All reagents were purchased from commercial sources and used as received, unless otherwise mentioned. 1H NMR spectra were recorded on a Bruker DPX-400 MHz NMR spectrometer and all the spectra were calibrated against tetramethylsilane (TMS). Dynamic light scattering (DLS) measurements were carried out on a Malvern Nanozetasizer. TEM images were recorded on a JEOL-2000FX machine operating at an accelerating voltage of 100 kV. Cell imaging was performed using a Zeiss 510 META confocal microscope. Fluorescence measurements were performed on a fluorescence plate reader (Molecular Devices, SpectraMax M5).
Dpx 400 mhz nmr spectrometer
Manufactured by Bruker
Sourced in Germany, United Kingdom
The DPX-400 MHz NMR spectrometer is a high-performance nuclear magnetic resonance (NMR) instrument designed for analytical and research applications. It operates at a frequency of 400 MHz and is capable of detecting and analyzing the magnetic properties of atomic nuclei within a sample. The core function of the DPX-400 is to provide researchers and analysts with detailed information about the chemical structure and composition of their samples through the acquisition and interpretation of NMR spectra.
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Lab products found in correlation
5 protocols using dpx 400 mhz nmr spectrometer
1
Characterization of Nanomaterials
2
Enzyme Activity Characterization of GAA
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All the reagents were purchased from commercial
sources and used as such without further purification. 1H NMR spectra were recorded on a Bruker DPX-400 MHz NMR spectrometer,
and all the spectra were calibrated against tetramethylsilane. Dynamic
light scattering (DLS) measurements were carried out on a Malvern
Nanozetasizer. Transmission electron microscopy (TEM) images were
recorded on a JEOL-2000FX machine operating at an accelerating voltage
of 100 kV. Fluorescence emission spectra were recorded on a Photon
Technology International Quanta Master fluorometer. Mass spectrometric
data were acquired by an electron spray ionization (ESI) technique
on a Q-tof-micro quadruple mass spectrometer (Micromass). Absorbance
of para-nitophenolate was measured using a plate
reader (SpectraMax M5). The enzyme acid alpha glucosidase (GAA) was
provided by Genzyme. The GAA was stored as a lyophilized cake at 5
°C until reconstitution with Milli-Q H2O. The reconstituted
formulation contained 10 mg/mL GAA, 50 mM sodium phosphate, 4% mannitol,
and 0.01% Tween-80 at pH 6.2. Following reconstitution, the solution
was stored as frozen aliquots at −80 °C until use.
sources and used as such without further purification. 1H NMR spectra were recorded on a Bruker DPX-400 MHz NMR spectrometer,
and all the spectra were calibrated against tetramethylsilane. Dynamic
light scattering (DLS) measurements were carried out on a Malvern
Nanozetasizer. Transmission electron microscopy (TEM) images were
recorded on a JEOL-2000FX machine operating at an accelerating voltage
of 100 kV. Fluorescence emission spectra were recorded on a Photon
Technology International Quanta Master fluorometer. Mass spectrometric
data were acquired by an electron spray ionization (ESI) technique
on a Q-tof-micro quadruple mass spectrometer (Micromass). Absorbance
of para-nitophenolate was measured using a plate
reader (SpectraMax M5). The enzyme acid alpha glucosidase (GAA) was
provided by Genzyme. The GAA was stored as a lyophilized cake at 5
°C until reconstitution with Milli-Q H2O. The reconstituted
formulation contained 10 mg/mL GAA, 50 mM sodium phosphate, 4% mannitol,
and 0.01% Tween-80 at pH 6.2. Following reconstitution, the solution
was stored as frozen aliquots at −80 °C until use.
3
NMR Spectroscopy and GPC Analysis of Polymers
4
1H NMR Spectroscopy of EPO Variants
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1 H nuclear magnetic resonance spectra were recorded for EPO, AEPO25 and AEPO50 using a DPX 400 MHz NMR spectrometer (Bruker, Germany). All samples were dissolved in deuterated chloroform and transferred to 5 mm Norell tubes (Standard Series™ 400 MHz NMR). All chemical shifts were reported as δ in parts per million (ppm).
5
Solution-state NMR Analysis of APIs and Silicone Elastomers
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For solution-state 1 H and 13 C-NMR analysis, samples were dissolved, dispersed or swollen in CDCl3. Spectra were recorded using a Bruker DPX 400 MHz NMR spectrometer (Bruker UK Ltd., Coventry, UK). Chemical shifts were recorded in ppm (parts per million) with the chemical shift of the internal reference set to 77.0 ppm for 13 C-NMR and 7.26 ppm for 1 H-NMR with respect to CDCl3. A series of reference spectra for the supplied APIs and DDU-4331 Part A and Part B silicone elastomer components were recorded to enable identification of characteristic API and silicone elastomer signals.
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