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iFluor® Ultra 750 maleimide

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Physical properties
Molecular weight1208.27
SolventDMSO
Spectral properties
Absorbance (nm)750
Correction Factor (260 nm)0.04
Correction Factor (280 nm)0.05
Extinction coefficient (cm -1 M -1)2500001
Excitation (nm)749
Emission (nm)773
Quantum yield0.321
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
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iFluor® 820 goat anti-mouse IgG (H+L)
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iFluor® 840 goat anti-mouse IgG (H+L)
iFluor® 840 goat anti-mouse IgG (H+L) *Cross Adsorbed*
iFluor® 860 goat anti-mouse IgG (H+L)
iFluor® 860 goat anti-mouse IgG (H+L) *Cross Adsorbed*
iFluor® 800 goat anti-rabbit IgG (H+L)
iFluor® 800 goat anti-rabbit IgG (H+L) *Cross Adsorbed*
iFluor® 810 goat anti-rabbit IgG (H+L)
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iFluor® 820 goat anti-rabbit IgG (H+L)
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iFluor® 840 goat anti-rabbit IgG (H+L)
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iFluor® 860 goat anti-rabbit IgG (H+L)
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iFluor® 660 succinimidyl ester
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iFluor® 750 succinimidyl ester
iFluor® 610 succinimidyl ester
iFluor® 710 succinimidyl ester
iFluor® 790 succinimidyl ester
iFluor® 800 succinimidyl ester
iFluor® 810 succinimidyl ester
iFluor® 820 succinimidyl ester
iFluor® 860 succinimidyl ester
iFluor® 546 succinimidyl ester
iFluor® 568 succinimidyl ester
iFluor® 430 succinimidyl ester
iFluor® 450 succinimidyl ester
iFluor® 840 succinimidyl ester
iFluor® 560 succinimidyl ester
iFluor® 670 succinimidyl ester
iFluor® 460 succinimidyl ester
iFluor® 440 succinimidyl ester
iFluor® 665 succinimidyl ester
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iFluor® Ultra 594 succinimidyl ester
iFluor® Ultra 647 succinimidyl ester
iFluor® 720 succinimidyl ester
iFluor® 740 succinimidyl ester
iFluor® 597 succinimidyl ester
iFluor® 770 succinimidyl ester
iFluor® 780 succinimidyl ester
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iFluor® 350-Wheat Germ Agglutinin (WGA) Conjugate
iFluor® 532-Wheat Germ Agglutinin (WGA) Conjugate
iFluor® 680-Wheat Germ Agglutinin (WGA) Conjugate
iFluor® 700-Wheat Germ Agglutinin (WGA) Conjugate
iFluor® 750-Wheat Germ Agglutinin (WGA) Conjugate
iFluor® 790-Wheat Germ Agglutinin (WGA) Conjugate
iFluor® 570 Styramide *Superior Replacement for Alexa Fluor 568 tyramide*
iFluor® 670 Styramide *Replacement for Opal 690*
iFluor® 445 succinimidyl ester
iFluor® 500 succinimidyl ester
iFluor® 680 Tyramide *Superior Replacement for Opal 690*
iFluor® 790 Azide
iFluor® 790 Alkyne
iFluor® 720 maleimide
Show More (281)

OverviewpdfSDSpdfProtocol


Molecular weight
1208.27
Absorbance (nm)
750
Correction Factor (260 nm)
0.04
Correction Factor (280 nm)
0.05
Extinction coefficient (cm -1 M -1)
2500001
Excitation (nm)
749
Emission (nm)
773
Quantum yield
0.321
The iFluor® Ultra series represents an enhancement of our established iFluor® dyes, optimized for antibody labeling in fluorescence imaging and flow cytometry. Within this series, iFluor® Ultra 750 is a bright NIR fluorescent dye excitable by 633 nm to 685 nm laser lines, with a peak emission at 773 nm. Antibody conjugates with iFluor® Ultra 750 demonstrate superior brightness compared to those labeled with spectrally similar dyes such as Cy7, Dylight 755, IRDye750, and Alexa Fluor® 750 under the same conditions. Additionally, iFluor® Ultra 750 maintains stable fluorescence across a pH range of 4 to 10. The maleimide derivative of iFluor® Ultra 750 is widely used for conjugation to thiol groups on proteins, oligonucleotide thiophosphates, or low molecular weight ligands. Conjugates with iFluor® Ultra 750 demonstrate higher fluorescence intensity and greater photostability compared to those with other spectrally similar fluorophores, enhancing their utility for advanced fluorescence applications. Fluorescent dye-conjugated antibodies are crucial for protein identification in various applications, including fluorescent cell imaging, flow cytometry, western blotting, and immunohistochemistry. The advantages of these conjugates include increased sensitivity, multiplexing capabilities, and ease of use, facilitating complex biological studies.

Example protocol


PREPARATION OF STOCK SOLUTIONS

Unless otherwise noted, all unused stock solutions should be divided into single-use aliquots and stored at -20 °C after preparation. Avoid repeated freeze-thaw cycles

iFluor® Ultra 750 maleimide Stock Solution (Solution B)
  1. Prepare a 10 mM iFluor® Ultra 750 maleimide stock solution by adding anhydrous DMSO to the vial of iFluor® Ultra 750 maleimide. Mix well by pipetting or vortexing.

    Note: Before starting the conjugation process, prepare the dye stock solution (Solution B) and use it promptly. Prolonged storage of Solution B may reduce its activity. If necessary, Solution B can be stored in the freezer for up to 4 weeks, provided it is protected from light and moisture. Avoid freeze/thaw cycles.

Protein Stock Solution (Solution A)
  1. Prepare a 1 mL protein labeling stock solution, by mixing 100 µL of a reaction buffer (e.g., 100 mM MES buffer with a pH ~6.0) with 900 µL of the target protein solution (e.g., an antibody or protein solution with a concentration >2 mg/mL if possible).

    Note: The pH of the protein solution (Solution A) should be 6.5 ± 0.5.

    Note: Impure antibodies or antibodies stabilized with bovine serum albumin (BSA) or other proteins will not be labeled well.

    Note: The conjugation efficiency is significantly reduced if the protein concentration is less than 2 mg/mL. To achieve optimal labeling efficiency, it is recommended to maintain a final protein concentration within the range of 2-10 mg/mL.

Disulfide Reduction (If Necessary)

If your protein does not contain a free cysteine, it must be treated with DTT or TCEP to generate a thiol group. DTT and TCEP are utilized to convert disulfide bonds into two free thiol groups. If using DTT, ensure to remove any free DTT via dialysis or gel filtration before conjugating a dye maleimide to your protein. Below is a sample protocol for generating a free thiol group:

  1. To prepare a fresh solution of 1 M DTT, dissolve 15.4 mg of DTT in 100 µL of distilled water.

  2. To prepare the IgG solution in 20 mM DTT, first, add 20 µL of DTT stock to each milliliter of the IgG solution while mixing gently. Then, allow the solution to stand at room temperature for 30 minutes without additional mixing. This resting period helps to minimize the reoxidation of cysteines to cystines.

  3. Pass the reduced IgG through a filtration column that has been pre-equilibrated with "Exchange Buffer." Collect 0.25 mL fractions as they elute from the column.

  4. Determine the protein concentrations and combine the fractions containing the highest amounts of IgG. This can be accomplished using either spectrophotometric or colorimetric methods.

  5. Proceed with the conjugation immediately after this step (refer to the Sample Experiment Protocol for details).

    Note: IgG solutions should be >4 mg/mL for the best results. The antibody should be concentrated if less than 2 mg/mL. Include an extra 10% for losses on the buffer exchange column.

    Note: The reduction can be carried out in almost any buffers from pH 7-7.5, e.g., MES, phosphate, or TRIS buffers.

    Note: Steps 3 and 4 can be replaced by dialysis.

SAMPLE EXPERIMENTAL PROTOCOL

This labeling protocol was designed for the conjugation of goat anti-mouse IgG with iFluor® Ultra 750 maleimide. You may need to further optimize the protocol for your specific proteins.

Note: Each protein requires a specific dye-to-protein ratio, which varies based on the properties of the dyes. Over-labeling a protein can negatively impact its binding affinity while using a low dye-to-protein ratio can result in reduced sensitivity.

Run the Conjugation Reaction
  1. Use a 10:1 molar ratio of Solution B (dye)/Solution A (protein) as the starting point. Add 5 µL of the dye stock solution (Solution B, assuming the dye stock solution is 10 mM) to the vial of the protein solution (95 µL of Solution A), and mix thoroughly by shaking. The protein solution has a concentration of ~0.05 mM assuming the protein concentration is 10 mg/mL and the molecular weight of the protein is ~200KD.

    Note: We recommend using a 10:1 molar ratio of Solution B (dye) to Solution A (protein). If this ratio is not suitable, determine the optimal dye/protein ratio by testing 5:1, 15:1, and 20:1 ratios.

  2. Continue to rotate or shake the reaction mixture at room temperature for 30-60 minutes.
Purify the Conjugate

The following protocol serves as an example for purifying dye-protein conjugates using a Sephadex G-25 column.

  1. Follow the manufacturer's instructions to prepare the Sephadex G-25 column.

  2. Load the reaction mixture (from the "Run conjugation reaction" step) onto the top of the Sephadex G-25 column.

  3. Add PBS (pH 7.2-7.4) as soon as the sample runs just below the top of the resin surface.

  4. Add more PBS (pH 7.2-7.4) to the desired sample to complete the column purification. Then, combine the fractions that contain the desired dye-protein conjugate.

    Note: For immediate use, dilute the dye-protein conjugate with staining buffer. If you need to use it multiple times, divide it into aliquots.

    Note: For long-term storage, the dye-protein conjugate solution should be either concentrated or freeze-dried.

Characterize the Desired Dye-Protein Conjugate

The Degree of Substitution (DOS) is a key factor in characterizing dye-labeled proteins. Proteins with a lower DOS generally have weaker fluorescence intensity, while those with a higher DOS may also have reduced fluorescence. For most antibodies, the optimal DOS is recommended to be between 2 and 10, depending on the properties of the dye and protein. For effective labeling, the DOS should be controlled to have 5-8 moles of iFluor® Ultra 750 maleimide per mole of antibody. The following steps outline how to determine the DOS of iFluor® Ultra 750 maleimide-labeled proteins.

Measure Absorption

To measure the absorption spectrum of a dye-protein conjugate, maintain the sample concentration between 1 and 10 µM. The exact concentration within this range will depend on the dye's extinction coefficient.

Read OD (absorbance) at 280 nm and dye maximum absorption (ƛmax = 773 nm for iFluor® Ultra 750 dyes)

For most spectrophotometers, dilute the sample (from the column fractions) with de-ionized water until the OD values fall within the range of 0.1 to 0.9. The optimal absorbance for protein is at 280 nm, while for iFluor® Ultra 750 maleimide, it is at 773 nm. To ensure accurate readings, make sure the conjugate is free of any non-conjugated dye.

Calculate DOS

You can calculate DOS using our tool by following this link:

https://www.aatbio.com/tools/degree-of-labeling-calculator

Calculators


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of iFluor® Ultra 750 maleimide 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 mM82.763 µL413.815 µL827.63 µL4.138 mL8.276 mL
5 mM16.553 µL82.763 µL165.526 µL827.63 µL1.655 mL
10 mM8.276 µL41.381 µL82.763 µL413.815 µL827.63 µL

Molarity calculator

Enter any two values (mass, volume, concentration) to calculate the third.

Mass (Calculate)Molecular weightVolume (Calculate)Concentration (Calculate)Moles
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Spectrum


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spectrum

Spectral properties

Absorbance (nm)750
Correction Factor (260 nm)0.04
Correction Factor (280 nm)0.05
Extinction coefficient (cm -1 M -1)2500001
Excitation (nm)749
Emission (nm)773
Quantum yield0.321

Product Family


NameExcitation (nm)Emission (nm)Extinction coefficient (cm -1 M -1)Quantum yieldCorrection Factor (260 nm)Correction Factor (280 nm)
iFluor® Ultra 594 maleimide58660118000010.9110.070.05
iFluor® Ultra 647 maleimide65567025000010.3910.070.07

References


View all 32 references: Citation Explorer
Targeting lung cancer with clinically relevant EGFR mutations using anti-EGFR RNA aptamer.
Authors: Thomas, Brian J and Guldenpfennig, Caitlyn and Guan, Yue and Winkler, Calvin and Beecher, Margaret and Beedy, Michaela and Berendzen, Ashley F and Ma, Lixin and Daniels, Mark A and Burke, Donald H and Porciani, David
Journal: Molecular therapy. Nucleic acids (2023): 102046
pH-responsive graphene oxide loaded with targeted peptide and anticancer drug for OSCC therapy.
Authors: Li, Ran and Gao, Ruifang and Zhao, Yingjiao and Zhang, Fang and Wang, Xiangyu and Li, Bing and Wang, Lu and Ma, Lixin and Du, Jie
Journal: Frontiers in oncology (2022): 930920
Near-Infrared Fluorescence Imaging of Carotid Plaques in an Atherosclerotic Murine Model.
Authors: Wu, Xiaotian and Daniel Ulumben, Amy and Long, Steven and Katagiri, Wataru and Wilks, Moses Q and Yuan, Hushan and Cortese, Brian and Yang, Chengeng and Kashiwagi, Satoshi and Choi, Hak Soo and Normandin, Marc D and El Fakhri, Georges and Zaman, Raiyan T
Journal: Biomolecules (2021)
Challenging a Preconception: Optoacoustic Spectrum Differs from the Optical Absorption Spectrum of Proteins and Dyes for Molecular Imaging.
Authors: Fuenzalida Werner, Juan Pablo and Huang, Yuanhui and Mishra, Kanuj and Janowski, Robert and Vetschera, Paul and Heichler, Christina and Chmyrov, Andriy and Neufert, Clemens and Niessing, Dierk and Ntziachristos, Vasilis and Stiel, Andre C
Journal: Analytical chemistry (2020)
CD24-targeted intraoperative fluorescence image-guided surgery leads to improved cytoreduction of ovarian cancer in a preclinical orthotopic surgical model.
Authors: Kleinmanns, Katrin and Fosse, Vibeke and Davidson, Ben and de Jalón, Elvira García and Tenstad, Olav and Bjørge, Line and McCormack, Emmet
Journal: EBioMedicine (2020): 102783
Mechanistic profiling of the release kinetics of siRNA from lipidoid-polymer hybrid nanoparticles in vitro and in vivo after pulmonary administration.
Authors: Thanki, Kaushik and van Eetvelde, Delphine and Geyer, Antonia and Fraire, Juan and Hendrix, Remi and Van Eygen, Hannelore and Putteman, Emma and Sami, Haider and de Souza Carvalho-Wodarz, Cristiane and Franzyk, Henrik and Nielsen, Hanne Mørck and Braeckmans, Kevin and Lehr, Claus-Michael and Ogris, Manfred and Foged, Camilla
Journal: Journal of controlled release : official journal of the Controlled Release Society (2019): 82-93
Generation and characterization of novel recombinant anti-hERG1 scFv antibodies for cancer molecular imaging.
Authors: Duranti, Claudia and Carraresi, Laura and Sette, Angelica and Stefanini, Matteo and Lottini, Tiziano and Crescioli, Silvia and Crociani, Olivia and Iamele, Luisa and De Jonge, Hugo and Gherardi, Ermanno and Arcangeli, Annarosa
Journal: Oncotarget (2018): 34972-34989
Enhanced Release of Molecules upon Ultraviolet (UV) Light Irradiation from Photoresponsive Hydrogels Prepared from Bifunctional Azobenzene and Four-Arm Poly(ethylene glycol).
Authors: Rastogi, Shiva K and Anderson, Hailee E and Lamas, Joseph and Barret, Scott and Cantu, Travis and Zauscher, Stefan and Brittain, William J and Betancourt, Tania
Journal: ACS applied materials & interfaces (2018): 30071-30080
Phosphorothioate-Modified AP613-1 Specifically Targets GPC3 when Used for Hepatocellular Carcinoma Cell Imaging.
Authors: Dong, Lili and Zhou, Hongxin and Zhao, Menglong and Gao, Xinghui and Liu, Yang and Liu, Dongli and Guo, Wei and Hu, Hongwei and Xie, Qian and Fan, Jia and Lin, Jiang and Wu, Weizhong
Journal: Molecular therapy. Nucleic acids (2018): 376-386
In vivo fluorescence imaging of hepatocellular carcinoma using a novel GPC3-specific aptamer probe.
Authors: Zhao, Menglong and Dong, Lili and Liu, Zhuang and Yang, Shuohui and Wu, Weizhong and Lin, Jiang
Journal: Quantitative imaging in medicine and surgery (2018): 151-160