The crystal structures of luminescent material samples were characterized by an X-ray diffractometer (XRD, Cu-Kα: λ = 1.542 Å, D8 Advance, German). Transmission electron microscope (TEM) images were obtained from JEOl 2100 transmission electron microscope operated at an acceleration voltage of 200 kV. The optical properties of absorption were measured using an ultraviolet-visible diffuse reflectance spectrophotometer (UV-vis DR, Hitachi U-4100, Japan). Photoluminescence spectra including emission and excitation spectra were obtained using a Hitachi F-7000 spectrophotometer equipped with InGaAs as the detector with both continuous (150 W, Hitachi F7000, Japan) and pulsed xenon lamps. All the measurements were performed at room temperature.
F 7000
Manufactured by Hitachi
Sourced in Japan, United States, China
The Hitachi F-7000 is a high-performance fluorescence spectrophotometer designed for versatile laboratory applications. It features advanced optics and a sensitive detector to provide accurate and reliable measurements of fluorescence intensity.
Automatically generated - may contain errors
Lab products found in correlation
Escalab 250xi, by Thermo Fisher Scientific (14 mentions)
Escalab 250, by Thermo Fisher Scientific (12 mentions)
D8 advance, by Bruker (11 mentions)
Uv 3600, by Shimadzu (9 mentions)
S 4800, by Hitachi (8 mentions)
Uv 2600, by Shimadzu (6 mentions)
Uv 1800, by Shimadzu (6 mentions)
Nicolet 6700, by Thermo Fisher Scientific (6 mentions)
Miniflex 600, by Rigaku (5 mentions)
U 3900, by Hitachi (5 mentions)
Jem 2100f, by JEOL (5 mentions)
Jem 2100, by JEOL (5 mentions)
Tensor 27, by Bruker (4 mentions)
Lambda 35, by PerkinElmer (4 mentions)
U 4100, by Hitachi (4 mentions)
Fls920, by Edinburgh Instruments (4 mentions)
Uv 2450, by Shimadzu (4 mentions)
Cary 5000, by Agilent Technologies (4 mentions)
K alpha, by Thermo Fisher Scientific (4 mentions)
Fls980, by Edinburgh Instruments (3 mentions)
493 protocols using f 7000
1
Characterization of Luminescent Materials
2
Probing Porphyrin-DNA Interactions
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
UV–vis
spectrophotometer (UV-1800, SHIMADZU, Japan) and fluorescence spectrophotometer
(F-7000, HITACHI, Japan) were used to investigate the interaction
between DNA and the free base porphyrin and its metalloderivatives.
The progress of the interaction between DNA and porphyrins was monitored
by observing the changes in the absorbance of the relevant metalloporphyrin
upon the addition of DNA. For example, the absorbances for [H2TMPyP]4+, [Co(II)TMPyP]4+, and [Zn(II)TMPyP]4+ have been measured at 422, 438, and 437 nm, respectively.
A fluorescence spectrophotometer (F-7000, Hitachi, Japan) was also
employed to investigate the interactions of DNA with the porphyrins.
The fluorescence spectra were recorded by setting the fluorescence
excitation wavelength at 433, 448, and 449 nm for [H2TMPyP]4+, [Co(II)TMPyP]4+, and [Zn(II)TMPyP]4+, respectively, because the isosbestic points of the binary system
of free base porphyrin-DNA and metalloporphyrin-DNA were observed
at those wavelengths. The wavelengths of emission were maintained
at 550–800 nm.
spectrophotometer (UV-1800, SHIMADZU, Japan) and fluorescence spectrophotometer
(F-7000, HITACHI, Japan) were used to investigate the interaction
between DNA and the free base porphyrin and its metalloderivatives.
The progress of the interaction between DNA and porphyrins was monitored
by observing the changes in the absorbance of the relevant metalloporphyrin
upon the addition of DNA. For example, the absorbances for [H2TMPyP]4+, [Co(II)TMPyP]4+, and [Zn(II)TMPyP]4+ have been measured at 422, 438, and 437 nm, respectively.
A fluorescence spectrophotometer (F-7000, Hitachi, Japan) was also
employed to investigate the interactions of DNA with the porphyrins.
The fluorescence spectra were recorded by setting the fluorescence
excitation wavelength at 433, 448, and 449 nm for [H2TMPyP]4+, [Co(II)TMPyP]4+, and [Zn(II)TMPyP]4+, respectively, because the isosbestic points of the binary system
of free base porphyrin-DNA and metalloporphyrin-DNA were observed
at those wavelengths. The wavelengths of emission were maintained
at 550–800 nm.
3
Fluorescence Spectroscopy of ELP-TEMP
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
We performed fluorescence spectroscopy measurements by an FP-750 spectrofluorometer (JASCO) equipped with a temperature controller unit (ETC-272T, JASCO). We diluted proteins in a PBS solution (T900, Takara Bio) and loaded into a quartz cuvette. We took 5 min to wait for temperature equilibration at each temperature point before starting measurement. The excitation wavelength was 430 nm.
To investigate the effect of macromolecular crowding, we dissolved ELP-TEMP in a PBS solution containing Ficoll PM70 (F2878, Sigma-Aldrich). To examine the effect of salts, we added CaCl2, MgCl2, or 1 mM EDTA to a PBS solution, where 1 mM EDTA was used to achieve the condition of 0 mM CaCl2 or MgCl2. For NaCl and KCl, we added a salt to a 10 mM sodium phosphate buffer (pH 7.4). For pH dependence measurement, we prepared a mixture of 30 mM trisodium citrate and 30 mM borax adjusted to pH 8.0, 7.0, 6.0, and 5.0 by adding HCl.
To measure the fluorescence of ELP-TEMP in a cell suspension, we suspended ~ 5 million HeLa cells expressing ELP-TEMP in 0.5 mL of a PBS solution, and measured the fluorescence by a fluorescence spectrophotometer (F-7000, Hitachi-Hightech). For background correction, we measured the baseline from a suspension containing ~ 5 million untransfected HeLa cells. The excitation wavelength was 430 nm.
To investigate the effect of macromolecular crowding, we dissolved ELP-TEMP in a PBS solution containing Ficoll PM70 (F2878, Sigma-Aldrich). To examine the effect of salts, we added CaCl2, MgCl2, or 1 mM EDTA to a PBS solution, where 1 mM EDTA was used to achieve the condition of 0 mM CaCl2 or MgCl2. For NaCl and KCl, we added a salt to a 10 mM sodium phosphate buffer (pH 7.4). For pH dependence measurement, we prepared a mixture of 30 mM trisodium citrate and 30 mM borax adjusted to pH 8.0, 7.0, 6.0, and 5.0 by adding HCl.
To measure the fluorescence of ELP-TEMP in a cell suspension, we suspended ~ 5 million HeLa cells expressing ELP-TEMP in 0.5 mL of a PBS solution, and measured the fluorescence by a fluorescence spectrophotometer (F-7000, Hitachi-Hightech). For background correction, we measured the baseline from a suspension containing ~ 5 million untransfected HeLa cells. The excitation wavelength was 430 nm.
4
Assaying Cellular Oxidative Stress and Lipid Peroxidation
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
OS cells, with or without applied genetic modifications, were placed onto 12-well plates at 0.5 × 105 cells per well and cultivated for indicated time periods. Cells were then washed once with PBS and stained with the applied fluorescence dyes (DCF-DA or CellROX, dissolved in the medium). After extensive washes, fluorescence images were visualized under a fluorescence microscopy (Leica), and its intensity was detected by a fluorescence spectrophotometer (F-7000, Hitachi-Hightech). A thiobarbituric acid reactive substances (TBAR) activity assay kit was employed to examine cellular lipid peroxidation levels using the protocol described [21 (link), 22 (link)].
5
Fluorescent Lanthanide Labeling of Cells
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Excitation and emission spectra of the cell sample were measured with a fluorescence spectrophotometer (F7000, Hitachi High-Technologies). Briefly, MCF-7 cells were detached from the culturing dish with trypsin-EDTA (201-16945, Wako Chemicals), permeabilized and fixed with 95% ethanol, and immersed in a buffer solution containing Tb3+ at the concentration of 10 mM. The cell suspension was then put in a quartz cuvette containing a rotating microstirrer, and emission and excitation spectra of the cell suspension was acquired. As a reference, the buffer solution containing Tb3+ at the concentration of 10 mM was also measured.
6
Fluorescence Spectroscopy of Cellular Probes
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Fluorescence intensity was measured with a spectrofluorimeter model F7000 (Hitachi High Technologies America, Schaumburg, IL) equipped with a high-sensitivity cell holder using excitation and emission slit widths of 5 nm and integration time of 10 s. Additionally, light scattering was monitored by setting both the excitation and emission wavelength to 400 nm. We used the following excitation and emission wavelengths to measure the intensity of individual probes: TOE, λex/λem = 284/335 nm; DHE, λex/λem = 327/393; and TFPC, λex/λem = 500/520 nm. FRET was measured as sensitized acceptor emission upon donor excitation using the following wavelength combinations: TOE/DHE, λex/λem = 284/393; and DHE/TFPC, λex/λem = 327/520 nm.
7
Determining Enzyme Kinetics by pNPB Hydrolysis
8
Antiport Activity Assay for Cation Transport
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Na+(Li+, K+)/H+ antiport activity assays were performed as previously described (Bassilana et al., 1984 (link); Nakamura et al., 1986 (link); Goldberg et al., 1987 (link)). Everted vesicles containing approximately 100 μg of total membrane protein were added into a 2 ml reaction buffer containing 140 mM choline chloride, 250 mM sucrose, 1 μM acridine orange and 10 mM BTP/HCl adjusted to the indicated pH. Respiration-dependent formation of ΔpH was initiated by the addition of 10 mM Tris-D-lactate, which resulted in the quenching of acridine orange fluorescence. Antiport activity was estimated from the dequenching percentage after the addition of NaCl, LiCl or KCl at the final concentration of 5 mM. Fluorescence was measured with a fluorescence spectrophotometer F-7000 (Hitachi High-Technologies, Japan) with excitation at 490 nm and emission at 530 nm. The apparent affinity of the antiporter for the cations was estimated through the calculation of K0.5 values, which were obtained by fitting the antiport activity as the functions of corresponding cation concentrations followed by non-linear regression analysis using the software Prism 7.0.
9
Comprehensive Characterization of N-CQDs
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Transmission electron microscope (TEM) images were collected from a Tecnai G2 20 transmission electron microscope (FEI company, USA). A transient fluorescence spectrometer (FLS 980, Edinburgh Instruments, UK) was used for analysis of fluorescence lifetime. A fluorescence spectrophotometer (F-7000, Hitachi High-Tech, Japan) was used for fluorescence intensity detection. An atomic absorption spectrometer (TAS990AFG, Beijing Purkinje General, China) was used to detect Ag+ by the Chinese standard method GB 11907-89. The characterization and structure of N-CQDs were measured by Fourier-transform infrared spectroscopy (FT-IR: TENSOR-27, Bruker, Germany). X-ray photoelectron spectroscopy (XPS) measurements were recorded using an ESCALAB 250XI (Thermo Fisher Scientific, USA). Elemental analysis was carried out by an Organic Elemental Analyzer (Elementar Vario EL Ⅲ, Elementar, Germany).
10
Comprehensive Characterization of OACT Materials
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The morphology was observed using a scanning electron microscope (SEM; S-4800, Hitachi High-Technologies Co., Hitachi, Japan). The pore volumes of OACT and OACT@ASO were determined by means of a pore analyzer (BELSORP-max, MicrotracBEL, Osaka, Japan) through the Barrett-Joyner-Halenda (BJH) method. The structure and chemical state were analyzed using a Fourier transform infrared (FTIR) spectrometer (NEXUS-670, Nicolet Co., Thermo Fisher Scientific, Waltham, MA, USA) and a TTRIII X-ray diffractometer (XRD; D/max-2550VB/PC, Rigaku Co., Hitachi, Japan). Thermal gravimetric analysis (TGA) and differential thermal analysis (DTA) were studied using a thermogravimetric analyzer (DSCQ2000, TA Co., Newcastle, DE, USA). Fluorescence EEM measurements were conducted using a Fluorescence spectrophotometer (F-7000, Hitachi High-Technologies Co., Hitachi, Japan). The CCP concentrations were measured by an inductively coupled plasma-optical emission spectrometer (ICP-OES; ICAP7200, Thermo Fisher Scientific, Waltham, MA, USA). The concentration of FA was detected on a UV-vis spectrophotometer (UV-1900i, Shimadzu Corp., Kyoto, Japan) at 282 nm.
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
Revolutionizing how scientists
search and build protocols!