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Nanomate device

Manufactured by Advion
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The Nanomate device is a versatile, high-performance laboratory equipment designed for precise liquid handling and sample preparation. Its core function is to automate the process of sample pipetting, dispensing, and mixing, enabling researchers to achieve consistent and reproducible results in their experiments.

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Lab products found in correlation

Q tof premier, by Waters Corporation (4 mentions) Nai clusters, by Waters Corporation (2 mentions) Isopropanol h2o 50 50, by Waters Corporation (2 mentions) Tsq altis, by Thermo Fisher Scientific (2 mentions) Xcalibur system, by Advion (2 mentions) Precellys evolution tissue homogenizer, by Bertin Technologies (2 mentions) Tsq vantage, by Advion (2 mentions) Electrospray q tof mass spectrometer, by Waters Corporation (2 mentions) Maxent algorithm, by AB Sciex (2 mentions) Triple quadrupole mass spectrometer, by Thermo Fisher Scientific (2 mentions) Bicinchoninic acid protein assay, by Thermo Fisher Scientific (1 mentions) Peakview 2, by AB Sciex (1 mentions) Masslynx 4, by Waters Corporation (1 mentions) Masslynx version 4, by Waters Corporation (1 mentions) Peakview version 2, by AB Sciex (1 mentions) Protein assay, by Bio-Rad (1 mentions)

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Nanomate (29 citations)

12 protocols using nanomate device

1

Purification and Characterization of Nopaline and Pyronopaline

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Nopaline was extracted from crushed tomato plant tumour tissues and purified according to the procedure described by Tempé [42] . Pyronopaline was obtained by synthesis using arginine and α-KG as precursors in the presence of sodium cyanoborohydride as described by Tempé [42] . This synthesis resulted in a mix of nopaline and pyronopaline. The complete conversion of this mix into pyronopaline was obtained as described previously [17] (link). The quantification of nopaline was performed as previously described [31] (link) from macerates of whole tomato tumours.
All solutions of nopaline, pyronopaline and nopaline/pyronopaline were checked by mass spectrometry. The mass spectrometry measurements were performed in negative mode with an electrospray Q/TOF mass spectrometer (Q/TOF Premier, Waters) equipped with the Nanomate device (Advion) with compounds diluted in 50% acetonitrile and 1% formic acid. The Mass Lynx 4.1 software was used for acquisition and data processing. The external calibration was performed with NaI clusters (2 µg/µL, isopropanol/H2O 50/50, Waters) in the acquisition m/z mass range and the estimated mass accuracy is ±0.01 Da (at 300 Da). The spectra of nopaline and pyronopaline are shown in the figure S5.
Lang J., Vigouroux A., Planamente S., El Sahili A., Blin P., Aumont-Nicaise M., Dessaux Y., Moréra S, & Faure D. (2014). Agrobacterium Uses a Unique Ligand-Binding Mode for Trapping Opines and Acquiring A Competitive Advantage in the Niche Construction on Plant Host. PLoS Pathogens, 10(10), e1004444.
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2

Native Mass Spectrometry of Protein Complexes

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Mass spectrometry measurements were performed with an electrospray Q/TOF mass spectrometer (Q/TOF Premier, Waters) equipped with the Nanomate device (Advion). The HD_A_384 chip (5 μm I.D.nozzle chip, flow rate range 100−500 nL/min) was calibrated before use. For ESI−MS measurements, the Q/TOF instrument was operated in RF quadrupole mode with the TOF data being collected between m/z 400−2990 and 1000-6000 for denaturant and native conditions respectively. Collision energy was set to 10 eV and argon was used as collision gas. Mass spectra acquisition was performed after denaturation of protein (±)-GR24 in 50% acetonitrile and 1% formic acid. In native conditions, mass spectra of RMS3 (50 μM) in 50 mM ammonium acetate in presence or without (±)-GR24 (50 to 500 μM) were acquired with backing and cone voltage set at 4 mBar and 120 V respectively. The Mass Lynx 4.1 software was used for acquisition and data processing. Deconvolution of multiply charged ions was performed by applying the MaxEnt1 algorithm. The protein average masses are annotated in the spectra (Fig. 5), and the estimated mass accuracy is ± 2 Da. External calibration was performed with NaI clusters (2 μg/μL, isopropanol/H2O 50/50, Waters) in the acquisition m/z mass range.
de Saint Germain A., Clavé G., Badet-Denisot M.A., Pillot J.P., Cornu D., Le Caer J.P., Burger M., Pelissier F., Retailleau P., Turnbull C., Bonhomme S., Chory J., Rameau C, & Boyer F.D. (2016). An histidine covalent receptor/butenolide complex mediates strigolactone perception. Nature chemical biology, 12(10), 787-794.
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3

Native Mass Spectrometry of Protein Complexes

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Mass spectrometry measurements were performed with an electrospray Q/TOF mass spectrometer (Q/TOF Premier, Waters) equipped with the Nanomate device (Advion). The HD_A_384 chip (5 μm I.D.nozzle chip, flow rate range 100−500 nL/min) was calibrated before use. For ESI−MS measurements, the Q/TOF instrument was operated in RF quadrupole mode with the TOF data being collected between m/z 400−2990 and 1000-6000 for denaturant and native conditions respectively. Collision energy was set to 10 eV and argon was used as collision gas. Mass spectra acquisition was performed after denaturation of protein (±)-GR24 in 50% acetonitrile and 1% formic acid. In native conditions, mass spectra of RMS3 (50 μM) in 50 mM ammonium acetate in presence or without (±)-GR24 (50 to 500 μM) were acquired with backing and cone voltage set at 4 mBar and 120 V respectively. The Mass Lynx 4.1 software was used for acquisition and data processing. Deconvolution of multiply charged ions was performed by applying the MaxEnt1 algorithm. The protein average masses are annotated in the spectra (Fig. 5), and the estimated mass accuracy is ± 2 Da. External calibration was performed with NaI clusters (2 μg/μL, isopropanol/H2O 50/50, Waters) in the acquisition m/z mass range.
de Saint Germain A., Clavé G., Badet-Denisot M.A., Pillot J.P., Cornu D., Le Caer J.P., Burger M., Pelissier F., Retailleau P., Turnbull C., Bonhomme S., Chory J., Rameau C, & Boyer F.D. (2016). An histidine covalent receptor/butenolide complex mediates strigolactone perception. Nature chemical biology, 12(10), 787-794.
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4

Cerebral Lipid Profiling by Mass Spectrometry

Cited 3 times
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Briefly, fresh and/or frozen cerebral tissue was homogenized in ice-cold 0.1 × phosphate-buffered saline (PBS) using Precellys® Evolution Tissue Homogenizer (Bertin, France) as previously described [18 (link)]. Protein concentration of homogenates was determined using the bicinchoninic acid protein assay (Thermo Fisher Scientific, New York, NY, USA). Lipids were extracted by a modified procedure of Bligh and Dyer extraction in the presence of internal standards, which were added based on the total protein content of each sample [57 (link),58 (link),59 (link)]. Lipids were assessed using a triple-quadrupole mass spectrometer (TSQ Altis (Thermo Fisher Scientific, Waltham, MA, USA) equipped with a Nanomate device (Advion, Ithaca, NY, USA) and Xcalibur system as previously described [60 (link),61 (link),62 (link)]. Data processing including ion peak selection, baseline correction, data transfer, peak intensity comparison, 13C deisotoping, and quantitation were conducted using a custom programmed Microsoft Excel macro as previously described after considering the principles of lipidomics [61 (link),62 (link)].
Palavicini J.P., Ding L., Pan M., Qiu S., Wang H., Shen Q., Dupree J.L, & Han X. (2022). Sulfatide Deficiency, an Early Alzheimer’s Lipidomic Signature, Causes Brain Ventricular Enlargement in the Absence of Classical Neuropathological Hallmarks. International Journal of Molecular Sciences, 24(1), 233.
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5

Intact Protein Mass Spectrometry

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Mass spectrometry (MS) measurements were performed with an electrospray Q/TOF mass spectrometer (Q/TOF Premier, Waters) equipped with the Nanomate device (Advion). The HD_A_384 chip (5 μm I.D. nozzle chip, flow-rate range 100−500 nL/min) was calibrated before use. The Q/TOF instrument was operated in the RF quadrupole mode and data were acquired in the 400–3990 m/z range. Collision energy was set to 6 eV and argon was used as collision gas. Mass spectrometry of the intact proteins was performed after 5 min denaturation in 50% acetonitrile and 1% formic acid. Acquisition and data processing were performed with Mass Lynx 4.1 software. Deconvolution of multiply charged ions was performed by applying the MaxEnt1 algorithm. The average protein masses are annotated in the spectra, and the estimated mass accuracy is ± 2 Da. External calibration was performed with NaI clusters (2 μg/μL in 50/50 v/v isopropanol/water) in the same m/z range.
Hai J., Serradji N., Mouton L., Redeker V., Cornu D., El Hage Chahine J.M., Verbeke P, & Hémadi M. (2016). Targeted Delivery of Amoxicillin to C. trachomatis by the Transferrin Iron Acquisition Pathway. PLoS ONE, 11(2), e0150031.
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6

Lipid Analysis by Triple-Quadrupole Mass Spectrometry

Cited 2 times
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A triple-quadrupole mass spectrometer (Thermo Scientific TSQ Vantage, CA, USA) equipped with a Nanomate device (Advion Bioscience Ltd., NY, USA) and Xcalibur system software was used as previously described [47 (link), 133 (link)]. Diluted lipid extracts were directly infused into the ESI source through a Nanomate device [47 (link)]. Typically, signals were averaged over a 1-min period in the profile mode for each full scan MS spectrum. For tandem MS, a collision gas pressure was set at 1.0 mTorr, but the collision energy varied with the classes of lipids as described previously [45 (link), 133 (link)]. Similarly, a 2- to 5-min period of signal averaging in the profile mode was employed for each tandem MS mass spectrum. All full and tandem MS mass spectra were automatically acquired using a customized sequence subroutine operated under Xcalibur software. Data processing including ion peak selection, baseline correction, data transfer, peak intensity comparison, 13C deisotoping, and quantitation were conducted using a custom programmed Microsoft Excel macro as previously described [133 (link)] after considering the principles of lipidomics [125 ].
Palavicini J.P., Wang C., Chen L., Hosang K., Wang J., Tomiyama T., Mori H, & Han X. (2017). Oligomeric amyloid-beta induces MAPK-mediated activation of brain cytosolic and calcium-independent phospholipase A2 in a spatial-specific manner. Acta Neuropathologica Communications, 5, 56.
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7

Q-TOF Mass Spectrometry of CpD14 Protein

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Mass spectrometry measurements were performed with an electrospray Q‐TOF mass spectrometer (Waters) equipped with the Nanomate device (Advion Inc., Ithaca, NY, USA). The HD_A_384 chip (5 µm I.D. nozzle chip, flow rate range 100–500 nl min−1) was calibrated before use. For ESI‐MS measurements, the Q‐TOF instrument was operated in RF quadrupole mode with the TOF data being collected between m/z 400 and 2990. Collision energy was set to 10 eV, and argon was used as collision gas. Mass spectra acquisition was performed after denaturation of CpD14 ± ligand in 50% acetonitrile and 1% formic acid using Mass Lynx 4.1 (Waters) and Peakview 2.2 (Sciex). Deconvolution of multiply‐charged ions was performed by applying the MaxEnt algorithm (Sciex). The estimated mass accuracy is ± 2 Da. External calibration was performed with NaI clusters (2 µg µl−1, isopropanol : H2O, 50 : 50; Waters) in the acquisition m/z mass range.
Fiorilli V., Forgia M., de Saint Germain A., D’Arrigo G., Cornu D., Le Bris P., Al‐Babili S., Cardinale F., Prandi C., Spyrakis F., Boyer F., Turina M, & Lanfranco L. (2022). A structural homologue of the plant receptor D14 mediates responses to strigolactones in the fungal phytopathogen Cryphonectria parasitica. The New Phytologist, 234(3), 1003-1017.
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8

Mass spectrometry analysis of PsKAI2 protein

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Mass spectrometry measurements were performed with an electrospray Q-TOF mass spectrometer (Waters) equipped with the Nanomate device (Advion, Inc.). The HD_A_384 chip (5 μm I.D. nozzle chip, flow rate range 100−500 nL/min) was calibrated before use. For ESI − MS measurements, the Q-TOF instrument was operated in RF quadrupole mode with the TOF data being collected between m/z 400 and 2990. Collision energy was set to 10 eV and argon was used as the collision gas. PsKAI2 proteins (50 µM) in 50 mM ammonium acetate (pH 6.8) in presence or without (-)-GR24 (500 µM) were incubated for 10 min at room temperature before denaturation in 50% acetonitrile and 1% formic acid. The solutions were directly injected for Mass spectra acquisition or digested before LC-MS/MS analyses. Mass Lynx version 4.1 (Waters) and Peakview version 2.2 (Sciex) software were used for acquisition and data processing, respectively. Deconvolution of multiply charged ions was performed by applying the MaxEnt algorithm (Sciex). The average protein masses were annotated in the spectra and the estimated mass accuracy was ± 2 Da. External calibration was performed with NaI clusters (2 μg/μL, isopropanol/H2O 50/50, Waters) in the acquisition m/z mass range.
Guercio A.M., Torabi S., Cornu D., Dalmais M., Bendahmane A., Le Signor C., Pillot J.P., Le Bris P., Boyer F.D., Rameau C., Gutjahr C., de Saint Germain A, & Shabek N. (2022). Structural and functional analyses explain Pea KAI2 receptor diversity and reveal stereoselective catalysis during signal perception. Communications Biology, 5, 126.
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9

Shotgun Lipidomics for Molecular Lipid Profiling

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Lipid analysis was performed using multi‐dimensional mass spectrometry‐based shotgun lipidomics as previously described.26 Briefly, frozen samples were weighed and homogenized in diluted PBS. Protein concentration was determined using bicinchoninic acid (BCA) assay. An equal amount of homogenate from individual samples based on protein content was used for lipid extraction using a modified procedure of Bligh and Dyer extraction in the presence of internal standards. The levels of lipid molecular species were assessed using a triple‐quadrupole mass spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) equipped with a Nanomate device (Advion, Ithaca, NY, USA) and Xcalibur system as previously described.27 Subsequent data processing was conducted using a custom‐programmed Microsoft Excel macro as previously described.28
He S., Qiu S., Pan M., Palavicini J.P., Wang H., Li X., Bhattacharjee A., Barannikov S., Bieniek K.F., Dupree J.L, & Han X. (2023). Central nervous system sulfatide deficiency as a causal factor for bladder disorder in Alzheimer's disease. Clinical and Translational Medicine, 13(7), e1332.
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10

Multidimensional Lipidomic Analysis of Tissues

Cited 2 times
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Multidimensional mass spectrometry-based shotgun lipidomics was performed as previously described [50 (link)]. Briefly, frozen brain, spinal cord, or sciatic nerve tissues were homogenized in ice-cold phosphate-buffered saline (PBS) using Precellys® Evolution Tissue Homogenizer (Bertin, France). The protein concentration of homogenates was determined using the Bio-Rad protein assay (Bio-Rad, Hercules, CA, USA). Lipids were extracted by a modified procedure of Bligh and Dyer extraction in the presence of internal standards, which were added based on the total protein content of each sample [51 (link)]. Lipids were assessed using a triple-quadrupole mass spectrometer (TSQ Altis, (Thermo Fisher Scientific, Waltham, MA, USA) equipped with a Nanomate device (Advion Ithaca, NY, USA) and Xcalibur system as previously described [52 (link)]. Data processing including ion peak selection, baseline correction, data transfer, peak intensity comparison, 13C deisotoping, and quantitation were conducted using a custom-programmed Microsoft Excel macro as previously described [53 (link)].
Qiu S., Palavicini J.P., Wang J., Gonzalez N.S., He S., Dustin E., Zou C., Ding L., Bhattacharjee A., Van Skike C.E., Galvan V., Dupree J.L, & Han X. (2021). Adult-onset CNS myelin sulfatide deficiency is sufficient to cause Alzheimer’s disease-like neuroinflammation and cognitive impairment. Molecular Neurodegeneration, 16, 64.
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