Choose dyes across visible and near-infrared wavelengths. Distinguish custom conjugation from direct detection with WGA, CTB or streptavidin before selecting chemistry and detection band.
40 products
Select Cy3–Cy7.5 by detection band, reactive dyes by coupling handle, and WGA, CTB or streptavidin by recognition target. Assess labeling density and actual signal after protein coupling.
Showing 1–24 of 40 products
| Product / Cat. No. | Product form | Excitation / nm | Emission / nm | Pack sizes | Product details |
|---|---|---|---|---|---|
| Cy3 NHS EsterQH-30-3001 | NHS Ester | 554 | 566 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3 MaleimideQH-30-3001(Maleimide) | Maleimide | 554 | 566 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3 AzideQH-30-3001(Azide) | Azide | 554 | 566 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3 DBCOQH-30-3001(DBCO) | DBCO | 554 | 566 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3-StreptavidinQH-15-1014 | Streptavidin | 554 | 564 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3 WGAQH-30-3001(WGA) | WGA | 554 | 566 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3 CTBQH-30-3001(CTB) | CTB | 554 | 566 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3.5 NHS EsterQH-30-3002 | NHS Ester | 591 | 604 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3.5 MaleimideQH-30-3002(Maleimide) | Maleimide | 591 | 604 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3.5 AzideQH-30-3002(Azide) | Azide | 591 | 604 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3.5 DBCOQH-30-3002(DBCO) | DBCO | 591 | 604 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3.5 WGAQH-30-3002(WGA) | WGA | 591 | 604 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy3.5 CTBQH-30-3002(CTB) | CTB | 591 | 604 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5 NHS EsterQH-30-3003 | NHS Ester | 640 | 664 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5 MaleimideQH-30-3003(Maleimide) | Maleimide | 640 | 664 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5 AzideQH-30-3003(Azide) | Azide | 640 | 664 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5-StreptavidinQH-15-1015 | Streptavidin | 640 | 664 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5 WGAQH-30-3003(WGA) | WGA | 640 | 664 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5 CTBQH-30-3003(CTB) | CTB | 640 | 664 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5 DBCOQH-30-3003(DBCO) | DBCO | 649 | 667 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5.5 NHS EsterQH-30-3004 | NHS Ester | 680 | 698 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5.5 MaleimideQH-30-3004(Maleimide) | Maleimide | 680 | 698 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5.5 AzideQH-30-3004(Azide) | Azide | 680 | 698 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5.5 DBCOQH-30-3004(DBCO) | DBCO | 680 | 698 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5.5-StreptavidinQH-15-1016 | Streptavidin | 680 | 698 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5.5 WGAQH-30-3004(WGA) | WGA | 680 | 698 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy5.5 CTBQH-30-3004(CTB) | CTB | 680 | 698 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7 NHS EsterQH-30-3005 | NHS Ester | 740 | 770 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7 MaleimideQH-30-3005(Maleimide) | Maleimide | 740 | 770 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7 AzideQH-30-3005(Azide) | Azide | 740 | 770 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7 DBCOQH-30-3005(DBCO) | DBCO | 740 | 770 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7-StreptavidinQH-15-1017 | Streptavidin | 740 | 770 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7 WGAQH-30-3005(WGA) | WGA | 740 | 770 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7 CTBQH-30-3005(CTB) | CTB | 740 | 770 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7.5 NHS EsterQH-30-3006 | NHS Ester | 784 | 814 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7.5 MaleimideQH-30-3006(Maleimide) | Maleimide | 784 | 814 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7.5 AzideQH-30-3006(Azide) | Azide | 784 | 814 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7.5 DBCOQH-30-3006(DBCO) | DBCO | 784 | 814 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7.5 WGAQH-30-3006(WGA) | WGA | 784 | 814 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| Cy7.5 CTBQH-30-3006(CTB) | CTB | 784 | 814 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg |
For support, include: Sample, target handles or recognition target, and detection channel
Cy3–Cy7.5 cover different detection bands. Fluorescence after protein coupling also depends on the dye and labeling density; start with a small input series.
Method background: Cy labeling and fluorescence · Gruber et al. ↗
WGA already carries a Cy dye and recognizes accessible GlcNAc/sialic-acid-associated glycans.
The CTB probe already carries a Cy label and is handled as a protein probe for GM1-related recognition and trafficking.
Cy–streptavidin is a preconjugated biotin-detection probe whose workflow depends on the biotinylated sample.
Tris and glycine consume NHS dye. BSA and gelatin require separation from the target protein; routine buffer exchange is insufficient.
Applies to: For protein preparation before NHS-ester labeling; check competing amines and carrier proteins.
Calculate DOL with absorbance correction, distinguish input ratio from attached dye, and assess recovery and binding.
Applies to: For purified protein conjugates; use this dye’s absorbance parameters and distinguish input ratio from DOL.
Cysteines may be disulfide-bound or protected. Confirm free thiols before deciding on reduction.
Applies to: For maleimide reactive dyes; first establish accessible thiols on the sample.
DTT and β-mercaptoethanol compete for maleimide; residual TCEP can also interfere.
Applies to: For maleimide routes; assess reductant carryover and removal.
Use CuAAC for terminal alkynes and SPAAC for strained alkynes. Identify the handle before assessing copper compatibility.
Applies to: For azide reactive dyes; distinguish terminal from strained alkynes before choosing CuAAC or SPAAC.
Target-bound azides enable coupling; free azide reagents and sodium azide can compete for DBCO.
Applies to: For the SPAAC step between DBCO and a target azide; ordinary amines and thiols are not reaction partners.
WGA labels accessible glycans. Check outline continuity for segmentation; intensity is not a direct measure of membrane amount.
Applies to: For WGA conjugates; glycan accessibility and membrane outlines do not establish protein-specific targeting.
Fixation and permeabilization can change glycan accessibility. Compare outlines, intracellular signal and background separately.
Applies to: For comparing fixation and permeabilization with WGA probes, not for free-dye conjugation.
CTB fluorescence reports GM1-associated distribution; puncta alone do not establish native lipid-raft structure.
Applies to: For CTB–GM1 localization, including perturbation of membrane organization by multivalent binding.
Distinguish peripheral and intracellular CTB signals over time; one endpoint cannot establish a trafficking route.
Applies to: For CTB surface binding and trafficking; total intensity alone does not quantify uptake.
Free biotin occupies streptavidin-binding sites and can reduce detection of biotinylated targets.
Applies to: For prepared streptavidin probes; check competition from free biotin.
Use unstained, streptavidin-only and non-biotinylated-probe controls to distinguish autofluorescence, endogenous biotin and adsorption.
Applies to: For biotin-affinity detection; distinguish endogenous biotin from nonspecific adsorption.
These papers and manufacturer methods are selected for the current product use. Their reagents, conditions and parameters belong to the reported systems, not to measured Qihe product performance or universal operating conditions.
Gruber HJ, Hahn CD, Kada G, et al. · Bioconjugate Chemistry · 11(5):696–704 · 2000
Compares fluorescence changes when Cy3, Cy3.5, Cy5 and Cy7 associate with IgG or avidin, informing joint assessment of labeling density and the purified conjugate’s signal.
DOI: 10.1021/bc000015m
Nanda JS, Lorsch JR. · Methods in Enzymology · 536:87–94 · 2014
Uses FAM ester labeling of a protein to explain primary-amine chemistry and labeling-efficiency assessment. It informs NHS workflow design; input and reaction conditions depend on the actual dye and sample.
Vira S, Mekhedov E, Humphrey G, Blank PS. · Analytical Biochemistry · 402(2):146–150 · 2010
Uses FITC-labeled anti-HA antibody to assess changes in labeling density and antigen binding. It informs input-series design and post-purification functional testing; DOL alone is insufficient for selecting a conjugate.
Mujumdar RB, Ernst LA, Mujumdar SR, Lewis CJ, Waggoner AS. · Bioconjugate Chemistry · 4(2):105–111 · 1993
Studies sulfoindocyanine active-ester structures, spectra and labeling of amine-bearing biomolecules, providing background for cyanine NHS-labeling workflows.
DOI: 10.1021/bc00020a001
Shafer DE, Inman JK, Lees A. · Analytical Biochemistry · 282(1):161–164 · 2000
Examines TCEP interactions with reactive groups, informing evaluation of reductant carryover and buffer exchange.
Baldwin AD, Kiick KL. · Bioconjugate Chemistry · 22(10):1946–1953 · 2011
Studies exchange reactions of model adducts in thiol-containing environments to inform conjugate stability assessment.
DOI: 10.1021/bc200148v
Presolski SI, Hong VP, Finn MG. · Current Protocols in Chemical Biology · 3(4):153–162 · 2011
Describes CuAAC catalyst systems and reaction assessment for terminal-alkyne substrates.
Agard NJ, Prescher JA, Bertozzi CR. · Journal of the American Chemical Society · 126(46):15046–15047 · 2004
Introduces ring-strain-driven azide–alkyne coupling without copper, a foundational study in SPAAC bioconjugation.
DOI: 10.1021/ja044996f
Debets MF, van Berkel SS, Schoffelen S, et al. · Chemical Communications · 46(1):97–99 · 2010
Reports copper-free reaction of a strained alkyne with azides and its application to enzyme PEGylation.
DOI: 10.1039/b917797c
Chazotte B. · Cold Spring Harbor Protocols · 2011(5):pdb.prot5623 · 2011
Describes glycan-dependent membrane labeling with WGA, informing sample preparation and imaging design.
DOI: 10.1101/pdb.prot5623
Kabbani AM, Raghunathan K, Lencer WI, Kenworthy AK, Kelly CV. · PNAS · 117(26):14978–14986 · 2020
Examines how multivalent CTB binding affects GM1 organization and membrane shape, highlighting probe-induced perturbation.
Thermo Fisher Scientific
Sample preparation, free biotin and background control in biotin-affinity detection.
Thermo Fisher Scientific
Sample preparation, free biotin and background control in biotin-affinity detection.
Howarth M, Chinnapen DJF, Gerrow K, et al. · Nature Methods · 3:267–273 · 2006
Uses an engineered monovalent protein to investigate crosslinking by multivalent binding. It informs assessment of probe valency in membrane-protein motion and clustering studies.
DOI: 10.1038/nmeth861
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Product use, preparation, operating conditions and storage.
Spectra, measurement conditions and detection settings for the exact catalog number.
Lot-specific test results. Include the lot number from the vial.
Handling, storage and emergency response information.
Choose the Cy3–Cy7.5 band from actual excitation, emission and detection windows, then decide between conjugation and a WGA, CTB or streptavidin probe. Different forms of the same Cy dye still require catalog-specific parameters.
NHS targets primary amines and maleimide targets free thiols. For azides, distinguish terminal-alkyne CuAAC from strained-alkyne SPAAC; DBCO pairs with azides. Use route-specific buffers, preparation and purification rather than transferring NHS input or timing.
Fluorescence after protein coupling depends on dye, density and environment; dense labeling can cause quenching or functional loss. Compare purified input-series samples for labeling density, recovery, binding and negative background, separating free-dye effects from overlabeling.
WGA recognizes accessible GlcNAc/sialic-acid-associated glycans. Surface binding also fluoresces. Use temperature, incubation, fixation/permeabilization and localization controls to separate surface staining from uptake, and dilute as an aqueous protein probe.
CTB signal reflects accessible GM1, probe binding and trafficking. Membrane-domain or lipid-raft conclusions require independent evidence. Separate surface binding from uptake with time, temperature and localization controls; validate tissue tracing for the model and formulation.
Confirm accessible sample biotin, remove free biotin and excess biotinylation reagent, and check media and formulation additives. Then titrate the aqueous probe against a nonbiotinylated control. Increasing probe input does not replace these checks.
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