Nano easy lc

Manufactured by Thermo Fisher Scientific

Sourced in Germany

The Nano-Easy LC is a liquid chromatography system designed for capillary and nano-scale separations. It provides precise and reproducible solvent delivery for microscale liquid chromatography applications.

Automatically generated - may contain errors

Lab products found in correlation

Q exactive mass spectrometer, by Thermo Fisher Scientific (2 mentions) Q exactive hf x mass spectrometer, by Thermo Fisher Scientific (1 mentions) Reprosil pur 120 c18 aq, by Dr. Maisch (1 mentions) Amazon etd ion trap, by Bruker (1 mentions) Strav mag sepharose, by GE Healthcare (1 mentions) Illustrator 2022, by Adobe (1 mentions) Complete protease inhibitor cocktail, by Roche (1 mentions) Q exactive hf mass spectrometer, by Thermo Fisher Scientific (1 mentions) C18 material, by Dr. Maisch (1 mentions)

Close spelling variants of this product

Easy-nLC 1000 nano-LC EASY 1200 nano-LC System Easy nano LC II HPLC EASY-nLC 1200 nano-LC system Easy Nano LC II system Easy-nLC 1000 nano-LC system Thermo EASY nano-LC 1000 system Easy nano-LC Proxeon 1000 system EASY-nLC nano-LC system EASY-nano LC instrument

5 protocols using nano easy lc

Quantitative Proteomics of Yeast Cells

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Liquid Chromatography with tandem mass spectrometry measurements were performed on a nano EasyLC (Thermo Fisher Scientific) coupled to a Q Exactive HF-X mass spectrometer (Thermo Fisher Scientific). Peptides were separated on a fused silica column (I.D. 75 μm, New Objective, self-packed with ReproSil-Pur 120 C18-AQ, 1.9 μm (Dr Maisch) to a length of 20 cm) using a gradient of A (0.1% formic acid in water) and B (0.1% formic acid in 80% acetonitrile in water) from 5% B to 30 over 85 min at a 250 nl/min flow rate.
The mass spectrometer was operated in data-independent acquisition mode with MS scans acquired at a resolution of 120k covering a m/z range from 370 to 1200, followed by 35 consecutive MS/MS scan windows of 24 m/z acquired at a 30k resolution with 1 m/z overlap. Raw data were analyzed using Spectronaut version 16.2.220903.53000 (89 (link)), searched against S. cerevisiae proteome and common contaminants (Uniprot, March 2016). Pulsar search was performed allowing for a maximum of three missed cleavages. Cysteine carbamidomethylation was set as fixed modification. Protein N-terminal acetylation and methionine oxidation were set as variable modifications. DIA analysis crossrun normalization was turned off. When not mentioned otherwise, all other settings were left to default BGS factory settings.

Arlt H., Raman B., Filali-Mouncef Y., Hu Y., Leytens A., Hardenberg R., Guimarães R., Kriegenburg F., Mari M., Smaczynska-de Rooij I.I., Ayscough K.R., Dengjel J., Ungermann C, & Reggiori F. (2023). The dynamin Vps1 mediates Atg9 transport to the sites of autophagosome formation. The Journal of Biological Chemistry, 299(5), 104712.

+ Open protocol

+ Expand

Rotavirus Host Interactome Profiling

Check if the same lab product or an alternative is used in the 5 most similar protocols

MA104/NSP5-BioID2 cells (1.5 × 10⁸) were infected with SA11 (MOI, 5), treated at 6 hpi with 100 µM biotin, and lysed 24 h post-transfection in TNN buffer [Tris–HCl 100  mM (pH 8), NaCl 250  mM, and NP-40 0.5% with cOmplete protease inhibitor cocktail (Roche)]. The pull-down of biotinylated proteins was performed using 100 µL StrAv Mag Sepharose (GE Healthcare) for each condition and incubated in a rotation wheel for 3 h at 4°C. For mass spectrometry analysis, the washed biotin pull-downs were digested directly with trypsin (200 ng) in 20 µL of 20 mM triethyl ammonium bicarbonate pH 8.5 for 16 h at room temperature. The supernatant was removed, the beads were washed once with 50 µL of 0.1% formic acid, and the two fractions were pooled and concentrated using STAGE tips (90 (link)). The samples were resuspended in 10 µL of 0.1% formic acid and analyzed by LC-MS/MS using a NanoEASY LC (Thermo) coupled with an amaZon ETD ion trap (Bruker Daltonics). The resulting spectra were searched against the human and rotavirus proteomes using the GPM (91 (link)). Results were filtered to remove all results with an e-value > 0.05. Statistical analysis and plots were performed using R (4.1.3). The figure was finalized in Adobe Illustrator 2022.

Vetter J., Papa G., Tobler K., Rodriguez J.M., Kley M., Myers M., Wiesendanger M., Schraner E.M., Luque D., Burrone O.R., Fraefel C, & Eichwald C. (2024). The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication. mBio, 15(4), e00499-24.

+ Open protocol

+ Expand

Histone Modification Analysis by LC-MS

Check if the same lab product or an alternative is used in the 5 most similar protocols

For LC–MS analysis of modified histone proteins, the acidified histone peptide digests were analysed on the Q-Exactive HF mass spectrometer (Thermo Fisher Scientific) coupled in-line to a nanoEasy LC (Thermo Fisher Scientific). In brief, the samples were automatically loaded onto an in-house packed 2 cm 100 µm inner diameter C18 pre-column with buffer A (0.1% formic acid) and then eluted and separated on an in-house packed Reprosil-Pur 120 C18-AQ (3 µm; Dr. Maisch) analytical column (20 cm × 75 µm inner diameter) using a 35 min linear gradient from 0% to 40% buffer B (90% acetonitrile, 0.1% formic acid). Full scan MS spectra (m/z 300–1,000) and MS/MS fragment spectra were acquired in the Orbitrap with a resolution of 120,000 or 15,000, respectively, with maximum injection times of 50 ms each. Up to the 20 most intense ions were selected for higher-energy collisional dissociation fragmentation depending on signal intensity. Dynamic exclusion was disabled.

Lukauskas S., Tvardovskiy A., Nguyen N.V., Stadler M., Faull P., Ravnsborg T., Özdemir Aygenli B., Dornauer S., Flynn H., Lindeboom R.G., Barth T.K., Brockers K., Hauck S.M., Vermeulen M., Snijders A.P., Müller C.L., DiMaggio P.A., Jensen O.N., Schneider R, & Bartke T. (2024). Decoding chromatin states by proteomic profiling of nucleosome readers. Nature, 627(8004), 671-679.

+ Open protocol

+ Expand

Peptide Identification by Nano-LC-MS/MS

Check if the same lab product or an alternative is used in the 5 most similar protocols

Peptides from the various fractions were analyzed by a nano-Easy LC (Thermo Fisher Scientific) coupled with a Q-Exactive mass spectrometer (Thermo Fisher Scientific, Bremen, Germany). All peptide fractions were re-suspended in 0.1% formic acid (FA) and loaded onto a 2 cm 100 µm inner diameter pre-column using the nano-Easy LC. Peptides were eluted directly onto the analytical column using a gradient of 0–34% buffer B (90% Acetonitrile, 0.1% FA) over 30–90 min depending on the UV intensity of the individual HILIC fractions. All LC–MS/MS runs were performed using an analytical column of 20 cm × 75 µm inner diameter fused silica, packed with C18 material (Dr. Maisch, Ammerbuch-Entringen, Germany). Mass spectrometry was performed using higher energy collision fragmentation (HCD) fragmentation on a Q-Exactive instrument. MS settings: a full MS scan in the mass area of 400–1,800 Da was performed in the Orbitrap with a resolution of 70,000 FWHM and a target value of 1 × 10⁶ ions. For each full scan the 12 most intense ions (charge states 2–5) were selected for HCD fragmentation and the fragments were detected at a resolution of 17,500 FWHM. Threshold for ion selection was 1.0e4, the AGC target value 2.0e4, activation time was 0.1 ms, isolation window was 1.5 Da, and normalized collision energy was 29.

Blaabjerg M., Hemdrup A.L., Drici L., Ruprecht K., Garred P., Höftberger R., Kristensen B.W., Kondziella D., Sejbaek T., Hansen S.W., Nielsen H.H., Jensen P., Meyer M., Paul F., Lassmann H., Larsen M.R, & Illes Z. (2018). Omics-Based Approach Reveals Complement-Mediated Inflammation in Chronic Lymphocytic Inflammation With Pontine Perivascular Enhancement Responsive to Steroids (CLIPPERS). Frontiers in Immunology, 9, 741.

+ Open protocol

+ Expand

Nano-LC-MS/MS Peptide Quantification

Check if the same lab product or an alternative is used in the 5 most similar protocols

0.5 μg of peptide sample in 5 μL was loaded on a precolumn (3 cm long, 100 μm ID, packed with 5 μm C18 RP material (Dr. Maisch, Ammerbuch-Entringen, Germany) using nano-Easy LC (Thermo Fisher Scientific). Peptides were separated on a 18 cm long, 75 μm ID analytical column packed with 3 μm C18 material (Dr. Maisch, Ammerbuch-Entringen, Germany) using 62 min gradient of 90% ACN/0.1% FA (solvent B): 8% for 5 min, 8% to 30% (linear gradient) in 44 min, 30% to 100% in 5 min and 8 min at 100%. Peptides were fragmented and detected in Q-Exactive mass spectrometer (Thermo Fisher Scientific, Bremen, Germany). The MS settings: Full MS: Resolution at 120000, AGC target 3e6, Maximum IT 30 ms, scan range: 325–1200 m/z. PRM (10 reaction between Full MS scan): Resolution at 15000, AGC target 3e6, Maximum IT 15 ms, isolation window 1.1 m/z, NCE: 32. MS data were processed using Skyline. The low intensity of most of the detected peptides, originating from the investigated proteins resulted in poor MS2 spectra, therefore for the consistency, peptide relative quantification was performed using MS1 intensity of the precursor ion normalized to intensity of the corresponding SIS standard.

Martin N.A., Nawrocki A., Molnar V., Elkjaer M.L., Thygesen E.K., Palkovits M., Acs P., Sejbaek T., Nielsen H.H., Hegedus Z., Sellebjerg F., Molnar T., Barbosa E.G., Alcaraz N., Gallyas F J.r., Svenningsen A.F., Baumbach J., Lassmann H., Larsen M.R, & Illes Z. (2018). Orthologous proteins of experimental de- and remyelination are differentially regulated in the CSF proteome of multiple sclerosis subtypes. PLoS ONE, 13(8), e0202530.

+ Open protocol

+ Expand

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?

Revolutionizing how scientists
search and build protocols!