NMR experiments were performed on a 500.13 MHz Bruker Avance II spectrometer (Bruker BioSpin) equipped with a 5 mm ATM BBFO probe with a z-gradient. 13C NMR spectra were acquired using a 1D sequence with inverse gated decoupling and a flip angle of 30° (“zgig30” from the Bruker pulse program library). Each 1D 13C NMR spectrum was measured using the same parameters: a nominal temperature of 275 K, a spectral width of 34,000 Hz, a data size of 32 K points, 1280 transients, an acquisition time of 0.48 s, and a relaxation delay of 4 s. The total experiment time for the 13C NMR acquisition was about 96 min. The spectral processing was performed using the Bruker Topspin software (version 3.2, patch level 5). The free induction decays (FIDs) were exponentially weighted with a line broadening factor of 10 Hz, Fourier-transformed, manually phased, and baseline corrected. For each sample, the 13C lactate peak of interest was integrated. The absolute integral was then converted into an mM value using the integral of the starting condition with a known concentration of 20 mM lactate. For the analysis, lactate consumption values, normalized for the cell number, were calculated via subtraction of the lactate concentration value of a specific sample from 20 mM lactate at the starting condition.
Avance 2 spectrometer
Manufactured by Bruker
Sourced in Germany, United States, Switzerland, France
The Avance II spectrometer is a high-performance nuclear magnetic resonance (NMR) spectrometer produced by Bruker. It is designed to provide researchers and scientists with advanced capabilities for the analysis and characterization of materials and molecules. The Avance II spectrometer is capable of performing a wide range of NMR experiments and offers excellent sensitivity, resolution, and experimental flexibility.
Automatically generated - may contain errors
Lab products found in correlation
Topspin 3, by Bruker (4 mentions)
Nicolet 6700, by Thermo Fisher Scientific (3 mentions)
Jsm 6330f microscope, by JEOL (2 mentions)
Topspin 1, by Bruker (2 mentions)
2 propanol, by Merck Group (2 mentions)
Tga 2050, by TA Instruments (1 mentions)
Avance 300 spectrometer, by Bruker (1 mentions)
Topspin version 3, by Bruker (1 mentions)
Milli q water, by Merck Group (1 mentions)
Cryoprobe, by Bruker (1 mentions)
Jem 2010 microscope, by JEOL (1 mentions)
Ft ir 4200 spectrometer, by Jasco (1 mentions)
D8 advance x ray diffractometer, by Bruker (1 mentions)
Matlab v8, by MathWorks (1 mentions)
7 t wide bore 89 mm magnet, by Bruker (1 mentions)
4 mm hx cp mas probe, by Bruker (1 mentions)
Avance 3 hd spectrometer, by Bruker (1 mentions)
Agilent 1200 lc, by Agilent Technologies (1 mentions)
5 mm tci c n prodigy cryoprobe, by Bruker (1 mentions)
Mat 44 s apparatus, by Agilent Technologies (1 mentions)
58 protocols using avance 2 spectrometer
1
Quantifying Lactate Consumption in Cells
2
Plasma Biomarker Profiling in Stroke
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Plasma (lipo)protein biomarkers were measured in EDTA plasma of a subset of stroke patients and controls using proton nuclear magnetic resonance (1H-NMR) spectroscopy, using a 600-MHz Bruker Avance II spectrometer (Bruker BioSpin, Karlsruhe, Germany). Targeted TMAO measurements were performed using a high-performance liquid chromatography system consisting of an Ultimate 3000 Rapid Separation Quaternary System (ThermoFisher Scientific), combined with a maXis impact HD UHR-QqTOF mass spectrometer from Bruker Daltonics (Bremen, Germany). A detailed description of the sample preparation and measurement of EDTA plasma samples is described in the SI Appendix.
3
Solid-State NMR Analysis of VDAC2/DMPC Crystals
4
NMR Analysis of Polymer Samples
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
As for the polymer samples, it was necessary to dissolve them with a deuterated solvent. Each sample was suspended in 1 mL of CDCl3 and placed in an ultrasonic bath. The polymer fibers were shredded under the influence of ultrasound (30 min). The samples were then re-centrifuged for 10 min at 4 °C at 12,000 rpm, and 550 µL was transferred to a 5 mm NMR cuvette. NMR measurements were made using the AVANCE II spectrometer by BrukerDaltonik GmbH (Bremen, Germany), with the operating frequency of 600.58 MHz. A 90-degree pulse was used for the measurements.
5
High-Resolution NMR Analysis of Carbohydrates
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
All NMR spectra were recorded on an 800 MHz Avance II spectrometer (Bruker, Fällanden, Switzerland) equipped with a TCI Z-gradient CryoProbe and an 18.7 T magnet (Oxford Magnet Technology, Oxford, England). Highly resolved 1H–13C HSQC spectra employing a sweep width of 10 p.p.m. centred near the 13C chemical shift of the α-anomeric signals were recorded as data matrices of 1024 × 256 complex data points sampling acquisition times of 143 and 127 ms in the 1H and 13C dimensions, respectively. High-precision signal measurements in the two-dimensional spectra were thus used to enumerate the number of signals in the resultant reaction products and for the identification of the products by comparison with authentic standards including glucose, maltooligosaccharides, panose and limit dextrins (Petersen et al., 2014 ▸ , 2015 ▸ ).
All spectra were processed with extensive zero filling in both dimensions using a shifted sine-bell apodization function and were analysed with TopSpin 2.1 pl 5 (Bruker).
All spectra were processed with extensive zero filling in both dimensions using a shifted sine-bell apodization function and were analysed with TopSpin 2.1 pl 5 (Bruker).
6
Multimodal Characterization of Materials
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
1H NMR spectra
were recorded on a Bruker AVANCE 300 spectrometer (300 MHz). Solid-state 13C NMR spectra were obtained with a Bruker AVANCE II spectrometer
(500 MHz) equipped with a CP-MAS probe. FT-IR measurements were made
on a Thermo Scientific Nicolet 6700 using KBr pellets. SEM images
were obtained by using a JEOL JSM-6330F microscope. TEM images were
obtained by using a JEOL JEM-2010 microscope at 200 keV. UV–vis
spectra were recorded by using a SINCO S-3150 instrument. EDS elemental
maps were acquired using an Oxford instrument X-MaxN detector
and analyzed with an AZtecEnergy EDS analyzer. XRD measurements were
performed on a Smart lab equipped with a Mo Kα X-ray
source. TGA measurements were performed on a TA modulated TGA2050
with a heating rate of 10 °C min–1 under nitrogen.
Nitrogen adsorption–desorption isotherms were measured by using
a Belsorp-Max (BEL Japan, Inc.) apparatus.
were recorded on a Bruker AVANCE 300 spectrometer (300 MHz). Solid-state 13C NMR spectra were obtained with a Bruker AVANCE II spectrometer
(500 MHz) equipped with a CP-MAS probe. FT-IR measurements were made
on a Thermo Scientific Nicolet 6700 using KBr pellets. SEM images
were obtained by using a JEOL JSM-6330F microscope. TEM images were
obtained by using a JEOL JEM-2010 microscope at 200 keV. UV–vis
spectra were recorded by using a SINCO S-3150 instrument. EDS elemental
maps were acquired using an Oxford instrument X-MaxN detector
and analyzed with an AZtecEnergy EDS analyzer. XRD measurements were
performed on a Smart lab equipped with a Mo Kα X-ray
source. TGA measurements were performed on a TA modulated TGA2050
with a heating rate of 10 °C min–1 under nitrogen.
Nitrogen adsorption–desorption isotherms were measured by using
a Belsorp-Max (BEL Japan, Inc.) apparatus.
7
NMR Characterization of Peptides
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
NMR structure characterization was performed as previously described39 (link). Briefly, peptide was dissolved in 500 μL of Milli-Q water (MilliPore, USA) and 50 μL of D2O (Cambridge isotopes). A Bruker 900 MHz Avance II spectrometer equipped with a cryoprobe (Bruker, Billerica, MA < USA) was used to acquire 1D 1H NMR spectra at 25 °C. Spectra were processed using TopSpin version 3.5 (Bruker). The chemical shift of water at 4.76 ppm was used as reference.
8
Comprehensive Characterization of Nano Materials
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Solid-state 13C NMR spectra were recorded on a Bruker Avance II spectrometer (500 MHz) equipped with a cross-polarization/magic angle spinning (CP/MAS) probe. The FT-IR spectra were measured by a JASCO FT-IR 4200 spectrometer using KBr pellets. N2 adsorption-desorption isotherms were measured by a Belsorp-Max (BEL Japan, Inc.) apparatus. UV-Vis spectra were measured with a Sinco S-3150 spectrometer. Scanning electron microscopy (SEM) images were obtained by a JEOL JSM-6330F microscope. Transmission electron microscopy (TEM) images were obtained by a JEOL JEM-2010 microscope at 200 keV. Powder X-ray diffraction (PXRD) patterns were recorded on a Bruker D8 ADVANCE X-ray diffractometer (CuKα radiation, λ = 1.5418 Å). The dynamic mechanical analysis was conducted by a DMA Q800 instrument, in the tensile mode at a displacement rate of 100 µm/min. Thermogravimetric analysis (TGA) were performed using a TA modulated TGA2050 with a heating rate of 10 °C/min under nitrogen.
9
Serum NMR Metabolomics Protocol
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The collected serum samples were prepared according to a well-established protocol18 (link),19 (link). The serum samples were thawed at room temperature and vortexed. Each serum sample (200 μL) was mixed with 400 μL of saline solution (0.9% NaCl, w/v) containing 20% D2O and centrifuged (10 min, 12 000 RPM, 4 °C). Supernatant (550 μL) from each sample was transferred into a 5-mm NMR tube (SP, 5 mm ARMAR Chemicals). The samples were kept at 4 °C before measurement.
The one-dimensional (1D) NMR spectra of serum samples were recorded at 298 K using an Avance II spectrometer (Bruker, GmBH, Germany) and cpmg1dpr pulse sequence with water presaturation (Bruker notation), which was operating at a proton frequency of 600.58 MHz. The serum sample spectra were collected as 128 following scans with spin-echo delay of 1000 μs, 80 loops, relaxation delay of 3.5 s, acquisition time of 2.73 s, size of FID (TD), 65,536 points, spectra width of 20.01 ppm, line-broadening factor (LB), 0.3 Hz and transmitter frequency offset (O1P), 4.722 ppm.
Two-dimensional (2D) NMR experiments were recorded and processed for selected samples. The performed experiments included 1H−1H correlation spectroscopy (COSY), total correlation spectroscopy (TOCSY), and 1H−13C heteronuclear single quantum correlation (HSQC).
The one-dimensional (1D) NMR spectra of serum samples were recorded at 298 K using an Avance II spectrometer (Bruker, GmBH, Germany) and cpmg1dpr pulse sequence with water presaturation (Bruker notation), which was operating at a proton frequency of 600.58 MHz. The serum sample spectra were collected as 128 following scans with spin-echo delay of 1000 μs, 80 loops, relaxation delay of 3.5 s, acquisition time of 2.73 s, size of FID (TD), 65,536 points, spectra width of 20.01 ppm, line-broadening factor (LB), 0.3 Hz and transmitter frequency offset (O1P), 4.722 ppm.
Two-dimensional (2D) NMR experiments were recorded and processed for selected samples. The performed experiments included 1H−1H correlation spectroscopy (COSY), total correlation spectroscopy (TOCSY), and 1H−13C heteronuclear single quantum correlation (HSQC).
10
NMR Characterization of Biofluids and Tissues
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The NMR spectra of serum, urine and tissue samples were recorded at 300 K using the Avance II spectrometer (Bruker, GmBH, Germany) operating at a 600.58 MHz proton frequency. The NMR spectra of serum were recorded using a CPMG pulse sequence with water presaturation in a Bruker notation. For each sample, 128 subsequent scans were collected with a 400 μs spin-echo delay; 80 loops; 3.5 s relaxation delay; acquisition time of 2.73 s; TD of 64k; SW of 20.01 ppm.
The NMR spectra of urine and tissue were recorded with the use of the nuclear Overhauser effect spectroscopy, NOESY pulse sequence with water presaturation in a Bruker notation: with a relaxation delay of 3.5 s; acquisition time of 1.36 s; 128 transients; TD of 64k; SW of 20.01 ppm.
The spectra were processed using 0.3 Hz of line broadening and were manually phased and baseline corrected using Topspin 1.3 software (Bruker, GmBH, Germany) and referenced to α-glucose signal δ = 5.225 ppm for serum samples and to the TSP resonance at δ = 0.000 ppm for the urine and tissue samples. The correlation optimized warping algorithm, COW, and the icoshift algorithm implemented in Matlab (Matlab v. 8.1, Mathworks Inc.) were used to correct the peak positions (alignment). The spectra were normalized using the Probabilistic Quotient Normalization (PQN) method.
The NMR spectra of urine and tissue were recorded with the use of the nuclear Overhauser effect spectroscopy, NOESY pulse sequence with water presaturation in a Bruker notation: with a relaxation delay of 3.5 s; acquisition time of 1.36 s; 128 transients; TD of 64k; SW of 20.01 ppm.
The spectra were processed using 0.3 Hz of line broadening and were manually phased and baseline corrected using Topspin 1.3 software (Bruker, GmBH, Germany) and referenced to α-glucose signal δ = 5.225 ppm for serum samples and to the TSP resonance at δ = 0.000 ppm for the urine and tissue samples. The correlation optimized warping algorithm, COW, and the icoshift algorithm implemented in Matlab (Matlab v. 8.1, Mathworks Inc.) were used to correct the peak positions (alignment). The spectra were normalized using the Probabilistic Quotient Normalization (PQN) method.
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!