BODIPY FL products include WGA, DBCO, Maleimide, Azide, NHS Ester; select for the intended labeling or staining application.
5 products
5 matching products
| Product / Cat. No. | Chemistry | Excitation / nm | Emission / nm | Pack sizes | Product details |
|---|---|---|---|---|---|
| BODIPY FL Succinimidyl EsterQH-40-4004 | NHS Ester | 502 | 510 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| BODIPY FL MaleimideQH-40-4004(Maleimide) | Maleimide | 502 | 510 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| BODIPY FL AzideQH-40-4004(Azide) | Azide | 502 | 510 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| BODIPY FL DBCOQH-40-4004(DBCO) | DBCO | 502 | 510 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg | |
| BODIPY FL WGAQH-40-4004(WGA) | WGA | 502 | 510 | 1 mg / 5 mg / 10 mg / 25 mg / 100 mg |
Need help with reactive forms or detection channels?
QH-40-4004
| Product / Cat. No. | Form | Ex / Em · nm |
|---|---|---|
| BODIPY FL WGAQH-40-4004(WGA) | WGA | 502 / 510 |
| BODIPY FL DBCOQH-40-4004(DBCO) | DBCO | 502 / 510 |
| BODIPY FL MaleimideQH-40-4004(Maleimide) | Maleimide | 502 / 510 |
| BODIPY FL AzideQH-40-4004(Azide) | Azide | 502 / 510 |
| BODIPY FL Succinimidyl EsterQH-40-4004 | NHS Ester | 502 / 510 |
Identify the dye by the complete BODIPY FL name, then choose a suitable reactive end or WGA conjugate. X-designated names remain distinct forms; use the exact catalog number for structure and parameters.
Accessible target-bound azide groups
DBCO is a strained alkyne that cycloadds to an azide. Ordinary unmodified proteins lack this paired handle; residual free azide reagents can consume DBCO.
Accessible free thiols
Maleimide adds to a free thiol to form a thioether-containing product. Sulfur in disulfide bonds is not an available free thiol; reduction must preserve the required sample structure and function.
Terminal alkynes or suitable strained alkynes such as DBCO and BCN
An azide dye does not directly label ordinary primary amines or thiols. Identify the target alkyne before choosing copper-catalyzed or strain-promoted cycloaddition.
Protein N-termini, lysine residues and introduced primary amines
The NHS ester forms an amide bond with a primary amine; hydrolysis competes with coupling. Proteins usually contain multiple accessible sites, and the input ratio is not the final degree of labeling.
Accessible N-acetylglucosamine- and sialic-acid-associated glycans
WGA is wheat germ agglutinin. Signal depends on glycan distribution and accessibility. Fixation, permeabilization, temperature and incubation time affect the observed pattern; signal is not a measure of total membrane amount.
Dye structure, solvent and the conjugated molecule affect a BODIPY readout. Check for cloudiness, adsorption and aggregation after aqueous dilution, then evaluate the purified product in its final buffer.
Selection criteria
Compare each product’s excitation and emission with the instrument’s light source, filters and detector. A number in a product name does not replace its specifications.
Use the matching reactive form for covalent protein, peptide or modified-nucleic-acid labeling. Use the listed WGA conjugate for glycan recognition; a dye name alone does not establish targeting.
Titrate the product in the actual sample, matching acquisition and processing conditions and including controls for the application.
Sample and experimental preparation
Run a small dilution test at a matched final organic-solvent fraction. Resolve cloudiness, precipitation or marked adsorption to tube walls before comparing input ratios.
Record target molecular weight, concentration, available handles and buffer additives. Select a method that separates the target product from free dye, using the product conditions for the actual reactive form.
Retain an unlabeled aliquot from the same preparation. Measure concentration, labeling density and function after purification. Use the actual conjugate for single-color references in multicolor detection.
WGA labels accessible glycans. Check outline continuity for segmentation; intensity is not a direct measure of membrane amount.
WGA can be internalized by live cells. Interpret intracellular signal using timing and localization.
Fixation and permeabilization can change glycan accessibility. Compare outlines, intracellular signal and background separately.
Target-bound azides enable coupling; free azide reagents and sodium azide can compete for DBCO.
Use product analysis to separate low conversion from detection bias, and a no-azide control to check adsorption.
Terminal alkynes pair with azides through CuAAC; DBCO pairs with azides through copper-free SPAAC.
Cysteines may be disulfide-bound or protected. Confirm free thiols before deciding on reduction.
DTT and β-mercaptoethanol compete for maleimide; residual TCEP can also interfere.
Measure labeling density after removing free dye, then check function and changes during storage.
Use CuAAC for terminal alkynes and SPAAC for strained alkynes. Identify the handle before assessing copper compatibility.
Check reactive handles, catalyst components and copper-binding additives when conversion is low.
Use a no-handle control to distinguish labeling from adsorption, and address free dye and catalyst carryover during purification.
Tris and glycine consume NHS dye. BSA and gelatin require separation from the target protein; routine buffer exchange is insufficient.
Check NHS hydrolysis and amine-containing additives, then distinguish low labeling from sample loss or reduced binding.
Calculate DOL with absorbance correction, distinguish input ratio from attached dye, and assess recovery and binding.
Loudet A, Burgess K. · Chemical Reviews · 107(11):4891–4932 · 2007
Reviews BODIPY synthesis, derivatization and spectroscopic properties as background for distinguishing members of the dye family.
DOI: 10.1021/cr078381n
Ksenofontova KV, Kerner AA, Ksenofontov AA, et al. · Molecules · 27(22):7911 · 2022
Studies solvent and protein-conjugation effects on NHS-Ph-BODIPY spectra, informing evaluation of a conjugate in its final sample environment.
Jones LJ, Upson RH, Haugland RP, et al. · Analytical Biochemistry · 251(2):144–152 · 1997
Studies quenching of densely BODIPY FL- and TR-X-labeled casein and dequenching after proteolysis, illustrating how labeling density can change the readout.
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
Cossarizza A, Chang HD, Radbruch A, et al. · European Journal of Immunology · 51(12):2708–3145 · 2021
Provides methodological guidance on detection settings, controls and experimental records for downstream conjugate evaluation.
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
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
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.
Hong V, Presolski SI, Ma C, Finn MG. · Angewandte Chemie International Edition · 48(52):9879–9883 · 2009
Examines ligand, copper catalyst and biomolecule effects to help troubleshoot low CuAAC conversion.
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.
Request the manual, SDS or lot-specific CoA by catalog number. Include the vial lot number for a CoA.
Product use, preparation, operating conditions and storage.
Lot-specific test methods and results.
Handling, storage and emergency response information.
Identify the sample handle or required recognition mechanism, then select a matching reactive dye or preconjugated probe. Use preparation, reaction and storage requirements for the exact catalog number.
Measure labeling density and signal after purification. High local label density can change fluorescence; assess background, recovery and sample function together.
Match target concentration, acquisition settings and sample processing. Compare labeling density together with specific signal, negative background, recovery and function; a free-dye or single endpoint measurement does not assess every performance characteristic.
Use molecular weight, an appropriate extinction coefficient and protein-absorbance correction for the exact catalog number after removing free dye. Request parameters not shown on the product page through its Documents tab.
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