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Samplejet

Manufactured by Bruker
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Sourced in Germany, United States

The SampleJet is a lab equipment product from Bruker. It is designed to automate the sample loading process for various analytical instruments. The core function of the SampleJet is to efficiently and accurately transfer samples from a sample holder to the instrument's sample introduction system.

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Lab products found in correlation

Icon nmr, by Bruker (5 mentions) Avance 3, by Bruker (3 mentions) Avance 3 nmr spectrometer, by Bruker (3 mentions) Qci 5 mm cryoprobe, by Bruker (3 mentions) Avance 3 hd 600 mhz, by Bruker (2 mentions) Qci f cryoprobe, by Bruker (2 mentions) Topspin 3, by Bruker (2 mentions) Avance 3 hd spectrometer, by Bruker (2 mentions) Topspin 3.5pl6, by Bruker (2 mentions) Avance 3 hd 500 nmr, by Bruker (1 mentions) Janus automated workstation, by PerkinElmer (1 mentions) 215 liquid handler, by Gilson (1 mentions) Cryoprobe, by Bruker (1 mentions) Avance 2 nmr spectrometer, by Bruker (1 mentions) Avance 3 hd nmr spectrometer, by Bruker (1 mentions) Avance 2 600 mhz spectrometer, by Bruker (1 mentions) 5 mm tci cryogenic probe head, by Bruker (1 mentions) Samplepro, by Bruker (1 mentions) Avance neo 600 spectrometer, by Bruker (1 mentions) Speedvac, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

SampleJet autosampler (25 citations) SampleJet NMR tubes (12 citations) SampleJet sample changer (8 citations) SampleJet automated sample changer (7 citations) SampleJet rack tube (5 citations) SampleJet system (3 citations) SampleJet tubes (3 citations) SampleJet robot (3 citations) SampleJet automatic sample changer (2 citations) SampleJet automated (2 citations)

36 protocols using samplejet

1

Quantitative Lipoprotein Analysis by NMR Spectroscopy

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NMR analysis was performed on Bruker Avance III HD 600 MHz spectrometers (Bruker Biospin GmbH, Rheinstetten, Germany) equipped with a TXI probes and the Bruker SampleJet automatic robot cooling system set to 6 °C. The 100 μL plasma samples supernatant was mixed with 75 mM pH 7.4 sodium phosphate (buffer in 1:1 ratio) and 200 μL were ceded into a 3 mm × 4 inch Bruker SampleJet NMR tube.
Lipoprotein analysis reports containing around 112 lipoprotein paramecium for each plasma sample were generated using the Bruker IVDr Lipoprotein Subclass Analysis (B.I.-LISA) method. This is completed by mathematically interrogating and quantifying the −CH2 (δ = 1.25 ppm) and −CH3 (δ = 0.8 ppm) peaks of the 1D spectrum from normalization to the Bruker QuantRef manager among Topspin by using a PLS-2 regression model [31 (link)].
Chou T.H., Cheng C.H., Lo C.J., Young G.H., Liu S.H, & Wang R.Y. (2024). New Advances in Rapid Pretreatment for Small Dense LDL Cholesterol Measurement Using Shear Horizontal Surface Acoustic Wave (SH-SAW) Technology. International Journal of Molecular Sciences, 25(2), 1044.
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2

Validated NMR Metabolomics for Canine Analysis

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The samples were analyzed using a validated, dog-specific 1H NMR metabolomics platform quantifying 123 measurands in absolute units (24 (link)). The quantified measurands are presented in Figure 1. Details about the method and its validation is provided elsewhere (24 (link)–27 (link)).
Briefly, the method utilizes a Bruker AVANCE III HD 500 NMR spectrometer equipped with a 5 mm triple-channel (1H, 13C, 15N) z-gradient Prodigy probe head and a cooled high-throughput sample changer SampleJet (Bruker Corp., Billerica, Massachusetts, USA). Sample preparation begins with light mixing of the sample and centrifugation to remove possible precipitate (25 (link)). The highly automated process then continues by transfer of each sample into individual NMR tubes and mixing with sodium phosphate buffer using a PerkinElmer JANUS Automated Workstation equipped with an 8-tip dispense arm with Varispan (PerkinElmer Inc., Waltham, Massachusetts, USA) (26 (link)). The NMR spectra are acquired automatically from each sample using standardized parameters and are automatically processed using in-house scripts optimized for dogs (24 (link)–27 (link)). Result generation is based on regression modeling and includes integrated quality control (27 (link)).
Ottka C., Vapalahti K., Arlt S.P., Bartel A, & Lohi H. (2023). The metabolic differences of anestrus, heat, pregnancy, pseudopregnancy, and lactation in 800 female dogs. Frontiers in Veterinary Science, 10, 1105113.
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3

NMR Metabolite Profiling of Plasma

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Plasma samples were thawed at 4°C in a cold room. Four hundred μL of saline solution (NaCl 0.9% in 10% D2O) was added to 200 μL of each plasma sample. The mixtures were vortexed for 1 minute and centrifuged at 16, 000 g for 15 min at 4°C and 550 μL of supernatant was transferred into 5 mm Bruker NMR tubes (Z105684 Bruker 96 well rack) using Gilson 215 Liquid Handler (Trilution software version 2.0). All 1H-NMR spectra were collected on a 600 MHz Avance II NMR spectrometer (Bruker Biospin, Rheinstetten, Germany) equipped with a 5 mm CryoProbe. A Bruker sampleJet operated by IconNMR in Topspin was used to record spectra automatically. 1D CPMG-presaturated spectra for plasma were recorded. Optimal probe tuning and matching, 90° pulse length, water offset, and receiver gain were adjusted on the representative sample. The probe was automatically locked to H2O+D2O (90%+10%) and shimmed for each sample. All NMR data were acquired at 300 K.
Liu H., Garrett T.J., Tayyari F, & Gu L. (2015). Profiling the Metabolome Changes Caused by Cranberry Procyanidins in Plasma of Female Rats using 1H NMR and UHPLC-Q-Orbitrap-HRMS Global Metabolomics Approaches. Molecular nutrition & food research, 59(11), 2107-2118.
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4

High-throughput NMR Acquisition Protocol

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All spectral acquisitions were performed in Bruker Avance III HD NMR spectrometer, equipped with a triple resonance inverse (TXI) 3 mm probe (Bruker Biospin). Bruker Samplejet was used for sample handling to ensure high throughput nature. The pulseprogram took the shape of first transient of a 2 dimensional NOESY and generally of the form RD-90-t-90-tm-90-ACQ [12 (link)]. Where RD = relaxation delay, t = small time delay between pulses, tm = mixing time and ACQ = acquisition. Water signal was saturated using continuous irradiation during RD and tm. The spectra were acquired using 76 K data points and 14 ppm spectral width. Sixty-four scans were performed and 1 s interscan (relaxation) delay and 0.1 s mixing time was allowed. The FIDs were zero filled to 128 K; 0.1 Hz of linear broadening was applied followed by Fourier transformation, baseline and phase correction using an automated program provided by Bruker Biospin.
Sengupta A., Krishnaiah S.Y., Rhoades S., Growe J., Slaff B., Venkataraman A., Olarerin-George A.O., Van Dang C., Hogenesch J.B, & Weljie A.M. (2016). Deciphering the Duality of Clock and Growth Metabolism in a Cell Autonomous System Using NMR Profiling of the Secretome. Metabolites, 6(3), 23.
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5

NMR Spectroscopy Protocol for Metabolite Analysis

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1H NMR data were collected using a Bruker 600MHz AVANCE II spectrometer equipped with a 5mm TCI cryogenic probe head and a z-gradient system. A Bruker SampleJet was used for sample insertion and removal. All experiments were recorded at 300K. A fresh sample of 99.8% methanol-d4 was used for temperature calibration [21 (link)] before each batch of measurements. Duration of 90° pulses were automatically calibrated for each individual sample using a homonuclear-gated mutation experiment [22 (link)] on the locked and shimmed samples after automatic tuning and matching of the probe head. One-dimensional (1D) 1H NMR spectra were recorded using the first increment of a NOESY pulse sequence [23 (link)] with presaturation (γB1 = 50Hz) during a relaxation delay of 4s and a mixing time of 10ms for efficient water suppression [24 (link)]. Initial shimming was performed using the TopShim (Bruker Corporation, 2011) tool on a random mix of urine samples from the study, and subsequently the axial shims were optimized automatically before every measurement. Sixteen scans of 65,536 points covering 12,335Hz were recorded. J-resolved (JRES) spectra were recorded with a relaxation delay of 2s and two scans for each increment in the indirect dimension. A data matrix of 40×12,288 data points was collected covering a sweep width of 78×10,000 Hz.
Dekker S.E., Verhoeven A., Soonawala D., Peters D.J., de Fijter J.W, & Mayboroda O.A. (2020). Urinary metabolites associate with the rate of kidney function decline in patients with autosomal dominant polycystic kidney disease. PLoS ONE, 15(5), e0233213.
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6

High-throughput NMR Experiments Protocol

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All NMR experiments were performed on a Bruker Avance III spectrometer operating at 800.15 MHz (1H resonance frequency), equipped with either a 5 mm TXI solution NMR probe or a 4 mm HCP high-resolution MAS probe, and associated automated sample changers with cooling capacity for high-throughput acquisition (Bruker SampleJet and SamplePro for solution and HR-MAS NMR, respectively). Detailed NMR experimental parameters are provided in the Supplementary Material.
Elena-Herrmann B., Montellier E., Fages A., Bruck-Haimson R, & Moussaieff A. (2020). Multi-platform NMR Study of Pluripotent Stem Cells Unveils Complementary Metabolic Signatures towards Differentiation. Scientific Reports, 10, 1622.
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7

Comprehensive Metabolome Analysis of Human Milk

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The HM metabolome including HMOs will be analysed by NMR as described elsewhere.46 (link) Briefly, samples are skimmed by centrifugation at 4000 g for 15 min. To extract metabolites, the samples will be filtered using Amicon Ultra 0.5 mL 10 kDa (Millipore, Billerica, Massachusetts, USA) spin filters at 10 000 g for 60 min at 4°C. 1H NMR spectroscopy is performed on a Bruker Avance Neo 600 spectrometer, at a 1H frequency of 600.03 MHz, equipped with a 5 mm 1H BBI probe and SampleJet (Bruker BioSpin, Rheinstetten, Germany).
In addition, the Biocrates MxP Quant 500 Targeted Metabolomics Kit (Biocrates, Innsbruck, Austria) will be used for HM metabolomics as described.47 (link) The kit can identify and quantify up to 13 different small molecule classes, hexoses and 12 lipid classes using MS.
Overgaard Poulsen K., Astono J., Jakobsen R.R., Uldbjerg N., Fuglsang J., Nielsen D.S, & Sundekilde U.K. (2022). Influence of maternal body mass index on human milk composition and associations to infant metabolism and gut colonisation: MAINHEALTH – a study protocol for an observational birth cohort. BMJ Open, 12(11), e059552.
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8

Quantitative 1H NMR Metabolite Analysis

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1H NMR spectra were acquired using a Bruker 600 or 900 MHz spectrometer equipped with a TCI H/F-cryogenic probe. Samples (pH 6.9 ± 0.1) were mixed 1:1 (v/v) with D2O containing TSP (1.0 mM [22 (link)]). Each spectrum represents the average of 64 spectra acquired using a 1D pulse sequence that included a 4.0 s relaxation delay and 2.73 s acquisition time. Water suppression was accomplished using Excitation Sculpting [23 ]. Samples were equilibrated, and spectra were acquired at 298 ± 2 °K. 600 MHz spectra were collected using the Bruker automated acquisition software ICON-NMR and SampleJet. Peaks were fit to a Lorentzian peak shape using TopSpin3.5 [24 (link)]. Metabolite concentrations were determined by normalizing their peak areas to that of the TSP signal [24 (link)].
Cook I., Wang T, & Leyh T.S. (2018). Isoform-specific therapeutic control of sulfonation in humans. Biochemical pharmacology, 159, 25-31.
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9

NMR Analysis of Cell Extracts

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Cell extract preparation was performed at + 4 °C. First, cells were washed with PBS, after which they were vortexed in 80% ethanol and centrifuged (4000 rpm, 5 min). The supernatant was collected and the vortexing in 80% ethanol was repeated for the pellet. Next, the supernatant samples were dried in SpeedVac (Savant SVC-100, Thermo Fisher Scientific), stored at − 80 °C, and reconstituted in 600 µL D2O immediately before NMR analysis. The samples were transferred to 5 mm NMR tubes (SampleJet, Bruker Biospin GmbH), and analyzed on a 600 MHz Bruker Avance III NMR spectrometer (Bruker Biospin GmbH) with a 5 mm QCI Cryoprobe. Proton spectra were acquired at 300 K using 1D NOESY (Bruker: noesygppr1d) with presaturation and spoiler gradients as described previously (Itkonen et al. 2016 (link)). Data were collected with 32 scans and four dummy scans, Fourier transformed with an exponential line broadening of 0.3 Hz, baseline corrected using asymmetric least-squares method (Eilers 2004 (link)), and peak aligned using icoshift (Savorani et al. 2010 (link)). The water resonance and areas in the spectra with contamination and noise only were removed. All spectra were mean normalized and mean centered before principal component analysis was performed with PLS toolbox v8.2.1 (Eigenvector Research).
Pallasaho S., Gondane A., Kuivalainen A., Girmay S., Moestue S., Loda M, & Itkonen H.M. (2022). Castration-resistant prostate cancer cells are dependent on the high activity of CDK7. Journal of Cancer Research and Clinical Oncology, 149(8), 5255-5263.
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10

NMR Screening of SUMO1 Inhibitors

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Uniformly 15N-labeled mature SUMO1 was expressed and purified as described previously 14 (link). All 15N-SUMO1 samples (20 μM) used in the NMR screening experiments were in phosphate buffer (20 mM, 1 mM DTT, 90% H2O, 10% D2O, pH 6.8). For inhibitor screening, 15N-SUMO1 samples were added with 0.5, 1.0, and 2.0 mol equivalence of the compounds identified from the high throughput screen and transferred to the 96-well SampleJet tubes 5.0 mm (5.0×103.5 mm). 1H-15N-HSQC spectra of the samples were collected on Bruker Avance III spectrometer equipped with a cryoprobe operating at 700.243 MHz 1H frequency using the Bruker SampleJet automated sample changer. The weighted proton and nitrogen chemical shifts were calculated and quantified. The final concentrations of deuterated DMSO in all the samples after addition of the compounds were below 2% (v/v). All experiments were carried out at 298K. NMR data were processed using NMRPipe and analyzed with the program Sparky 15 (link).
Line shape analysis was carried out by using the software package LineShapeKin 13 (link). The 1D slices from the proton dimension in 1H-15N HSQC spectra were obtained at the SIMI-4:SUMO1 molar ratios of 0, 0.5, 1, 1.5, 2, 3, 4 from extraction using LineShapeKin SPARKY extension. Kd values were obtained from fitting line shape changes to the Bloch-McConnel equation for a 2-site exchange model.
Alontaga A.Y., Li Y., Chen C.H., Ma C.T., Malany S., Key D.E., Sergienko E., Sun Q., Whipple D.A., Matharu D.S., Li B., Vega R., Li Y.J., Schoenen F.J., Blagg B.S., Chung T.D, & Chen Y. (2015). Design of High Throughput Screening Assays and Identification of a SUMO1-Specific Small Molecule Chemotype Targeting the SUMO-Interacting Motif-Binding Surface. ACS combinatorial science, 17(4), 239-246.
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