Fluoromax 3 spectrofluorometer

Manufactured by Horiba

Sourced in United States, Japan, France

The Fluoromax-3 is a spectrofluorometer manufactured by Horiba. It is a instrument used to measure the fluorescence properties of samples. The Fluoromax-3 can detect and analyze the emission spectra of fluorescent materials.

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Lab products found in correlation

Fluoressence v3, by Horiba (3 mentions) 8452a diode array spectrophotometer, by Hewlett-Packard (2 mentions) Uv 2501pc spectrophotometer, by Shimadzu (2 mentions) Transwell insert, by Corning (1 mentions) Evom2 epithelial voltohmmeter, by World Precision Instruments (1 mentions) Jsm 6500f, by JEOL (1 mentions) V 670 spectrophotometer, by Jasco (1 mentions) Drx 500, by Bruker (1 mentions) Nanostar saxs instrument, by Bruker (1 mentions) Hitrap desalting column, by GE Healthcare (1 mentions) Hitrap, by Cytiva (1 mentions) Amplex red, by Thermo Fisher Scientific (1 mentions) Superoxide dismutase, by Merck Group (1 mentions) Horseradish peroxidase hrp, by Merck Group (1 mentions) Avance 500 spectrometer, by Bruker (1 mentions) Avance 300 spectrometer, by Bruker (1 mentions) Kaleidagraph software, by Synergy Software (1 mentions) El808 plate reader, by Agilent Technologies (1 mentions) Fluoromax 3 spectrophotometer, by Horiba (1 mentions) Avance 300, by Bruker (1 mentions)

Spelling variants of this product

FluoroMax-3 (99 citations) Spectrofluorometer (35 citations) Fluoromax spectrofluorometer (22 citations) Jobin Yvon FluoroMax-3 spectrofluorometer (4 citations)

74 protocols using fluoromax 3 spectrofluorometer

Transendothelial Transport of Nanoparticles

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HUVECs were seeded in a Corning Transwell insert coated with rat tail collagen type I and grown in EGM-2 complete medium. The transendothelial electrical resistance (TEER) across the HUVEC layer in the Transwell insert was monitored daily by EVOM2™ epithelial voltohmmeter (World Precision Instruments, Sarasota, FL, USA). When the TEER value reached a plateau (indicating confluency), the HUVEC layer was treated with 10 ng/mL of TNF-α for 4 h, followed by incubation with 0.1 mg/mL of FITC-labeled NP or QA-NP for 8 h. The fluorescence intensity of total NPs prior to incubation and those of NPs in the apical and basolateral sides of a Transwell insert after incubation period were measured by FluoroMax^®-3 spectrofluorometer (Horiba Scientific, Edison, NJ, USA). In a separate study, the confluent, TNF-α activated HUVECs were treated with 0.1 mg/mL of NP or QA-NP for 8 h, followed by 16 h incubation in NP-free medium. The TEER values were measured at 0, 4, 8, 12, and 24 h from the NP treatment.

Xu J., Seung-Young Lee S., Seo H., Pang L., Jun Y., Zhang R.Y., Zhang Z.Y., Kim P., Lee W., Kron S.J, & Yeo Y. (2018). Quinic Acid-Conjugated Nanoparticles Enhance Drug Delivery to Solid Tumors via Interactions with Endothelial Selectins. Small (Weinheim an der Bergstrasse, Germany), 14(50), e1803601.

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FtsZ Protein FRET Assay

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FtsZ-CFP or FtsZΔCTC-CFP and/or YFP-FzlC (2 μM final concentration) were added to TK300 buffer. MgCl₂ was used at 2.5 mM, GTP was used at 2 mM and PG vesicles were used at 1 mg/mL. A Fluoromax-3 spectrofluorometer (Jobin Yvon Inc.) was used for fluorescence measurements. The solution was excited at 435 nm (CFP excitation) and scanned for emission from 450–560 nm. FRET/CFP ratios were determined by dividing peak YFP emission (523–528 nm) by peak CFP emission (472–477 nm).

Meier E.L., Razavi S., Inoue T, & Goley E.D. (2016). A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in Caulobacter crescentus. Molecular microbiology, 101(2), 265-280.

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Fluorescence Quenching Assay for FMN Binding

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Noncovalent binding of FMN to apoNqrC' was measured by quenching of FMN fluorescence by apoNqrC'. Solution of free FMN at 0.35 μM in 50 mM potassium phosphate buffer (pH = 7.0) was titrated with varying concentrations of apoNqrC' (from 0.08 to 45 μM). Fluorescence emission spectra were recorded at room temperature with a FluoroMax-3 spectrofluorometer (Horiba Jobin Yvon) using an excitation wavelength of 450 nm. To estimate fluorescence quenching at 100% FMN binding, emission spectrum of 0.35 μM holoNqrC' was determined under the same conditions.
Noncovalent binding of FMN to apoNqrC' was also determined by quenching of apoNqrC' tryptophan fluorescence by free FMN. The apoprotein at 0.32 μM in 50 mM potassium phosphate buffer (pH = 7.0) was titrated with varying amounts of FMN. Fluorescence emission spectra were recorded at room temperature with a FluoroMax-3 spectrofluorometer using an excitation wavelength of 280 nm. To estimate the protein fluorescence quenching at 100% FMN binding, emission spectrum of 0.32 μM holoNqrC' was determined at the same conditions.

Borshchevskiy V., Round E., Bertsova Y., Polovinkin V., Gushchin I., Ishchenko A., Kovalev K., Mishin A., Kachalova G., Popov A., Bogachev A, & Gordeliy V. (2015). Structural and Functional Investigation of Flavin Binding Center of the NqrC Subunit of Sodium-Translocating NADH:Quinone Oxidoreductase from Vibrio harveyi. PLoS ONE, 10(3), e0118548.

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Quantifying Liposome Leakage Dynamics

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The leakage of encapsulated solutes was assayed by the method of ANTS/DPX52 (link). LUVs containing ANTS and DPX were prepared as described previously53 (link). Changes in fluorescence intensity were recorded in a FluoroMax-3 spectrofluorometer (Horiba, Japan) with excitation and emission wavelengths set at 355 nm and 515 nm, respectively. A 475 nm filter was placed between the sample and the emission monochromator. Liposome concentration was 100 μM. Toxin was added at a final concentration of 0.6 μM (lipid/protein molar ratio was 150:1). The complete release of the fluorescent probe (100% signal) was achieved by the addition of Triton X-100 (final concentration=0.1% w/v). Measurements were carried out at 25 °C with constant stirring. The levels of encapsulation were similar in all the compositions of LUV tested (not shown).

Tanaka K., Caaveiro J.M., Morante K., González-Mañas J.M, & Tsumoto K. (2015). Structural basis for self-assembly of a cytolytic pore lined by protein and lipid. Nature Communications, 6, 6337.

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Amyloid-beta Binding Assay

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Aβ samples were first mixed with 0.5 µM Bis-ANS solution and measured the fluorescence signal. The emission spectra of Bis-ANS were collected from 450 to 550 nm with excitation at 400 nm. Fluorescence emission spectra were obtained using a FluoroMax-3 spectrofluorometer (Horiba Jobin Yvon). The background from buffer control was subtracted.

Lee M.C., Yu W.C., Shih Y.H., Chen C.Y., Guo Z.H., Huang S.J., Chan J.C, & Chen Y.R. (2018). Zinc ion rapidly induces toxic, off-pathway amyloid-β oligomers distinct from amyloid-β derived diffusible ligands in Alzheimer’s disease. Scientific Reports, 8, 4772.

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Spectroscopic Analysis of Hydrazone Fluorophore

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Absorption spectra were obtained at room temperature using a Hewlett Packard 8452A Diode Array Spectrophotometer. Emission spectra were recorded at room temperature using a Jobin Yvon Horiba FluoroMax-3 spectrofluorometer. The samples were excited at 405 nm.
Stock solutions of the fluorophore were made fresh by dissolving the solid molecule in 10 mM phosphate buffer, pH 7.0 (PB). An extinction coefficient of ε₃₄₆ =1.9 x 10⁴ M^-1 cm^-1 was used to obtain the concentration of the solution. A propanal hydrazone of CH was prepared by mixing large excess of propanal with CH in PB.

Mukherjee K., Chio T.I., Sackett D.L, & Bane S.L. (2015). Detection of Oxidative Stress-Induced Carbonylation in Live Mammalian Cells. Free radical biology & medicine, 84, 11-21.

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Characterization of Polymer Thin Films

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The NMR measurements were carried out on a Bruker DRX-500 at 600 MHz for ¹H NMR and 150 MHz for ¹³C NMR spectra. Absorption and transmittance spectra were performed on a JASCO-V-670 spectrophotometer. The background of ITO or glass (where the thin film were deposited) was subtracted when we tested the absorption and transmittance spectra of polymer films. Photoluminescence excitation spectra of polymer films were recorded on a HORIBA Jobin Yvon FluoroMax-3 spectrofluorometer. Cyclic voltammetry (CV) was conducted with CHI model 619A. ITO and a platinum wire were used as a working electrode and an auxiliary electrode, respectively. The CV and EC experiments were performed in a solution of 0.1 M tetrabutylammonium perchlorate (TBAP)/acetonitrile (CH₃CN) against a Ag/Ag⁺ reference electrode. High resolution field-emission scanning electron microscope (SEM) images of polymer films were conducted on JEOL JSM-6500F. EIS measurements of polymer films were performed on BCS-815 with the frequency range of 10 mHz–10 kHz. DPV of PI-1a and PI-2a films were performed on Autolab PGSTATE302 MBA. XRD was performed on D2 PHASER (BRUKER). SAXS was performed on an in-house Bruker Nanostar SAXS instrument. AFM was performed on Dimension Icon (BRUKER).

Zhang Q., Tsai C.Y., Li L.J, & Liaw D.J. (2019). Colorless-to-colorful switching electrochromic polyimides with very high contrast ratio. Nature Communications, 10, 1239.

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Spectroscopic Characterization of Fluorescent Proteins

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Absorbance was measured using a Hitachi U-2000 spectrophotometer (Hitachi High Technologies, Schaumburg, IL). Excitation and emission spectra were measured with a FluoroMax-3 spectrofluorometer (Horiba/Jobin Yvon, Edison, NJ). Purified protein samples were measured in PBS at room temperature. To determine extinction coefficients and quantum yields, absorbance and fluorescence of the new fluorescent variants were compared with that of parental proteins. To assess photobleaching sensitivity under comparable imaging parameters, oxFPs and parental FPs were transiently expressed in U-2 OS cells. Cells were imaged using standard live cell imaging conditions. Images were acquired at 5 frames/s for 400 frames.

Costantini L.M., Baloban M., Markwardt M.L., Rizzo M.A., Guo F., Verkhusha V.V, & Snapp E.L. (2015). A palette of fluorescent proteins optimized for diverse cellular environments. Nature Communications, 6, 7670.

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Histone Peptide Binding Kinetics

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Spectra were recorded at 25 °C on a Fluoromax-3 spectrofluorometer (HORIBA). The samples containing 1–2 μM wild type or mutated Set3 PHD finger and progressively increasing concentrations of the histone peptide were excited at 295 nm. Emission spectra were recorded between 315 and 405 nm with a 0.5 nm step size and a 1 s integration time and averaged over 3 scans. The K_d values were determined using a nonlinear least-squares analysis and the equation:

Δ I = Δ I_{\max} \frac{(([L] + [P] + K_{d}) - \sqrt{{([L] + [P] + K_{d})}^{2} - 4 [P] [L])})}{2 [P]}

where [L] is the concentration of the histone peptide, [P] is the concentration of the protein, ΔI is the observed change of signal intensity, and ΔI_max is the difference in signal intensity of the free and bound states of the protein. Each K_d value was averaged over three separate experiments, with error calculated as the standard deviation between the runs.

Gatchalian J., Ali M., Andrews F.H., Zhang Y., Barrett A.S, & Kutateladze T.G. (2016). Structural insight into recognition of methylated histone H3K4 by Set3. Journal of molecular biology, 429(13), 2066-2074.

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Fluorescence-based Histone Peptide Binding Assay

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Spectra were recorded at 25 °C on a Fluoromax-3 spectrofluorometer (HORIBA). The samples containing 0.5–1 μM wild type or mutated PHD fingers in 20 mM phosphate (or 25 mM Tris) pH 6.0, 6.9 or 7.5, 150 mM NaCl, 3 mM DTT buffer and progressively increasing concentrations of the histone peptides were excited at 295 nm. Emission spectra were recorded between 320 and 360 nm with a 0.5 nm step size and a 0.5 s integration time and averaged over 3 scans. The K_d values were determined using a nonlinear least-squares analysis and the equation:

Δ I = Δ I_{\max} \frac{(([L] + [P] + K_{d}) - \sqrt{{([L] + [P] + K_{d})}^{2} - 4 [P] [L])})}{2 [P]}

where [L] is the concentration of the histone peptide, [P] is the concentration of the protein, ΔI is the observed change of signal intensity, and ΔI_max is the difference in signal intensity of the free and bound states of the protein. The K_d values were averaged over three separate experiments (two in Fig. 4f for pH 7.5), with error calculated as the standard deviation between the runs.

Tencer A.H., Gatchalian J., Klein B.J., Khan A., Zhang Y., Strahl B.D., van Wely K.H, & Kutateladze T.G. (2017). A unique pH-dependent recognition of methylated histone H3K4 by PPS and DIDO. Structure (London, England : 1993), 25(10), 1530-1539.e3.

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