F 2500 fluorescence spectrometer

Manufactured by Hitachi

Sourced in Japan

The F-2500 fluorescence spectrometer is an analytical instrument designed for the measurement of fluorescence phenomena. It features a high-intensity xenon lamp as the excitation light source and a monochromator system to select specific wavelengths. The spectrometer is capable of recording excitation and emission spectra.

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Lab products found in correlation

Vector 22 ft ir spectrophotometer, by Bruker (2 mentions) Jem 2100hr transmission electron microscope, by JEOL (1 mentions) D8 advance, by Bruker (1 mentions) Evolution 350 uv vis spectrophotometer, by Thermo Fisher Scientific (1 mentions) Spectrum 100 spectrometer, by PerkinElmer (1 mentions) Synergy ht, by Agilent Technologies (1 mentions) Tensor 27 fourier transform infrared spectrometer, by Bruker (1 mentions) Ix81 confocal laser scanning microscope, by Olympus (1 mentions) Uv 3310 spectrophotometer, by Hitachi (1 mentions) Lambda 35, by PerkinElmer (1 mentions) Uv 2700 uv vis spectrophotometer, by Shimadzu (1 mentions) Nano zs90, by Malvern Panalytical (1 mentions) Mos 500 cd spectrometer, by Bio-Logic (1 mentions) Tskgel g2000swxl, by Tosoh (1 mentions)

Spelling variants of this product

F-2500 (145 citations) Fluorescence spectrometer (7 citations) F-2500 spectrometer (4 citations)

10 protocols using f 2500 fluorescence spectrometer

Calcein Release Assay for Membrane Disruption

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Membrane activity of the designed polypeptides was characterized by monitoring the increase of fluorescence intensity upon leakage of the self-quenched calcein (75 mM) to the surrounding medium of the liposomes. Then, the EggPC liposomes (2.0 mM) were mixed and incubated with polypeptide samples. The fluorescence of the released calcein was measured using a HITACHI F-2500 fluorescence spectrometer at a 488 nm/520 nm excitation/emission wavelengths. The maximum release (100%) was achieved by the addition of Triton X-100 (0.5% final concentration).
For investigating a detailed pH dependence of the rLPE-St anchoring liposomes, 0.1 mL of the calcein (75 mM) contained liposome solution (pH 10.0) was added to a 2.9 mL of 100 mM phosphate buffer at the desired pH (8.5, 8.0, 7.5, 7.4, 7.0, 6.5, 6.0, 5.5, 5.0). The fluorescence of the released calcein was measured using a HITACHI F-2500 fluorescence spectrometer at a 488/520 nm excitation/emission wavelengths. The maximum release (100%) was achieved by the addition of Triton X-100 (0.5% final concentration).
The percentage of calcein leakage was calculated as follows: calcein leakage % = (F -F 0 )/(F t -F 0 ) × 100, in which F and F t represent the fluorescence intensity of calcein before and after the addition of Triton X-100, respectively, and F 0 represents is the initial fluorescence before the addition of lytic polypeptides.

Kashiwada A., Namiki K., & Mori H. (2020). Design and Construction of pH-Selective Self-Lytic Liposome System. Processes, 8(12), 1526-1526.

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Nanomaterial Characterization by Advanced Microscopy

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The images of transmission electron microscopy (TEM) were recorded on a JEM-2100 (HR) transmission electron microscope (JEOL, Tokyo, Japan). The images of scanning electron microscopy (SEM) were recorded on a S4800 transmission electron microscope (JEOL, Japan). FT-IR spectra were recorded on a Spectrum 100 spectrometer (Perkin Elmer, Waltham, MA, USA). Powder X-ray diffraction (PXRD) patterns were recorded on a Bruker D8 Advance X-ray diffractometer using Cu Kα radiation at 40 mA and 40 kV. UV-vis absorption and fluorescence spectra were recorded using an Evolution 350 UV-vis spectrophotometer (Thermo, USA) and an F-2500 fluorescence spectrometer (Hitachi, Tokyo, Japan), respectively.

Yao C.X., Dong L., Yang L., Wang J., Li S.J., Lv H., Ji X.M., Liu J.M, & Wang S. (2022). Integration of Metal-Organic Frameworks with Bi-Nanoprobes as Dual-Emissive Ratiometric Sensors for Fast and Highly Sensitive Determination of Food Hazards. Molecules, 27(7), 2356.

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Characterization of Nanoparticle Synthesis

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The size and shape of the as-prepared products were characterized by transmission electron microscopy (TEM) (2010 FEF, JEOL, Japan) with an attached energy-dispersive X-ray spectroscope (EDS). Powder X-ray diffraction (XRD) patterns of the dried powders were measured on a Siemens D5005 X-ray powder diffractometer (Bruker, Germany) at a scanning rate of 1° min⁻¹ in the 2θ range from 20° to 70°. Fourier transform infrared (FT-IR) spectra (4000–400 cm⁻¹) were carried out by using a Vector 22 FT-IR spectrophotometer (Bruker, Germany). Fluorescence spectra were performed on an F-2500 Fluorescence spectrometer (Hitachi, Japan) equipped with an external 980 nm laser (Beijing Viasho Technology Co.) instead of internal excitation source. The datas of zeta potential were got on a ZS 90 zeta potentiometer (Malvern, UK). The picture was drawn by Origin 8.

Wang K., Li Y., Li H., Yin M., Liu H., Deng Q, & Wang S. (2019). Upconversion fluorescent nanoparticles based-sensor array for discrimination of the same variety red grape wines. RSC Advances, 9(13), 7349-7355.

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Multimodal Characterization of Nanomaterials

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FT-IR spectra were collected on a Bruker Tensor-27 Fourier transform infrared spectrometer (Bruker, Germany). UV-visible absorption spectra were detected by a Hitachi UV-3310 spectrophotometer (Tokyo, Japan). Fluorescence intensities were measured by a Hitachi F-2500 fluorescence spectrometer (Tokyo, Japan). X-ray photoelectron spectroscopy (XPS) measurements were recorded on an ESCALab220i-XL (VG, England). Zeta potential was conducted on a Zetasizer nano ZS (ZEN3600) instrument (Malvern, England). The absorbance for MTT reduction assay was recorded with a microplate reader (BIO-TEK Synergy HT, USA) at 570 nm. Cell imaging was recorded by Olympus IX81 confocal laser scanning microscope. All measurements were performed at room temperature.

Zhang X., Gao Q., Zhuang Q., Zhang L., Wang S., Du L., Yuan W., Wang C., Tian Q., Yu H., Zhao Y, & Liu Y. (2021). A dual-functional nanovehicle with fluorescent tracking and its targeted killing effects on hepatocellular carcinoma cells. RSC Advances, 11(18), 10986-10995.

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Comprehensive Characterization of GQDs and their Bioconjugates

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GQDs and their bioconjugates were characterized by spectrophotometeric techniques such as transmission electron microscopy (TEM), Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), and zeta potential. The optical studies were investigated by PL and UV–visible spectroscopy. PL was recorded on F-2500 Fluorescence spectrometer (Hitachi Ltd., Tokyo, Japan). UV/Vis absorption spectra were obtained on Lambda 35 (PerkinElmer Inc., Waltham, MA, USA) spectrometer. TEM (JEOL, Tokyo, Japan) was employed for analysis of morphology of the prepared samples. Powdered XRD (PANalytical, Almelo, the Netherlands) was performed for analyzing surface characterstics of the particles. Zeta potential was measured for size and charge determination using Malvern Zetasizer. FTIR (Perkin Elmer) demonstrated the chemical nature of novel compounds. Confocal laser scanning microscopy (CLSM) using NIKON C2+ instrument was performed to determine cellular internalization of drugs by cancerous cells.

Bansal S., Singh J., Kumari U., Kaur I.P., Barnwal R.P., Kumar R., Singh S., Singh G, & Chatterjee M. (2019). Development of biosurfactant-based graphene quantum dot conjugate as a novel and fluorescent theranostic tool for cancer. International Journal of Nanomedicine, 14, 809-818.

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Characterization of Upconversion Nanoparticles

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UCNPs material fluorescence
spectra were measured on an F-2500 fluorescence spectrometer (Hitachi,
Japan) under the excitation of a 980 nm diode laser (1 W, continuous
wave with 1 m fiber). UCNP material morphologies were observer by
a JEOL 2010F (JEOL, Japan) TEM. UCNP material FT-IR spectra (4000–400
cm^–1) in KBr were measured in a Vector 22 FT-IR
spectrophotometer (Bruker, Germany). Zeta potentials of UCNP material
were recorded in neutral water solution at room temperature with a
Zetasizer Nano ZS90 (Malvern). Ultraviolet–visible (UV–vis)
absorption spectra were measured in a Shimadzu UV-2700 UV–vis
spectrophotometer (Shimadzu, Japan).

Yin M., Wu C., Li H., Jia Z., Deng Q., Wang S, & Zhang Y. (2019). Simultaneous Sensing of Seven Pathogenic Bacteria by Guanidine-Functionalized Upconversion Fluorescent Nanoparticles. ACS Omega, 4(5), 8953-8959.

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Verifying α-synuclein Amyloid Formation

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α-synuclein PFF formation was verified using an amyloid-specific fluorescent dye, ThT, which was added to a 10-times diluted α-synuclein solution up to a final concentration of 10 μM. The ThT fluorescent spectra were measured using a Hitachi F-2500 fluorescence spectrometer at 25 °C. The spectra were recorded between 450 and 600 nm at an excitation of 440 nm.

Gima S., Oe K., Nishimura K., Ohgita T., Ito H., Kimura H., Saito H, & Takata K. (2024). Host-to-graft propagation of inoculated α-synuclein into transplanted human induced pluripotent stem cell-derived midbrain dopaminergic neurons. Regenerative Therapy, 25, 229-237.

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ANS-Based Protein Hydrolysate Analysis

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A 1.5 mL aliquot of T. molitor protein hydrolysate solution (1 μg/mL, in 10 mM PBS at pH 7.0) was mixed with 20 μL of an 8 mM ANS solution. Relative fluorescence intensity was assayed using an F-2500 fluorescence spectrometer (Hitachi Ltd., Tokyo, Japan) in the range of 400–700 nm [28 (link)].

Tan J., Yang J., Zhou X., Hamdy A.M., Zhang X., Suo H., Zhang Y., Li N, & Song J. (2022). Tenebrio molitor Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding Mechanism. Foods, 11(22), 3626.

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Surface Hydrophobicity Determination

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The method reported by Mondoulet [32 (link)] was used in this part of the experiment. In short, samples were diluted to different concentrations as described earlier [33 (link)]. Protein samples (4 mL) were then mixed with ANS (8 mmol/L, 20 μL) and reacted in the dark for 15 min. The fluorescence intensity was detected by a F2500 fluorescence spectrometer (Hitachi, Tokyo, Japan), the excitation and emission wavelength were set as 390 and 470 nm, respectively. The surface hydrophobicity index (H0) was presented as the initial slope of fluorescence intensity versus protein concentration plot.

Tian Y., Liu C., Xue W, & Wang Z. (2020). Crosslinked Recombinant-Ara h 1 Catalyzed by Microbial Transglutaminase: Preparation, Structural Characterization and Allergic Assessment. Foods, 9(10), 1508.

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Structural Characterization of YCH Biopolymer

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The YCH was structurally characterized using circular dichroism (CD) spectroscopy using a MOS-500 CD spectrometer (Bio-Logic Science Instruments). The YCH solution (0.1 mg/mL) was prepared in deionized water. Parameters were as follows: wavelength range, 190-250 nm; scan speed, 100 nm/min; path length, 1 mm. Ellipticity (θ) was measured in millidegrees (mdeg).
The conformational change of the YCH was assessed by ANS fluorescence spectroscopy. The YCH was dissolved in phosphate buffer (pH 7.0, 10 mM) at a concentration of 1 μg/mL. Then, 20 μL of 8 mM ANS was mixed with 1.5 mL of the YCH solution, and the fluorescence spectrum was recorded using an F-2500 fluorescence spectrometer (Hitachi Ltd.) in a wavelength range from 400 to 700 nm.
The molecular weight distribution of the YCH was further analyzed, as described previously (Sun et al., 2021) (link). In brief, the mobile phase was composed of acetonitrile, water, and trifluoroacetic acid (45/55/0.1, vol/vol/vol). The YCH was dissolved in the mobile phase and filtered through a 0.45-μm filter. Then, the YCH solution was loaded on a TSK gel G2000 SWXL (300 × 7.8 mm internal diameter) column (Tosoh) for separation at a flow rate of 0.5 mL/min under a detection wavelength of 220 nm. The standards of cytochrome C, aprotinin, bacitracin, Gly-Gly-Tyr-Arg, and Gly-Gly-Gly were used to prepare a calibration curve of molecular weight.

Zhang X., Yang J., Suo H., Tan J., Zhang Y, & Song J. (2023). Identification and molecular mechanism of action of antibacterial peptides from Flavourzyme-hydrolyzed yak casein against Staphylococcus aureus. Journal of dairy science, 106(6).

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