Nanoelectrospray ion source

Manufactured by New Objective

Sourced in United States

The Nanoelectrospray ion source is a compact and versatile device used in mass spectrometry applications. It generates a fine spray of charged particles from a liquid sample, allowing for efficient ionization and transfer of analytes into the mass spectrometer for analysis.

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Lab products found in correlation

Orbitrap fusion mass spectrometer, by Thermo Fisher Scientific (2 mentions) Ultimate 3000 rslc system, by Thermo Fisher Scientific (1 mentions) Protein assay kit, by Bio-Rad (1 mentions) Ripa lysis and extraction buffer, by Thermo Fisher Scientific (1 mentions) Agilent 1100 series, by Agilent Technologies (1 mentions) Agilent 1100 series binary hplc pump, by Agilent Technologies (1 mentions) Ltq ft icr ms, by Thermo Fisher Scientific (1 mentions) Magic c18aq resin, by Bruker (1 mentions) Tsq vantage triple quadrupole mass spectrometer, by Thermo Fisher Scientific (1 mentions) Easy nlc 2 system, by Thermo Fisher Scientific (1 mentions) Picochip, by New Objective (1 mentions)

6 protocols using nanoelectrospray ion source

Proteomic Profiling of CD18 Glycosylation

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The purified CD18 was excised from the coomassie-stained gel and in-gel digested by trypsin. The digested peptides were extracted by gradient acetonitrile (ACN) with 0.1% trifluoroacetic acid (TFA) from 10% to 100% ACN. The extracted peptides were pooled and speedvac dried. Then the peptides were desalted using Sep-Pak tC18 1 cc Vac cartridge (WAT054960). In brief, the columns were pre-equilibrated using 1 ml 100% ACN and washed with 0.1% TFA twice. The digested peptides were added to 200 μl with 0.1% TFA and load into the columns and washed with 1 ml 0.1% TFA twice, followed with 200 μl 0.5% acetic acid. The digested peptides were eluted using 75% ACN/0.5% acetic acid. The eluted peptides were dried in speedvac and then dissolved in 0.1% formic acid for nanoLC-MS/MS using an Orbitrap Fusion mass spectrometer (Thermo Scientific) equipped with a nanoelectrospray ion source (New Objective) and an UltiMate 3,000 RSLCnano system pump (Thermo Scientific Dionex). PMI-Byonic was used for the MS/MS-based protein and glycosylation site identification⁴⁷. Methionine oxidation was enabled as a variable modification. O-glycopeptides were searched against 78 mammalian and 70 human databases.

Uhrig J.F., Soellick T.R., Minke C.J., Philipp C., Kellmann J.W, & Schreier P.H. (1999). Homotypic interaction and multimerization of nucleocapsid protein of tomato spotted wilt tospovirus: Identification and characterization of two interacting domains. Proceedings of the National Academy of Sciences of the United States of America, 96(1), 55-60.

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Proteomic Alterations in Cancer Cells

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Proteomic alterations in FaDu and OECM-1 cells induced by macrophage coculture were identified by mass spectrometric (MS) analysis. Total proteins were extracted from FaDu and OECM-1 cells using RIPA lysis and extraction buffer (Thermo Fisher Scientific) and sonication. Protein concentrations were determined using Bio-Rad Protein Assay kits by measuring absorbance at 595 nm. Total protein samples (40 μg) were separated using 10% SDS-PAGE and divided into 5 gel fractions. After fine cutting (<1 mm³), gel pieces were subjected to in-gel digestion to produce tryptic peptides. An Orbitrap Fusion mass spectrometer (Thermo Fisher Scientific) equipped with the Ultimate 3000 RSLC system (Dionex) and a nano-electrospray ion source (New Objective) was used for MS analysis. The survey scan was set at a mass range (m/z) of 375–1,500 (automatic gain control target, 4 × 10⁵) and resolution of 120,000 at m/z 200. The 20 most abundant multiple-charged ions were sequentially fragmented by collision-induced dissociation for tandem mass analysis. Protein identification and label-free quantification were performed using the computational platform, Proteome Discovery (v2.4). The identification threshold was set at a P < 0.05.

Hsieh C.Y., Lin C.C., Huang Y.W., Chen J.H., Tsou Y.A., Chang L.C., Fan C.C., Lin C.Y, & Chang W.C. (2022). Macrophage secretory IL-1β promotes docetaxel resistance in head and neck squamous carcinoma via SOD2/CAT-ICAM1 signaling. JCI Insight, 7(23), e157285.

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Phosphorylation Site Mapping of TssL Protein

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Phosphorylation site mapping was determined by in-gel trypsin or trypsin/chymotrypsin digestion of purified TssL-His followed by nanoLC/nanospray/tandem mass spectrometry (LC-ESI/MS/MS) analysis. TssL-His proteins expressed in A. tumefaciens were purified by use of Ni-NTA resins and separated by 12% SDS-PAGE followed by Coomassie blue staining. TssL-His protein bands were cut out for in-gel trypsin or trypsin/chymotrypsin digestion as described [58] (link), [59] (link). The extracted tryptic peptides were subjected to the LC separation followed by a linear quadrupole ion trap-Fourier transform (LTQ-FT) ion cyclotron resonance mass spectrometer (Thermo Fisher Scientific) equipped with a nanoelectrospray ion source (New Objective, Woburn, MA, USA) for protein identification and phosphorylation site mapping.

Lin J.S., Wu H.H., Hsu P.H., Ma L.S., Pang Y.Y., Tsai M.D, & Lai E.M. (2014). Fha Interaction with Phosphothreonine of TssL Activates Type VI Secretion in Agrobacterium tumefaciens. PLoS Pathogens, 10(3), e1003991.

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LTQ-FT ICR Mass Spectrometry Protocol

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MS/MS experiments were performed as previously reported (Chang et al., 2010 (link)). Briefly, MS/MS was performed with an LTQ-Fourier transform (FT) ion cyclotron resonance (ICR) mass spectrometer (Thermo Electron) equipped with a nanoelectrospray ion source (New Objective), an Agilent 1100 series binary high-performance liquid chromatography (HPLC) pump (Agilent Technologies), and a Famos autosampler (LC Packings). A minimum threshold of 1,000 counts was used as the cutoff for MS/MS sequential isolation by the LTQ, with singly charged ions rejected for MS/MS sequencing.

Wang W.B., Yen M.L., Liu K.J., Hsu P.J., Lin M.H., Chen P.M., Sudhir P.R., Chen C.H., Chen C.H., Sytwu H.K, & Yen B.L. (2015). Interleukin-25 Mediates Transcriptional Control of PD-L1 via STAT3 in Multipotent Human Mesenchymal Stromal Cells (hMSCs) to Suppress Th17 Responses. Stem Cell Reports, 5(3), 392-404.

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Label-free Quantification of Proteins by LC-MS/MS

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Mass spectrometer analysis was performed using the linear ion trap-Fourier transform ion cyclotron resonance mass spectrometer (LTQ-FTICR MS; Thermo Fisher) equipped with a nano-electrospray ion source (New Objective) and a nano-HPLC system. Nano-HPLC separation used a reverse nano-column (75 μm I.D. × 200 mm) packaged with Magic C18AQ resin (particle size 5 μm, pore size 200 A°; Michrom Bioresources) and an Agilent 1100 series binary HPLC pump (Agilent Technologies). The analytic program was set at a linear gradient from 10% to 50% ACN with a 60 min running cycle. The survey scan of MS analysis (m/z 320–2,000) was performed in LTQ-FTICR MS with a mass resolution of 100,000 at m/z 400. Top ten most abundant multiply charged ions were sequentially isolated for MS/MS by LTQ. The resulting data were applied to the MaxQuant software [23 (link)] for protein identification. Accurate label-free quantification was performed using the MaxLFQ program by normalization and maximal peptide ratio extraction methods [24 (link)]. The significance threshold for the identification was set to P < .01.

Tsai S.T., Wang P.J., Liou N.J., Lin P.S., Chen C.H, & Chang W.C. (2015). ICAM1 Is a Potential Cancer Stem Cell Marker of Esophageal Squamous Cell Carcinoma. PLoS ONE, 10(11), e0142834.

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Targeted Peptide Quantification by LC-MS

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The SRM measurements were performed on a TSQ Vantage triple quadrupole mass spectrometer (Thermo Fisher Scientific Inc, San Jose, CA, USA) equipped with a nano electrospray ion source (New Objective, Woburn, MA, USA), mass spectrometric settings were previously described 19 . Chromatographic separations of peptides were preformed on an Easy-nLC II system (Thermo Fisher Scientific Inc.), the non-linear gradient ranging from 3-10% acetonitrile over 3 minutes and from 10-32% acetonitrile over 34 minutes with a flow-rate of 300nl/min. PicoChip (New Objective) columns packed with Reprosil-PUR C18, a length of 105 mm, inner diameter of 75 μm and a tip size of 15 μm were used.

Säll A., Sjöholm K., Waldemarson S., Happonen L., Karlsson C., Persson H, & Malmström J. (2015). Development of Phage-Based Antibody Fragment Reagents for Affinity Enrichment of Bacterial Immunoglobulin G Binding Proteins. Journal of proteome research, 14(11).

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