.
In vitro, sulfo-Cy3 NHS ester can react with green-emitting QDs ligand-exchanged and LA/His-PIMA-PEG-NH2 to provide QD-dye conjugates .
 Reid, D. A.; Keegan, S.; Leo-Macias, A.; Watanabe, G.; Strande, N.T.; Chang, H.H.; Oksuz, B.A.; Fenyo, D.; Lieber, M.R.; Ramsden, D.A.; Rothenberg, E. Organization and dynamics of the nonhomologous end-joining machinery during DNA double-strand break repair. Proceedings of the National Academy of Sciences of the U.S.A., 2015, 112(20).