Fluorolog 3 22

Manufactured by Horiba

Sourced in Japan

The Fluorolog 3-22 is a fluorescence spectrometer designed for measuring the fluorescence properties of samples. It is capable of performing excitation and emission scans, as well as time-resolved fluorescence measurements. The core function of the Fluorolog 3-22 is to analyze the fluorescence characteristics of materials and compounds.

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Lab products found in correlation

Uv 3600, by Shimadzu (1 mentions) Spm 8100fm, by Shimadzu (1 mentions) Cary 300, by Agilent Technologies (1 mentions) Ltq orbitrap xl, by Thermo Fisher Scientific (1 mentions) Avance 3 700 mhz spectrometer, by Bruker (1 mentions) Msd sl ion trap mass spectrometer, by Agilent Technologies (1 mentions) Avance 300 mhz spectrometer, by Bruker (1 mentions) Nanoled 405l, by Horiba (1 mentions) Cary 5, by Agilent Technologies (1 mentions) Fluorolog 3 22 spectrofluorometer, by Horiba (1 mentions) Avance 3 500 spectrometer, by Bruker (1 mentions) D8 venture diffractometer, by Bruker (1 mentions) Eclipse spectrometer, by Agilent Technologies (1 mentions) Axis ultra dld, by Shimadzu (1 mentions) Ultra 55, by Zeiss (1 mentions) Quantax detector, by Bruker (1 mentions) C9920 02 absolute pl quantum yield measurement system, by Hamamatsu Photonics (1 mentions) Cary 300 bio uv vis spectrophotometer, by Agilent Technologies (1 mentions) Avance 2 spectrometer, by Bruker (1 mentions) Tensor 27 ft ir spectrophotometer, by Bruker (1 mentions)

Spelling variants of this product

Fluorolog-3 (201 citations) Fluorolog 3–22 spectrofluorometer (16 citations) Fluorolog FL 3-22 spectrometer (3 citations) Fluorolog 3–22 photon-counting spectrofluorometer (3 citations) Fluorolog 3–22 spectrophotometer (2 citations) Fluorolog-3 Model FL3-22 spectrofluorometer (2 citations) Yvon Fluorolog 3-22 spectrofluorometer (2 citations) Fluorolog 3-22 spectro uorometer (2 citations) FluoroLog-3 FL3-22 Spectrophotometer (2 citations) Jobin Yvon FluoroLog 3–22 (2 citations)

14 protocols using fluorolog 3 22

Diverse Characterization Techniques Protocol

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Contact angles were observed with CA-X (Kyowa Interface Science
Co. Ltd.). Synchrotron XRPD patterns were recorded on a large Debye–Scherrer
camera installed at SPring-8 BL02B2 (JASRI/SPring-8) using an imaging
plate as a detector. Atomic force microscope SPM-8100FM (Shimadzu)
was used for the measurements of FM-AFM. Electronic absorption spectra
in the solid state were observed from the diffused reflection method
with the conversion of the y-axis by UV-3600 (Shimadzu).
Polarized electronic absorption spectra using an optical waveguide
system was obtained using a modified SIS-5100 attached with a Glan–Taylor
polarizer prism (System Instruments Co.). Luminescence and excitation
spectra were recorded on a Fluorolog 3-22 (Horiba Jobin Yvon). Absolute
luminescence quantum yields and luminescence lifetimes were determined
using an absolute luminescence quantum yield C9920-02 spectrometer
(Hamamatsu Photonics K. K.) and a Quantaurus-Tau C11367-12 spectrometer
(Hamamatsu Photonics K. K.), respectively, with pulsed excitation
light sources.

Marets N., Kanno S., Ogata S., Ishii A., Kawaguchi S, & Hasegawa M. (2019). Lanthanide-Oligomeric Brush Films: From Luminescence Properties to Structure Resolution. ACS Omega, 4(13), 15512-15520.

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Fluorescent Labeling of Calmodulin

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Dansyl (5-(dimethylamino) naphthalene-1-sulfonyl chloride) is an amine-reactive fluorescent dye. Dansyl-CaM was prepared as described previously (85 (link)). CaM (1 mg/ml) was transferred into 10 mm NaHCO₃, 1 mm EDTA, pH 10.0, at 4 °C. 30 μl of 6 mm dansyl-chloride (1.5 mol/mol of CaM) in DMSO was added to 2 ml of CaM, with stirring. After incubation for 12 h at 4 °C, the mixture was first dialyzed against 500 volumes of 150 mm NaCl, 1 mm EDTA, 20 mm Tris-HCl, pH 7.5, at 4 °C, and then dialyzed against 500 volumes of water. Labeling yields were determined from absorbance spectra using the ϵ320 of 3,400 m⁻¹ cm⁻¹ and were compared with protein concentrations determined using the Bradford method with wild-type CaM used as the protein standard (86 (link)) ESI-MS was used to confirm successful dansyl-labeling of CaM protein. The concentration of dansyl-CaM in all experiments was 2 μm. Steady-state fluorescence was performed in a similar manner as the Trp experiments, except that a newer Fluorolog 3-22 (Horiba Scientific, Ltd.) fluorimeter was used, and the buffer used was 10 mm HEPES, pH 7.0, with supplemented 0.1 mm CaCl₂.

Chemin J., Taiakina V., Monteil A., Piazza M., Guan W., Stephens R.F., Kitmitto A., Pang Z.P., Dolphin A.C., Perez-Reyes E., Dieckmann T., Guillemette J.G, & Spafford J.D. (2017). Calmodulin regulates Cav3 T-type channels at their gating brake. The Journal of Biological Chemistry, 292(49), 20010-20031.

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Characterization of Spectroscopic Properties

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¹H NMR and ¹³C NMR spectra were recorded with a Bruker Avance 300 MHz spectrometer, but in some cases, a Bruker Avance‐III 700 MHz spectrometer was used. Chemical shifts are given in parts per million according to the solvent signal. Electrospray (ES) mass spectra were obtained with an Agilent MSD SL ion‐trap mass spectrometer (Agilent, Waldbronn, Germany), and high‐resolution mass spectrometry (HRMS) was performed with a LTQ Orbitrap XL from Thermo Fisher Scientific (Waltham, MA, USA), operating in positive‐ion mode by using electrospray ionization. Absorption measurements were performed with a Hitachi U‐3010 or an Agilent Cary 300. Emission spectra were measured with a Hitachi F‐4500 or a Horiba Fluorolog‐3–22. The quantum yields were determined in aerated HBS 7.3 by the relative method41 by using rhodamine 6G (Φ=94 %)31, 32 as a standard. The quantum yield determinations were performed with a Cary 300 UV/Vis spectrophotometer and a Fluorolog‐3–22 fluorimeter, whereby the data were corrected for changes in refractive indices. Excitation of reference standard and samples was performed at λ=335 nm, and the concentration was held below an absorbance value of 0.1. During all the measurements, the same quartz glass cuvette was used, and the orientation of the cuvette in the spectrometers was always identical.

Faschinger F., Ertl M., Zimmermann M., Horner A., Himmelsbach M., Schöfberger W., Knör G, & Gruber H.J. (2017). Stable Europium(III) Complexes with Short Linkers for Site‐Specific Labeling of Biomolecules. ChemistryOpen, 6(6), 721-732.

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Spectroscopic Characterization of Materials

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UV-vis measurements were performed on a Varian Cary 5. PL spectra were obtained with Fluorolog 322 (Horiba Jobin Yvon, Ltd) with the range of wavelength from 500 to 800 nm by exciting at 450 nm with a standard 450-W Xenon CW lamp. The samples were mounted at 60° and the emission recorded at 90° from the incident beam path. Time-resolved PL was performed using Fluorolog 322 spectrofluorometer (Horiba Jobin Yvon, Ltd). A NanoLED-405L (Horiba) laser diode (405 nm) was used for excitation. The samples were mounted at 60° and the emission collected at 90° from the incident beam path. The detection monochromator was set to 650 nm and the PL was recorded using a picosecond photodetection module (TBX-04, Horiba Scientific).

Xiang W., Wang Z., Kubicki D.J., Wang X., Tress W., Luo J., Zhang J., Hofstetter A., Zhang L., Emsley L., Grätzel M, & Hagfeldt A. (2019). Ba-induced phase segregation and band gap reduction in mixed-halide inorganic perovskite solar cells. Nature Communications, 10, 4686.

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Structural and Optical Characterization of Molecular Complexes

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X-ray diffraction measurements were made at 133 K on a Bruker D8 Venture diffractometer with a microfocus sealed tube and a Photon II detector using graphite monochromated Mo-Kα radiation (λ = 0.71073 Å). NMR spectra were recorded on a Bruker Avance III 500 spectrometer at 500 MHz for ¹H and 125.7 MHz for ¹³C. Lifetime measurements and photoluminescence measurements of the complexes were made on a Cary Eclipse spectrometer with a xenon lamp as an excitation source, as well as on an N-400M fluorescent microscope. The quantum yields and photoluminescence measurements are performed at FluoroLog3-22, Horiba JobinYvon equipped with an integration sphere.
The crystal structure was solved by direct methods using SHELXT [41 (link)] and was refined by full-matrix least-squares calculations on F2 (SHELXL2018 [42 (link)]) in the graphical user interface Shelxle [43 (link)]. The molecular structure is represented using Mercury v4.0 software [44 (link)]. The CIE 1931 chromatograms were obtained using the LED ColorCalculator v7.77 [45 ].

Romanova J., Lyapchev R., Kolarski M., Tsvetkov M., Elenkova D., Morgenstern B, & Zaharieva J. (2023). Molecular Design of Luminescent Complexes of Eu(III): What Can We Learn from the Ligands. Molecules, 28(10), 4113.

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Characterization of Novel Materials

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SEM images were obtained on a ZEISS ULTRA 55 microscope equipped with a secondary in-lens electron detector, together with a Bruker-QUANTAX detector for EDS studies. X-ray photoelectron spectroscopy (XPS) was performed using a KRATOS AXIS ULTRA DLD equipped with a monochromatic Al-Kα X-ray source (1253.6 eV); the binding energies were calibrated at the Au 4f level (84.0 eV). Synchrotron X-ray powder diffraction (XRPD) patterns were obtained with a large Debye-Scherrer camera installed at the SPring-8 BL02B2 beamline, using an imaging plate as the detector44 and an incident X-ray wavelength of 0.99933 Å. Luminescence spectra were recorded on a Horiba Jobin-Ybon Fluorolog 3–22 with a UV cut filter. The emission decay curves were acquired using a Quantaurus-Τau C11367-12 (Hamamatsu Photonics K. K.) with excitation via a xenon flash lamp with a band-path filter (λ_ex = 280 nm). Fluorescence quantum yields were measured by using a C9920-02 Absolute PL Quantum Yield Measurement System (Hamamatsu Photonics K. K.)45 46 (link)47 .

Ishii A, & Hasegawa M. (2015). An Interfacial Europium Complex on SiO2 Nanoparticles: Reduction-Induced Blue Emission System. Scientific Reports, 5, 11714.

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Characterizing Protein Optical Properties

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All the buffers in this study were treated with chelex-100 column to eliminate trace metal ions in solution. Protein samples were diluted to 0.4, 0.8, 1.2, 1.6 and 2.0 µM in 2x fluorescence buffer and their absorbance spectra were recorded with a Cary 300 Bio UV-Vis spectrophotometer. The absorbance and concentration were fitted into a linear equation and the extinction coefficients (ε) were calculated. Fluorescence measurements were performed in a 96-well plate reader attached to a fluorometer (Fluorolog3-22 and MicroMax 384, Horiba Jobin Yvon). The reference dye sampler kit (Molecular Probes) including Quinine sulfate, Fluorescein, 5-Carboxytetramethylrhodamine, Sulforhodamine 101, and Nile blue perchlorate were used as references in characterizing protein quantum yields (QY). The same concentrations of protein samples and buffer solution were used in measuring quantum yields and emission spectra.

Yu X., Strub M.P., Barnard T.J., Noinaj N., Piszczek G., Buchanan S.K, & Taraska J.W. (2014). An Engineered Palette of Metal Ion Quenchable Fluorescent Proteins. PLoS ONE, 9(4), e95808.

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Comprehensive Spectroscopic Analysis of Compounds

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The NMR spectra were recorded on a Bruker Avance II+ spectrometer operating with frequency 600 MHz for 1 H and 125 MHz for 13 C in DMSO-d 6 . ATR-FTIR spectra of the compounds were recorded on a Bruker Tensor 27 FTIR spectrophotometer in the range of 4400-600 cm -1 а with resolution of 2 cm -1 at room temperature. The external reflection diamond crystal was used and the samples were scanned 128 times. The molecular mass of the compounds was confirmed by a high resolution mass spectrometer Thermo DFS. The UV-VIS spectra were measured on a Jasco V-570 UV-vis-NIR spectrophotometer in spectral grade solvents in the concentration range ~10 -5- mol L -1 . The quantitative analysis of the observed enol⇋ keto equilibria for 5 was performed by using a Fishing-Net algorithm as described elsewhere [46, (link)47] (link). The steady-state fluorescence spectra were recorded with a FluoroLog 3-22 (HORIBA) spectrofluorometer in the range 200-800 nm with a resolution of 0.5 nm and double-grating monochromators using as excitation wavelength a value near the absorption maxima of the dyes with concentrations of ~6 × 10 -6 mol L -1 .

Yordanov D., Deneva V., Georgiev A., Crochet A., Fromm K.M, & Antonov L. (2020). Indirect solvent assisted tautomerism in 4-substituted phthalimide 2-hydroxy-Schiff bases. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 237.

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Photophysical Characterization of Compounds

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Steady-state luminescence
spectra at room temperature and 77 K were measured using a Fluorolog-3-22
instrument from Horiba Jobin-Yvon. Transient absorption and kinetic
emission and absorption measurements were performed on an LP920-KS
instrument from Edinburgh Instruments in MeCN. Excitation source was
a pulsed Quantel Brilliant b ND:YAG laser equipped with a Rainbow
optical parameter oscillator (OPO) with a pulse energy of 13 mJ at
435 nm and 20 mJ at 460 nm. The solutions typically had an optical
density below 0.4 and were deaerated through three cycles of freeze–pump–thaw.
The quantum yields were measured on a Hamamatsu absolute photoluminescence
quantum yield spectrometer C11347 Quantaurus QY with a sample concentration
of 2.5 × 10^–5 M, and the solutions were deaerated
by bubbling Ar for 10 min.

Bens T., Kübler J.A., Walter R.R., Beerhues J., Wenger O.S, & Sarkar B. (2023). Impact of Bidentate Pyridyl-Mesoionic Carbene Ligands: Structural, (Spectro)Electrochemical, Photophysical, and Theoretical Investigations on Ruthenium(II) Complexes. ACS Organic & Inorganic Au, 3(4), 184-198.

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Fluorescence Quenching and FRET Analyses

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The fluorescence self‐quenching and hetero‐FRET studies were carried out by performing both steady‐state and time‐resolved fluorescence measurements of the MLVs containing variable surface concentrations of the fluorescently‐labeled native and recombinant SP‐C protein. Steady‐state measurements were acquired with a Horiba‐Jobin Yvon Fluorolog 3‐22 (Tokyo, Japan) spectrofluorimeter, using 0.5 × 0.5 cm quartz cuvettes. For the time‐resolved fluorescence measurements, a time‐correlated single‐photon timing system was used. Excitation of Marina Blue and BODIPY‐labeled proteins was carried out at 340 nm (using the second harmonic of a secondary dye laser of DCM from Coherent DCM 700 series), and 488 nm (using a ps laser diode from Becker & Hickl [Berlin, Germany] series BPS‐488‐SM), respectively, whereas emission from MB‐ and BODIPY‐labeled proteins was recorded at 455m and 515 nm, respectively. Data analysis was carried out using the TRFA data processor Advanced Version 1.4 from Scientific Software Technologies Center (Belarusian State University, Minsk) (Marquardt, 1963 (link)). The goodness of the fits was judged from the experimental χ² value (χ² < 1.5 indicating adequate fitting), weighted residuals and autocorrelation plots.

Morán‐Lalangui M., Coutinho A., Prieto M., Fedorov A., Pérez‐Gil J., Loura L.M, & García‐Álvarez B. (2024). Exploring protein–protein interactions and oligomerization state of pulmonary surfactant protein C (SP‐C) through FRET and fluorescence self‐quenching. Protein Science : A Publication of the Protein Society, 33(1), e4835.

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