Nanospray flex

Manufactured by Thermo Fisher Scientific

Sourced in United States, Germany

The Nanospray Flex is a piece of lab equipment designed for nanoscale liquid sample introduction into mass spectrometers. It provides a reliable and reproducible method for analyzing small sample volumes.

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Nanospray Flex Ion Source (84 citations) Nanospray Flex source (24 citations) Nanospray Flex NG (7 citations) Nanospray Flex ion (6 citations) Nanospray Flex Ion Source ES071 (4 citations) Nanospray Flex™ ESI (3 citations)

76 protocols using nanospray flex

Nanoscale LC-MS/MS Peptide Identification

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Peptide digests (8 µL each) were injected onto a 1260 Infinity nHPLC stack (Agilent Technologies) and separated using a 75 micron I.D. x 15 cm pulled tip C-18 column (Jupiter C-18 300 Å, 5 micron, Phenomenex). This system runs in-line with a Thermo Orbitrap Velos Pro hybrid mass spectrometer, equipped with a Nanospray FlexTM ion source (Thermo Fisher Scientific), and all data were collected in CID mode. The nHPLC is configured with binary mobile phases that includes solvent A (0.1% FA in ddH2O), and solvent B (0.1% FA in 15% ddH2O/85% ACN), programmed as follows; 10 min @ 5% B (2 µL/ min, load), 90 min @ 5–40% B (linear: 0.5nL/min, analyze), 5 min @ 70% B (2 µL/ min, wash), 10 min @ 0% B (2 µL/min, equilibrate). Following parent ion scan (300–1200 m/z @ 60 k resolution), fragmentation data (MS2) was collected on the most intense 15 ions. For data dependent scans, charge state screening and dynamic exclusion were enabled with a repeat count of 2, repeat duration of 30 s, and exclusion duration of 90 s.

Kim H.S., Parker D.J., Hardiman M.M., Munkácsy E., Jiang N., Rogers A.N., Bai Y., Brent C., Mobley J.A., Austad S.N, & Pickering A.M. (2023). Early-adulthood spike in protein translation drives aging via juvenile hormone/germline signaling. Nature Communications, 14, 5021.

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Peptide Identification by Orbitrap LC-MS/MS

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Peptide digests (8 μL each) were injected onto a 1260 Infinity nHPLC stack (Agilent Technologies), and separated using a 75 μm inside diameter x 15 cm pulled tip C-18 column (Jupiter C-18 300 Å, 5 micron, Phenomenex). This system runs in-line with a Thermo Orbitrap Velos Pro hybrid mass spectrometer, equipped with a Nanospray Flex^TM ion source (Thermo Fisher Scientific); all data were collected in collision-induced dissociation mode. The nano-High Performance Liquid Chromatography is configured with binary mobile phases that includes solvent A (0.1%FA in ddH₂O), and solvent B (0.1%FA in 15% ddH₂O / 85% ACN), programmed as follows; 10min @ 5%B (2μL/ min, load), 90min @ 5%-40%B (linear: 0.5nL/ min, analyze), 5min @ 70%B (2μL/ min, wash), 10min @ 0%B (2μL/ min, equilibrate). Following each parent ion scan (300-1200m/z @ 60k resolution), fragmentation data (MS2) were collected on the top most intense 15 ions. For data dependent scans, charge state screening and dynamic exclusion were enabled with a repeat count of 2, repeat duration of 30 s, and exclusion duration of 90 s.

Xia Q.Q., Walker A.K., Song C., Wang J., Singh A., Mobley J.A., Xuan Z.X., Singer J.D, & Powell C.M. (2023). Effects of heterozygous deletion of autism-related gene Cullin-3 in mice. PLOS ONE, 18(7), e0283299.

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Positive-mode nanoESI-Orbitrap MS

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Electrospray ionization mass spectrometry (ESI-MS) was carried out in positive ion mode using a Q Exactive Hybrid Quadrupole-Orbitrap mass spectrometer (Thermo Fisher Scientific) equipped with the Nanospray Flex^TM ion source. The nanoflow ESI (nanoESI) was performed using tips pulled from a borosilicate capillary (1.0 mm o.d., 0.75 mm i.d.) by a micropipette puller (P-1000, Sutter Instruments). A voltage of 0.9 kV was applied to a platinum wire inserted into the nanoESI tip and in contact with the sample solution. The capillary temperature 160°C, maximum inject time 200 ms, microscans 10, S-lens RF level 100, and resolution 17,000 were applied, whereas other instrument parameters were set at default values. Data acquisition and processing were performed using Xcalibur (Thermo Fisher Scientific, version 4.4).

Xia M., Vago F., Han L., Huang P., Nguyen L., Boons G.J., Klassen J.S., Jiang W, & Tan M. (2023). The αTSR Domain of Plasmodium Circumsporozoite Protein Bound Heparan Sulfates and Elicited High Titers of Sporozoite Binding Antibody After Displayed by Nanoparticles. International Journal of Nanomedicine, 18, 3087-3107.

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Quantitative Proteomics Analysis by LCMS

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The experiments were performed using a Thermo Scientific (Rockford, IL, U.S.A.) Quantum Access triple quadrupole equipped with a stripped Nanospray Flex TM ESI source (Thermo Scientific) (Figure 1). The heated capillary was operated at 60 °C without ionizing voltage applied, similar to previous work. 7, (link)11 (link) Data was collected by selected reaction monitoring using the transitions and collision energies described in Table 1. Argon was used for collision induced dissociation (CID) at a gas pressure of 1.5 mTorr (except for in analysis of NLLGLIEAK and NLLGLIEA[K_ 13 C6_ 15 N2] where the CID gas pressure was 1.7 mTorr.

Skjaervø Ø., Trimpin S, & Halvorsen T.G. (2021). Matrix-assisted ionization mass spectrometry in targeted protein analysis - An initial evaluation. Rapid communications in mass spectrometry : RCM, 35 Suppl 1.

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Proteomics Analysis: Peptide, Glycopeptide, and Phosphopeptide Identification

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EASY‐nLC 1000 UHPLC (Thermo Scientific) interfaced via a Nanospray Flex ion source to an LTQ‐Orbitrap Velos Pro or Orbitrap Fusion spectrometer (Thermo Scientific) was used for peptide, glycopeptide, and phosphopeptide analysis as described previously 27. Data were processed using Proteome Discoverer 1.4 software (Thermo Scientific).

Bagdonaite I., Pallesen E.M., Ye Z., Vakhrushev S.Y., Marinova I.N., Nielsen M.I., Kramer S.H., Pedersen S.F., Joshi H.J., Bennett E.P., Dabelsteen S, & Wandall H.H. (2020). O‐glycan initiation directs distinct biological pathways and controls epithelial differentiation. EMBO Reports, 21(6), e48885.

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Native MS Analysis of Antibody-Antigen Complexes

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Native MS was performed as described [54 (link)] with minor modifications. Briefly, stock solutions of STEBVax and IgG-GC132a were buffer-exchanged to 150 mM ammonium acetate (pH 6.8) using Vivaspin 500 centrifugal concentrators (Sartorius, Göttingen, Germany). The working solution was prepared by mixing Ab and antigen solutions with a molar ratio of ~2:1 and a final total protein concentration of ~2 μM. The solution was loaded into NanoES spray capillaries (Thermo Fisher Scientific) on a Nanospray Flex ion source (Thermo Fisher Scientific). Mass spectra were collected on an Exactive Plus EMR mass spectrometer (Thermo Fisher Scientific). The in-source collisional ionization dissociation energy was 20 eV, spray voltage was 1.3 kV, capillary temperature was 100 °C and collision energy was 100 or 200 a.u.

Chen G., Karauzum H., Long H., Carranza D., Holtsberg F.W., Howell K.A., Abaandou L., Zhang B., Jarvik N., Ye W., Liao G.C., Gross M.L., Leung D.W., Amarasinghe G.K., Aman M.J, & Sidhu S.S. (2019). Potent Neutralization of Staphylococcal Enterotoxin B in vivo by antibodies that block binding to the T-cell receptor. Journal of molecular biology, 431(21), 4354-4367.

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Nano-UHPLC-MS/MS Protocol for Peptide Analysis

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Samples were analyzed on an Easy nLC-1200 nano UHPLC (Thermo Fisher Scientific) coupled online via a Nanospray Flex electrospray ion source (Thermo Fisher Scientific) equipped with a column oven (Sonation) to a Q-Exactive HF mass spectrometer (Thermo Fisher Scientific). An amount of 1.3 µg of peptides was separated on self-packed C18 columns (300 mm × 75 µm, ReproSilPur 120 C18-AQ, 1.9 µm; Dr Maisch) using a binary gradient of water (A) and acetonitrile (B) supplemented with 0.1% formic acid (gradient: 0 min, 2.4% B; 2 min, 4.8% B; 92 min, 24% B; 112 min, 35.2% B; 121 min, 60% B). Full mass spectrometry spectra were acquired at a resolution of 120,000 (automatic gain control target, 3 × 10⁶). The 15 most-intense peptide ions were chosen for fragmentation by higher-energy collisional dissociation (resolution, 15,000; isolation width, 1.6 m/z; automatic gain control target, 1 × 10⁵; normalized collision energy, 26%). A dynamic exclusion of 120 s was applied for fragment ion spectra acquisition. For EAE samples, two technical replicates were measured per sample.

Tai Y.H., Engels D., Locatelli G., Emmanouilidis I., Fecher C., Theodorou D., Müller S.A., Licht-Mayer S., Kreutzfeldt M., Wagner I., de Mello N.P., Gkotzamani S.N., Trovò L., Kendirli A., Aljović A., Breckwoldt M.O., Naumann R., Bareyre F.M., Perocchi F., Mahad D., Merkler D., Lichtenthaler S.F., Kerschensteiner M, & Misgeld T. (2023). Targeting the TCA cycle can ameliorate widespread axonal energy deficiency in neuroinflammatory lesions. Nature Metabolism, 5(8), 1364-1381.

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Peptide Separation and Identification by nHPLC-MS

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Peptide digests (8µL each) were injected onto a 1260 Infinity nHPLC stack (Agilent Technologies), and separated using a 75 micron I.D. x 15 cm pulled tip C-18 column (Jupiter C-18 300 Å, 5 micron, Phenomenex). This system runs in-line with a Thermo Q Exactive HFx mass spectrometer, equipped with a Nanospray Flex™ ion source (Thermo Fisher Scientific), and all data were collected in CID mode. The nHPLC is configured with binary mobile phases that includes solvent A (0.1%FA in ddH₂O), and solvent B (0.1%FA in 15% ddH₂O/85% ACN), programmed as follows; 10min @ 5%B (2µL/min, load), 30min @ 5%-40%B (linear: 0.5nL/min, analyze), 5min @ 70%B (2µL/min, wash), 10min @ 0%B (2µL/min, equilibrate). Following each parent ion scan (300-1200m/z @ 60k resolution), fragmentation data (MS2) were collected on the top most intense 18 ions @7.5K resolution. For data dependent scans, charge state screening and dynamic exclusion were enabled with a repeat count of 2, repeat duration of 30s, and exclusion duration of 90s.

Starr C.R., Zhylkibayev A., Mobley J.A, & Gorbatyuk M.S. (2023). Proteomic analysis of diabetic retinas. Frontiers in Endocrinology, 14, 1229089.

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Sheathless Capillary Electrophoresis-MS

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Separation was performed using a CESI 8000 (SCIEX, Brea, CA) on a bare fused silica capillary (90 cm, 30 μm ID, 150 μm OD) with a sheathless electrospray interface (SCIEX OptiMS cartridge). A 3 min ramp was applied to reach the separation voltage of +20 kV in normal polarity. MS acquisition was started after the initial 3 min CE voltage ramp up and ended at the start of a 5 min CE voltage ramp down. The BGE used was 40% acetic acid, and the conductive line was filled with 10% acetic acid. A supplemental pressure of 1 psi was applied throughout the 75 min run time. The capillary was interfaced with a Nanospray Flex ion source mounted at the front end of an Orbitrap Fusion Lumos Tribrid mass spectrometer (both Thermo Fisher Scientific).

Grilli M., Diodato E., Lozza G., Brusa R., Casarini M., Uberti D., Rozmahel R., Westaway D., St George-Hyslop P., Memo M, & Ongini E. (2000). Presenilin-1 regulates the neuronal threshold to excitotoxicity both physiologically and pathologically. Proceedings of the National Academy of Sciences of the United States of America, 97(23), 12822-12827.

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Peptide Identification by LC-MS/MS

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Liquid chromatography–tandem
mass spectrometry (MS/MS) was performed on a Q Exactive Plus equipped
with an ultrahigh-pressure liquid chromatography unit Easy-nLC1000
and a Nanospray Flex ion source (all three from Thermo Fisher Scientific).
Peptides were separated on an in-house-packed column (100 μm
inner diameter, 30 cm length, 2.4 μm Reprosil-Pur C18 resin
from Dr. Maisch GmbH, Germany) using a gradient from mobile phase
A (4% acetonitrile and 0.1% formic acid) to 30% mobile phase B (80%
acetonitrile and 0.1% formic acid) for 60 min followed by a second
step to 60% B for 30 min, with a flow rate of 300 nL/min. MS data
were recorded in data-dependent mode by selecting the 10 most abundant
precursor ions for HCD with a normalized collision energy of 27. The
full MS scan range was set from 350 to 2000 m/z with a resolution of 70 000. Ions with a charge
of ≥2 were selected for a tandem MS scan with a resolution
of 17 500 and an isolation window of 2 m/z. The maximum ion injection time for the survey scan and
the MS/MS scans was 80 ms, and the ion target values were set to 3
× 10⁶ and 1 × 10⁵, respectively. Dynamic
exclusion of selected ions was set to 60 s. Data were acquired using
Xcalibur software (Thermo Fisher Scientific).

Lang W.H., Calloni G, & Vabulas R.M. (2018). Polylysine is a Proteostasis Network-Engaging Structural Determinant. Journal of Proteome Research, 17(5), 1967-1977.

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