Fluorescence spectra were recorded using an RF-5301 PC fluorometer (Shimadzu, Kyoto, Japan) equipped with an R955 photomultiplier tube detector (Hamamatsu Photonics K.K., Hamamatsu City, Japan). Following excitation at 488 nm, emission spectra were obtained in the regions of 500–700 nm, at sampling intervals of 1 nm. Spectra were normalized to the wavelength of 592 nm [42 (link)].
Rf 5301pc fluorometer
Manufactured by Shimadzu
Sourced in Japan
The RF-5301PC fluorometer is a versatile laboratory instrument used for the measurement and analysis of fluorescent samples. It is designed to provide accurate and reliable fluorescence data for a wide range of applications. The core function of the RF-5301PC is to excite fluorescent molecules and detect the resulting emission, allowing researchers to obtain valuable insights about the composition and properties of their samples.
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Lab products found in correlation
R955 photomultiplier tube detector, by Hamamatsu Photonics (2 mentions)
Zetaplus apparatus, by Brookhaven Instruments (2 mentions)
Uv 1800 spectrophotometer, by Shimadzu (2 mentions)
Ac lehd afc, by Bachem (1 mentions)
Deltaflex, by Horiba (1 mentions)
Cary 100 bio uv visible spectrophotometer, by Agilent Technologies (1 mentions)
2010 lcms system, by Shimadzu (1 mentions)
Corm 3, by Merck Group (1 mentions)
7820a system, by Agilent Technologies (1 mentions)
Corm a1, by Merck Group (1 mentions)
Victor2, by PerkinElmer (1 mentions)
Corm 2, by Merck Group (1 mentions)
Hemoglobin, by Sangon (1 mentions)
Guanidine hydrochloride, by Merck Group (1 mentions)
Ovalbumin (ova), by Merck Group (1 mentions)
Mos 500 circular dichroism spectrometer, by Bio-Logic (1 mentions)
Tecnai g2 twin microscope, by Thermo Fisher Scientific (1 mentions)
Glutathione (gsh), by Sangon (1 mentions)
Hydrogen tetrachloroaurate 3, by Merck Group (1 mentions)
Bovine serum albumin (bsa), by Merck Group (1 mentions)
9 protocols using rf 5301pc fluorometer
1
Fluorescence Spectra Acquisition Protocol
2
Quantifying Apoptosis in Tumor Samples
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Apoptosis in tumors was analyzed by detection of caspase activity, which was measured by cleavage of specific fluorogenic substrates: Ac-DEVD-7-amino-4-trifluoromethyl coumarine (afc) (Bachem, Heidelberg, Germany) for caspase-3, Ac-LETD-afc (Alexis, Grünberg, Germany) for caspase-8 and Ac-LEHD-afc (Bachem) for caspase-9. After homogenization of tumors, corresponding fluorogenic substrate was added. Fluorescence intensity was measured in a Shimadzu RF-5301PC fluorometer. Caspase activity was calculated from the slope as fluorescence units/mg protein/minute of reaction time and converted to picomoles of substrate cleaved/mg protein/minute based on a standard curve for afc.
3
Characterization of Nanomaterial Properties
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Fluorescence spectra were recorded on a Shimadzu RF-5301PC fluorometer. Fluorescence decays were collected on a HORIBA DeltaFlex modular fluorescence lifetime system with an excitation pulse at 520 nm. The absolute photoluminescence quantum yield (PLQY) was obtained by a time-correlated single photon counting spectrometer in combination with a FLS980 Edinburgh fluorescence spectrometer. UV-vis spectra measurement was performed on a Shimadzu UV-1800 spectrophotometer. Transmission electron microscopy (TEM) images were obtained by a FEI-TECNAI G2 microscope operating at 200 kV. Dynamic light scattering and zeta-potential results were accessed on a Brookhaven ZetaPlus apparatus. The energy electron spectroscopy (EDS) pattern was recorded on the AMETEK SEM-associated EDAX GENSIS energy dispersive spectroscopy. Fourier transform infrared (FTIR) spectra were collected with a Nicolet is 50 FTIR spectrometer scanning over the frequency range of 4000 to 400 cm−1 The fluorescence images were obtained with a reflected fluorescence microscope system with a digital camera DP80 from Olympus. The absorbance for MTT assay was recorded by a Molecular Devices SpectraMax Reader.
4
Orai1 N-terminus Cholesterol Binding Assay
5
Synthetic Protocols and Characterization
6
Fluorescence Spectra Acquisition
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Fluorescence spectra were recorded using an RF-5301 PC fluorometer (Shimadzu, Kyoto, Japan) equipped with an R955 photomultiplier tube detector (Hamamatsu Photonics K.K., Hamamatsu City, Shizuoka Pref.430-8587, Japan). Following excitation at 340, 365, or 488 nm, emission spectra were obtained in the regions of 360–660, 380–660, and 500–700 nm, respectively, at sampling intervals of 1 nm.
7
Spectroscopic Characterization of Gold Nanoparticles
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Hydrogen
tetrachloroaurate(III) (≥99.9%), HSA, BSA, ovalbumin, lipase
and guanidine hydrochloride were purchased from Sigma. GSH, hemoglobin,
horseradish peroxidase, lysozyme, RNase A, carbonic anhydrase, immunoglobulin
G, trypsin, and BCA kit were purchased from Sangon Biotech. Phosphate
buffers (20 mM) with pH 4.0, 5.0, 6.0, 7.0, 8.0, and 9.0 were prepared
by mixing solutions of Na2HPO4 (20 mM) and NaH2PO4 (20 mM). The buffer pH was tuned by HCl/NaOH
solution.
Luminescence study was performed on a Shimadzu RF-5301PC
fluorometer. Time-resolved luminescence spectra were measured on an
Edinburgh FS 920 fluorometer. UV–vis spectra measurement was
performed on a Shimadzu UV-1800 spectrophotometer. TEM micrographs
were obtained by a FEI Tecnai G2-Twin microscope. XPS were obtained
using an ESCALAB-MKII spectrometer. CD spectra were carried out on
a Bio-Logic MOS 500 circular dichroism spectrometer. Secondary structural
contents were calculated by using the Dicro 2000 program. DLS and
ζ-potential measurement were performed on a Brookhaven ZetaPlus
apparatus.
tetrachloroaurate(III) (≥99.9%), HSA, BSA, ovalbumin, lipase
and guanidine hydrochloride were purchased from Sigma. GSH, hemoglobin,
horseradish peroxidase, lysozyme, RNase A, carbonic anhydrase, immunoglobulin
G, trypsin, and BCA kit were purchased from Sangon Biotech. Phosphate
buffers (20 mM) with pH 4.0, 5.0, 6.0, 7.0, 8.0, and 9.0 were prepared
by mixing solutions of Na2HPO4 (20 mM) and NaH2PO4 (20 mM). The buffer pH was tuned by HCl/NaOH
solution.
Luminescence study was performed on a Shimadzu RF-5301PC
fluorometer. Time-resolved luminescence spectra were measured on an
Edinburgh FS 920 fluorometer. UV–vis spectra measurement was
performed on a Shimadzu UV-1800 spectrophotometer. TEM micrographs
were obtained by a FEI Tecnai G2-Twin microscope. XPS were obtained
using an ESCALAB-MKII spectrometer. CD spectra were carried out on
a Bio-Logic MOS 500 circular dichroism spectrometer. Secondary structural
contents were calculated by using the Dicro 2000 program. DLS and
ζ-potential measurement were performed on a Brookhaven ZetaPlus
apparatus.
8
Fluorescence Spectroscopy of Solid and Thin Film Samples
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The fluorescence spectra
of both powder solid samples and spin-coated films were collected
using an RF-5301PC fluorometer (Shimadzu, Kyoto, Japan). The powdered
samples were sandwiched between two quartz slides. A solid sample
holder was used to hold the sample slides. The excitation wavelength
of 332 nm with an emission wavelength range of 332–550 nm was
selected. The excitation and emission slit widths of 5 and 1.5, respectively,
and a 0.2 nm scanning interval with an autoresponse time were chosen.
All fluorescence spectra were collected at a high sensitivity setting.
of both powder solid samples and spin-coated films were collected
using an RF-5301PC fluorometer (Shimadzu, Kyoto, Japan). The powdered
samples were sandwiched between two quartz slides. A solid sample
holder was used to hold the sample slides. The excitation wavelength
of 332 nm with an emission wavelength range of 332–550 nm was
selected. The excitation and emission slit widths of 5 and 1.5, respectively,
and a 0.2 nm scanning interval with an autoresponse time were chosen.
All fluorescence spectra were collected at a high sensitivity setting.
9
Synthesis and Characterization of Novel Compounds
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Chemical reagents were purchased
from Sigma-Aldrich (Saint Louis, MO) and/or Oakwood (Estill, SC).
Solvents were purchased from Fisher Scientific (Pittsburgh, PA), and
dry solvents were prepared by a Vigor Tech purification system (Houston,
TX). Certificated pure CO calibration gas was purchased from GASCO
(Oldsmar, FL). UV–vis absorption spectra were obtained by using
a Shimadzu PharmaSpec UV-1700 UV–visible spectrophotometer
(Kyoto, Japan). Fluorescence spectra were recorded on a Shimadzu RF5301PC
fluorometer (Kyoto, Japan). 1H NMR (400 MHz) and 13C NMR (101 MHz) were acquired with a Bruker AV-400 MHz Ultra Shield
NMR. Crystal data were acquired by the Emory Crystallography Center.
from Sigma-Aldrich (Saint Louis, MO) and/or Oakwood (Estill, SC).
Solvents were purchased from Fisher Scientific (Pittsburgh, PA), and
dry solvents were prepared by a Vigor Tech purification system (Houston,
TX). Certificated pure CO calibration gas was purchased from GASCO
(Oldsmar, FL). UV–vis absorption spectra were obtained by using
a Shimadzu PharmaSpec UV-1700 UV–visible spectrophotometer
(Kyoto, Japan). Fluorescence spectra were recorded on a Shimadzu RF5301PC
fluorometer (Kyoto, Japan). 1H NMR (400 MHz) and 13C NMR (101 MHz) were acquired with a Bruker AV-400 MHz Ultra Shield
NMR. Crystal data were acquired by the Emory Crystallography Center.
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