The XRD pattern was measured used a Bruker D8 QUEST. The SEM images were recorded on a SU8000 Schottky field emission scanning electron microscope (SFE-SEM) equipped with a Rontec EDX system. The UV-Vis absorbance spectra were recorded on a Lambda 35 UV-Vis spectrophotometer. X-ray photoelectron spectra (XPS) were recorded on a Thermo Scientific ESCALAB 250 instrument (150 W, spot size of 500 μm and Al Kα radiation at 1486.6 eV) to obtain the surface elements. Photoluminescence (PL) spectroscopy measurement was performed on a Cary Eclipse spectrophotometer.
Eclipse spectrophotometer
Manufactured by Agilent Technologies
Sourced in United States
The Eclipse spectrophotometer is a laboratory instrument designed to measure the absorption or transmission of light by a sample. It is capable of analyzing a wide range of materials, including liquids, solids, and gases. The Eclipse spectrophotometer provides accurate and reliable data for various applications, such as chemical analysis, life science research, and quality control. The core function of this product is to quantify the interaction between light and the sample under investigation.
Automatically generated - may contain errors
Lab products found in correlation
Escalab 250, by Thermo Fisher Scientific (3 mentions)
D8 quest, by Bruker (1 mentions)
Ecx nmr spectrometer, by JEOL (1 mentions)
Uv 2450, by Agilent Technologies (1 mentions)
X ray diffractometer, by Agilent Technologies (1 mentions)
Fluorolog instrument, by Horiba (1 mentions)
Pyris 1, by PerkinElmer (1 mentions)
Jena specord s600 spectrophotometer, by Analytik Jena (1 mentions)
Avance 400 spectrometer, by Bruker (1 mentions)
Lambda 35 uv vis spectrophotometer, by PerkinElmer (1 mentions)
Smart apex 2, by Bruker (1 mentions)
Uv vis spectrophotometer, by Shimadzu (1 mentions)
Qtof 6550 mass spectrometer, by Agilent Technologies (1 mentions)
Ix73 dp73, by Olympus (1 mentions)
Nanoglo assay substrate, by Promega (1 mentions)
Spark 10m plate reader, by Tecan (1 mentions)
Hela cell line, by American Type Culture Collection (1 mentions)
23 protocols using eclipse spectrophotometer
1
Multi-Technique Material Characterization
2
Comprehensive Spectroscopic Characterization
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1H and 13C NMR spectra were recorded on a JEOL ECX NMR spectrometer. FTIR
spectra of neat samples were recorded on a Carry-660 spectrophotometer.
HRMS-electrospray ionization (ESI) spectra were recorded on a Bruker
maXis impact HD instrument. UV–vis and fluorescence spectra
were recorded on a Shimadzu UV-2450 and a Cary Eclipse spectrophotometer,
respectively. Solid-state emission was recorded by preparing a thin
film of compounds on a quartz plate using the drop-cast method. Solvents
and chemicals were purchased from commercial sources and used without
further purification. Spectroscopic grade solvents were used for photophysical
studies. Melting points were recorded using a Stuart melting point
instrument. TGA was performed on a PerkinElmer Pyris 1 and NETZSCH
STA449 F1 Jupiter instrument under a nitrogen atmosphere at a heating
rate of 10 °C per minute. The temperature of degradation (Td) was correlated with a 5% weight loss. SC-XRD
studies were performed on an Agilent Technologies X-ray diffractometer.
3D structure visualization and exploration of crystal packing were
done using Mercury software. The absolute quantum yields (both solid
and solution state) were calculated using an integrating sphere on
a Fluorolog instrument (Horiba Scientific). DCM solutions of compounds
were used to calculate the absolute quantum yield. The lifetime data
were measured on an Agilent lifetime instrument.
spectra of neat samples were recorded on a Carry-660 spectrophotometer.
HRMS-electrospray ionization (ESI) spectra were recorded on a Bruker
maXis impact HD instrument. UV–vis and fluorescence spectra
were recorded on a Shimadzu UV-2450 and a Cary Eclipse spectrophotometer,
respectively. Solid-state emission was recorded by preparing a thin
film of compounds on a quartz plate using the drop-cast method. Solvents
and chemicals were purchased from commercial sources and used without
further purification. Spectroscopic grade solvents were used for photophysical
studies. Melting points were recorded using a Stuart melting point
instrument. TGA was performed on a PerkinElmer Pyris 1 and NETZSCH
STA449 F1 Jupiter instrument under a nitrogen atmosphere at a heating
rate of 10 °C per minute. The temperature of degradation (Td) was correlated with a 5% weight loss. SC-XRD
studies were performed on an Agilent Technologies X-ray diffractometer.
3D structure visualization and exploration of crystal packing were
done using Mercury software. The absolute quantum yields (both solid
and solution state) were calculated using an integrating sphere on
a Fluorolog instrument (Horiba Scientific). DCM solutions of compounds
were used to calculate the absolute quantum yield. The lifetime data
were measured on an Agilent lifetime instrument.
3
Absorption and Emission Spectroscopy of Compound 3
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Absorption spectra were recorded with an Analytik Jena Specord S600 spectrophotometer in Hellma quartz cells 110-QS or 114B-QS (10 mm) with baseline correction at 20 °C. Emission spectra were collected with a Cary Eclipse spectrophotometer equipped with a microplate reader. Emission spectra were measured in Hellma quartz cells 114F-QS (10 mm × 4 mm) at 20 °C and in a UV-Star®, 96 well, μClear®, F-bottom well plate.
Compound3 was synthesized according to published procedure [39 (link)]. All commercially available chemicals were reagent-grade and used without further purification unless otherwise mentioned. Spectroscopic grade solvents were used for solutions submitted to absorption and emission spectroscopy.
Compound
4
Kinetic Inhibition of Plx2A by Flavonoids
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Kinetic inhibition assays were conducted to determine the IC50 values for flavonoid inhibitors and the experiments were conducted on a Cary Eclipse spectrophotometer with an excitation of 305 nm, emission wavelength of 405 nm and bandpasses of 5 nm. Plx2A (5 μmol/L) was mixed with 250 μmol/L ε-NAD+, at various inhibitor concentrations in GH buffer. Triplicate reactions at 25 °C were monitored for 10 min intervals and then the initial slope was calculated for each trace. The kinetic data were fit to a Michaelis–Menten function generated in OriginLab Pro ver8 software to determine the IC50 value. The mechanism of flavonoid inhibition was determined for Quercetin as the model compound and entailed collection of full Michaelis–Menten datasets in the presence of 0, 10, 20, 30, and 40 μmol/L of inhibitor in a final DMSO concentration of 15% (v/v). Plx2A GH activity is not affected by DMSO in the reaction buffer until 20% (v/v). The inhibition data were transformed to the Lineweaver–Burk function and plotted to determine the inhibition pattern. Secondary plots were then generated to calculate the Ki value, which represents the Quercetin binding constant for Plx2A.
5
Characterization of Dye-Loaded Nanoparticles
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All chemicals were purchased from Aladin (China) and Aldrich and were used without further purification. All solvents were of analytical grade and used as received. 1H NMR (400 MHz) was recorded on a Bruker AVANCE 400 spectrometer. The linear absorption and emission spectra of free dye and dye-NPs were recorded by using a spectrophotometer (Lambda 35 UV/vis) and a Cary Eclipse spectrophotometer, respectively. Morphology of the nanoparticles was analyzed by using transmission electron micrograph (TEM).
6
Characterization of Organic Compounds
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NMR spectra were recorded on a Varian VR400-MHz spectrometer with TMS as the internal standard. The melting points of the compounds were determined on a Beijing XT4-100X microscopic melting point apparatus. The UV-Vis spectra were recorded on a Perkin-Elmer Lambda-35 UV-Vis spectrophotometer. Fluorescence spectra were obtained on a Cary Eclipse spectrophotometer at room temperature. The fluorescence image of the HeLa cells was obtained using Olympus FV1300 laser confocal fluorescence microscope. The crystal data were collected by the Bruker Smart-Apex-II instrument. The SEM images were obtained by F250 thermal field emission scanning electron microscope.
7
Determining Protein-DNA Binding Affinity
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The DNA binding affinity of NEQ395 was determined by fluorescence anisotropy titration measurements. The experiments were performed with a Cary Eclipse Spectrophotometer by measuring the fluorescence at 20°C. Oligodeoxynucleotides (50 nM, Table 1 ) used for this assay were labelled with FAM at the 5′-end and binding isotherms obtained by reverse titration of NEQ395. Reactions were caried out in 25 mM Tris/HCl pH 6.5, 1 mM DTT and the protein concentration gradually decreased by replacing 37.5% of the mix in the cuvette with a solution of DNA in the same buffer (1.6x dilution). Fluorophores were excited at 490 nm (10 nm slit width) and the anisotropy was measured by monitoring the emission at 530 nm (10 nm slit width) and an integration time of 2 s. For the calculation of the dissociation constant (KD) the intensity of the bound and unbound labelled DNA was taken into account. At least three measurements per data point were collected and the data fitted with a single-site binding model using the following formula: with (45 (link)).
8
Fluorescence Anisotropy of pKID-KIX Interactions
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FITC-pKID, FITC-KID, and FITC-KID-S133E (1 μM) samples were incubated at 10°C for 30 min in the presence of varying concentrations of KIX. Measurements were performed using a Cary Eclipse Spectrophotometer with a fluorescence polarization accessory. Excitation and emission wavelengths of 495 ± 5 and 515 ± 5 nm, respectively, were used. The sample holder was maintained at 10°C with a Peltier device. Fluorescence anisotropy equilibrium binding experiments and calculations were performed as described previously (34 (link)).
9
DNA-Ligand Fluorescence Binding Assay
10
Fluorescence Characterization of Molecular Probes
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The UV studies were done in the 1800 SHIMADZU UV-vis spectrophotometer at 25 °C. The PL spectra were recorded using a halogen lamp fitted Cary Eclipse spectrophotometer. The slit widths for excitation and emission were kept at 5 nm. Quartz cells were taken for spectral measurements. A fluorescent turn-on, which refers to the increase in the intensity of the PL spectra, or a fluorescent turn-off, which refers to the decrease in the intensity of the PL spectra of the probe on addition of the analytes is checked. Time-resolved photoluminescence (TRPL) study is done using the Edinburg Instruments FSP920, Picosecond Time-resolved cum Steady State Luminescence Spectrometer with an excitation LED source of wavelength 290 nm.
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