The largest database of trusted experimental protocols

F 7000 fluorescence spectrophotometer

Manufactured by Hitachi
Sourced in Japan, United States, United Kingdom

The Hitachi F-7000 fluorescence spectrophotometer is a laboratory instrument designed to measure the fluorescence properties of samples. It is capable of detecting and analyzing the emission spectrum of fluorescent materials. The core function of the F-7000 is to provide accurate and reliable fluorescence data for scientific research and analysis.

Automatically generated - may contain errors

357 protocols using f 7000 fluorescence spectrophotometer

1

NADH Autofluorescence Measurement Protocols

Check if the same lab product or an alternative is used in the 5 most similar protocols
The NADH autofluorescence was measured using two different instruments: (1) Hitachi F-7000 fluorescence spectrophotometer (Hitachi High Technologies, Maidenhead, UK) and (2) the NADH-Module of the NextGen-O2k (Oroboros Instruments, Innsbruck, Austria). The NADH measurements were performed in a Hitachi F-7000 fluorescence spectrophotometer at a 5 Hz acquisition rate, using 340 and 435 nm excitation and emission wavelengths, respectively. The NextGen-O2k allows for the simultaneous measurement of oxygen consumption and NADH autofluorescence, incorporating an ultraviolet (UV) LED with an excitation wavelength of 365 nm and an integrated spectrometer that records a wavelength range between 450 and 590 nm. The light intensity of the LED was set to 10 mA. A half a mg of mouse liver, kidney, or brain, or 0.25 mg of mouse heart mitochondria were suspended in 2 ml incubation medium, the composition of which was identical to that for ΔΨmt determination—as described in [32 (link)]. The experiments were performed at 37 °C.
+ Open protocol
+ Expand
2

Comprehensive material characterization protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols
Powder XRD measurements
were collected with
a Bruker D8 ADVANCE X-ray diffractometer (Bruker AXS Gmbh, Germany)
equipped with graphite-monochromatized Cu/Kα radiation (λ
= 1.5406 Å). The 2θ angle of the diffractometer was stepped
from 5° to 70° at a scan rate of 10°/min. FT-IR spectra
were recorded with a Nicolet 6700 FT-IR spectrometer (Thermo, American).
Zeta potential and hydrodynamic diameter were measured by using a
Zetasizer 3000HS nanogranularity analyzer (Malvern Instruments). Absorption
spectra were obtained by a UV-3900 UV–vis spectrophotometer
(Hitachi, Japan). The CL signal was measured on an ultraweak biophysics
CL (BPCL) analyzer (Institute of Biophysics, Chinese Academy of Science,
Beijing, China). The CL spectrum of this system was measured using
a F-7000 fluorescence spectrophotometer with the assistance of high-energy
cutoff filters from 400 to 540 nm (Hitachi, Japan). The fluorescence
spectra were performed using a F-7000 fluorescence spectrophotometer
(Hitachi, Japan). The slits of emission and excitation are 5.0 nm,
the voltage is 700 V, and the scanning rate is 1200 nm/min. The quantum
yields were measured with a FLS980 transient steady-state fluorescence
spectrometer (Edinburgh, U.K.).
+ Open protocol
+ Expand
3

Multi-Modal Characterization of Luminescent Materials

Check if the same lab product or an alternative is used in the 5 most similar protocols
CL aptitudes were
measured with a BPCL luminescence analyzer (Institute of Biophysics,
Chinese Academy of Sciences, Beijing, China). A F-7000 fluorescence
spectrophotometer (Hitachi, Japan) was used for the photoluminescence
(PL) study, and absorption spectra were recorded by a UV-3900s spectrophotometer
(Hitachi, Japan). Electron spin resonance (ESR) analysis was performed
on a JEOL JES-FA200 ESR spectrometer (ESP-300E, Bruker, Japan). Mass
spectrometry was performed on MALDI-TOF-MS (Shimadzu Biotech Axima,
Japan). Electrochemical measurements were carried out using a Zahner
IM6 potentiostat (Zahner Elektrik GmbH & Co. KG-Kronach, Germany).
The CL spectra were recorded by a F-7000 fluorescence spectrophotometer
(Hitachi, Japan) at a closed light source in a flow cell connected
to peristaltic pumps.
+ Open protocol
+ Expand
4

Cysteine-Stabilized Fluorescent Iron Oxide Nanoparticles

Check if the same lab product or an alternative is used in the 5 most similar protocols
All chemicals and reagents used in this work were AR grade 1 unless noticed and purchased from Sigma-Aldrich Chemical Corporation, including HAuCl4, L-cysteine (L-Cys) and anhydrous FeCl3. Other inorganic chemicals were purchased from Tianjin Chemical Corporation. Solvent water was purified and obtained from Millipore. All glassware was first treated with aqua regia at 40°C and then washed with purified water. XPS and DLS experiments were carried out by a PHI-5000 Versaprobe III X-ray photon–electron spectrophotometer (ULVCA-PHI, United States) and a Malvern Zetasizer Nano ZS90 laser particle size and zeta potential analyzer (Trek, Taiwan). IR spectra were recorded using a Bruker Vertex 70 FTIR spectrometer. The TEM image was obtained with a JEM-2010 transmission electron microscope (JEOL, Japan). UV-vis absorption spectra were obtained using a Shimadzu UV-3101PC spectrophotometer and a Biotek ELx800 automatic enzyme-linked immunosorbent assay. Emission spectra were recorded using a Hitachi F-7000 fluorescence spectrophotometer (Xe lamp). Emission quantum yield was determined by using this Hitachi F-7000 fluorescence spectrophotometer with the help of an integrating sphere. The reference was quinine sulfate (20 μM) in diluted H2SO4 (0.1 M). The emission lifetime was measured with a TEKTRONIX TDS-3052 oscilloscope (excited by an optical parametric oscillator).
+ Open protocol
+ Expand
5

Quantifying Luminescence Efficiency and Decay

Check if the same lab product or an alternative is used in the 5 most similar protocols
The PL and PLE spectra were recorded at 1 nm intervals at RT using a F7000 fluorescence spectrophotometer (Hitachi High-Tech, Japan). For PL measurements, slits of 2.5 nm were used for both excitation and emission. The absolute quantum efficiencies, also known as QYs, of the glasses were measured using a Quantaurus-QY integrating sphere spectrometer (Hamamatsu Photonics, Japan). The error bars were ± 2. The emission decay was measured at RT using a Quantaurus-Tau system (Hamamatsu Photonics, Japan) with a 340 nm LED. The accumulated counts for evaluation were 50,000.
+ Open protocol
+ Expand
6

Comprehensive Analytical Techniques for Materials

Check if the same lab product or an alternative is used in the 5 most similar protocols
1H NMR spectra
were measured using an Avance III HD 400 (Bruker Japan K. K., Kanagawa,
Japan) at 400 MHz and JNM-ECA500 (JEOL Ltd., Tokyo, Japan) at 500
MHz at 298 K. All pH values were recorded using a Horiba F-52 pH meter
(HORIBA, Ltd., Kyoto, Japan). UV–vis absorption spectra were
measured using a 10 mm quartz cell and a Jasco V-760 UV–vis
spectrophotometer (JASCO Corporation, Tokyo, Japan) equipped with
a Peltier thermocontroller. Fluorescence spectra were measured using
a 10 mm quartz cell and a HITACHI F-7000 fluorescence spectrophotometer
(Hitachi High-Technologies, Co., Tokyo, Japan) equipped with a Peltier
thermocontroller. DLS measurements were carried out at 25 °C
using a Zetasizer Nano ZS (Malvern Instruments Ltd., Malvern, Worcestershire,
UK).
+ Open protocol
+ Expand
7

Cell Viability Assay with Gefitinib

Check if the same lab product or an alternative is used in the 5 most similar protocols
Cells were seeded in a 96-well plate at a density of 5 × 103 cells per well. After 24 h of incubation, cells were treated with various concentrations of gefitinib (0, 0.01, 0.1, 1, 10, and 100 μM) for 48 h, then 10 μL of CCK-8 solution (Dojindo Molecular Technologies, Japan) was added and incubated for an additional 4 h. The absorbance was measured at 450 nm with a Hitachi F-7000 fluorescence spectrophotometer (Hitachi High-Tech, Japan).
+ Open protocol
+ Expand
8

Thioflavin T Fluorescence Protein Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
ThT fluorescence was recorded using F-7000 fluorescence spectrophotometer (Hitachi High-Technologies Corporation) with fluorescence excitation at 412 nm and emission at 485 nm. Protein solution was dissolved in 50 mM Tris-HCl pH 7.4, 150 mM NaCl buffer incubated for 2 h at 37 °C heat followed by 2 h at 25 °C. Readings were taken from samples after incubating 20 μM of induced and control protein solution with 20 μM of ThT for 15 min. Three independent measurements were performed and subsequently averaged for each sample.
+ Open protocol
+ Expand
9

Fluorescence Spectroscopy of Exfoliated TMDs

Check if the same lab product or an alternative is used in the 5 most similar protocols
Fluorescence measurements were carried out with an F-7000 fluorescence spectrophotometer from Hitachi High-Technologies Co. (Tokyo, Japan) equipped with a 1.0 cm quartz cuvette. The solvent-assisted exfoliation of the TMDs was done with a Transonic 570/H ultrasonic bath supplied by Elma Schmidbauer GmbH (Singen, Germany). The subsequent step to obtain a TMD suspension was performed with a centrifuge Rotofix 32A purchased from Hettich GmbH & Co.KG (Tuttlingen, Germany).
+ Open protocol
+ Expand
10

Optical Characterization of Glass Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
The PL and PLE spectra were recorded at 1 nm intervals at RT using an F7000 fluorescence spectrophotometer (Hitachi High-Tech. Japan). Band pass filters of 2.5 nm for the PL measurement were used for both excitation and emission. The absorption spectra at RT were recorded at 1 nm intervals using a U3500 UV-vis-NIR spectrometer (Hitachi High-Tech. Japan). The absolute quantum efficiencies, also known as quantum yields (QYs), of the glasses were measured using an integrating sphere Quantaurus-QY (Hamamatsu Photonics, Japan). The error bars were ±2. The emission decay at RT was measured using a Quantaurus-Tau system (Hamamatsu Photonics, Japan) with a 340 nm LED. The accumulated counts for evaluation were 50,000. Scintillation (radioluminescence) spectra were measured by using a CCD-based spectrometer (Andor DU920P CCD and SR163 monochromator) under X-ray exposure23 (link). The supplied bias voltage and tube current were 40 kV and 0.52 ~ 5.2 mA, respectively.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!