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Microflex maldi tof spectrometer

Manufactured by Bruker
Sourced in United States

The Microflex MALDI-TOF spectrometer is a laboratory instrument designed for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The core function of the Microflex is to analyze and identify molecules, including proteins, peptides, and small molecules, by measuring their mass-to-charge ratios.

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4 protocols using microflex maldi tof spectrometer

1

MALDI-TOF Mass Spectrometry of Target Compounds

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Mass spectra were measured on Microflex MALDI-TOF spectrometer (Bruker Daltonics) with a N2 laser (337 nm), using the Flex Control software in linear negative mode. For samples with a mass higher than 1000 Da, the laser was set at 70% of its maximal intensity. One spectrum was the sum of 200 laser shots at 1.5 Hz frequency. For target compounds with a mass lower than 1000 Da, laser intensity was dropped to 50%, with a frequency of 2 Hz and accumulation of 150 shots. Aliquots of assay solutions (0.7 μL) were desalted with the ammonium form of cation exchange resin Dowex 50 WX8-200 in 25 μL volume for 20 min. Sample of 0.5 μL were dried on the MALDI target, and a mixture (0.4 μL) of matrix and co-matrix solutions (0.3 M trihydroxyacetophenone in EtOH, and 0.1 M aqueous ammonium citrate; 2:1) was placed on the spot. Analysis was performed on the [M–H] ions.
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2

1H NMR, MALDI-TOF, and HPLC Analysis

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1H NMR spectra were recorded on a Bruker DMX360 or UNI500 spectrometer in CDCl3 or CD3OD using tetramethylsilane (TMS) as an internal standard. Chemical shifts are reported in ppm. Mass spectra were recorded on a Bruker Microflex MALDI-TOF spectrometer. HPLC analysis was performed as described elsewhere (38 (link)). Solvents were purchased from Fisher Scientific. 1,4-Diphenylbutane was purchased from Pfaltz & Bauer, Inc., Waterbury, CT. All other chemicals were purchased from Sigma-Aldrich and used as received. The compounds were named with ChemBioDraw Ultra (v. 13, CambridgeSoft).
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3

MALDI-TOF Characterization of Peptides

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A Microflex MALDI-TOF spectrometer (Bruker Daltonics, Billerica, MA, USA) was used for characterising the products; 18.0 μL of an oversaturated α-cyano-4-hydroxycinnamic acid matrix solution was mixed with 2.0 μL peptide solution (5.0 × 10−4 mg/μL), and then 2.5 μL of this mixture was placed in the 96-well plates to be analysed.
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4

Multimodal Characterization of Catalysts

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Scanning electron microscope (SEM) images were obtained using a Hitachi S-4700 II Field Emission SEM with an Energy Dispersive Spectrometer (EDX) at an acceleration voltage of 15 kV. X-ray diffraction (XRD) was performed using a Bruker D2 X-ray Diffractometer using carbon paper as a substrate (Fuel Cell Store, AvCarb EP40T). ICP-MS was conducted by Western Environmental Testing Laboratory (Sparks, NV). All Ni:Cu ratios reported in this manuscript come from ICP-MS results as opposed to the nominal ratios of the Ni and Cu salts used during synthesis. The Faradaic efficiency for O2 evolution was determined using a SRI 8610C gas chromatograph equipped with a thermal conductivity detector and a previously described custom-built electrochemical cell.15 Matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectra were recorded on a Bruker microflex MALDI-TOF spectrometer using 2,5-dihydroxybenzoic acid as the matrix. High-resolution mass spectrometry with electrospray ionization (ESI-MS) analysis was obtained using an Agilent G6230B time-of-flight mass spectrometer. Fluorescence spectroscopy was performed with a Jobin Yvon Horiba FluoroMax-3 using an excitation wavelength of 365 nm and ethanol as a solvent.
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