Nanolc 1d

Manufactured by AB Sciex

The NanoLC 1D is a high-performance liquid chromatography system designed for nano-scale separations. It features a compact and robust design, precise flow control, and high sensitivity detection capabilities. The NanoLC 1D is suitable for a wide range of applications, including proteomics, metabolomics, and small molecule analysis.

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Lab products found in correlation

Ltq orbitrap xl, by Thermo Fisher Scientific (1 mentions) Ltq orbitrap, by Thermo Fisher Scientific (1 mentions) Ltq velos mass spectrometer, by Thermo Fisher Scientific (1 mentions) Sodium deoxycholate, by Merck Group (1 mentions) Trypsin, by Promega (1 mentions)

Spelling variants of this product

NanoLC Ultra 1D plus (15 citations) NanoLC Ultra 1D Plus system (12 citations) Eksigent nanoLC-1D plus system (8 citations) Eksigent® NanoLC-1D™ Plus nanoLC™ system (5 citations) Eksigent nanoLC‐Ultra 1D+ (4 citations) NanoLC-Ultra 1D+, (3 citations) NanoLC-1D plus system (2 citations)

3 protocols using nanolc 1d

Capillary LC-MS/MS Analysis of Peptides

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Peptides were re-suspended in 40 µl 3% v/v acetonitrile, 0.1% v/v formic acid. Measurements were performed on a LTQ-Orbitrap XL (Thermo Scientific) coupled with a NanoLC 1D (Eksigent). Samples were loaded onto a laboratory-made capillary column (75 µm inner diameter, 9 cm long), packed with Magic C18 AQ beads (3 µm, 100 Å, Microm) at flow 0.5 µl min⁻¹ in 3% v/v acetonitrile, 0.2% v/v formic acid and eluted with a 5–40% v/v acetonitrile concentration gradient over 70 min, followed by 80% v/v acetonitrile for 10 min, at 0.25 µl min⁻¹. Peptide ions were detected in a full scan from mass-to-charge ratio 300–2000. MS/MS scans were performed for the five peptides with the highest MS signal (minimal signal strength 500 hits, isolation width mass-to-charge ratio 3 m/z, relative collision energy 35%). Peptides for which MS/MS spectra had been recorded were excluded from further MS/MS scans for 20 s.

Graf A., Coman D., Uhrig R.G., Walsh S., Flis A., Stitt M, & Gruissem W. (2017). Parallel analysis of Arabidopsis circadian clock mutants reveals different scales of transcriptome and proteome regulation. Open Biology, 7(3), 160333.

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Quantitative Proteomics for cGVHD Prediction

Cited 1 time

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Samples were depleted of the 6 most abundant proteins (albumin, IgG, IgA, transferrin, haptoglobin and antitrypsin), pooled and labeled with light acrylamide (cases: subsequent cGVHD-positive) or with a heavy 1,2,3-¹³C-acrylamide (controls: subsequent cGVHD-negative).^{5 (link), 18 (link)} The pool of cases and the pool of controls were mixed together before further processing and IPA analysis. Proteins were separated by an automated online 2D-HPLC system controlled by Workstation Class-VP 7.4 (Shimadzu Corporation).^{5 (link), 18 (link)} Separation consisted of anion exchange chromatography followed by reverse-phase chromatography. In-solution tryptic digestion was conducted with lyophilized aliquots from the reverse-phase (second dimension) fractionation step.^{13 (link), 23 (link)} Aliquots were subjected to tandem mass spectrometry shotgun analysis using an LTQ-Orbitrap (Thermo) mass spectrometer coupled with a NanoLC-1D (Eksigent) on a 2-hour gradient.^{13 (link), 23 (link)}

Inamoto Y., Martin P.J., Paczesny S., Tabellini L., Momin A.A., Mumaw C.L., Flowers M.E., Lee S.J., Carpenter P.A., Storer B.E., Hanash S, & Hansen J.A. (2017). Association of plasma CD163 concentration with de novo-onset chronic graft-versus-host disease. Biology of blood and marrow transplantation : journal of the American Society for Blood and Marrow Transplantation, 23(8), 1250-1256.

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Mitochondrial Proteomics by Mass Spectrometry

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Strains were grown as described for the metabolomic studies. Mitochondria were isolated as previously described [3 (link), 12 (link), 15 (link)]. Proteins were then isolated as previously published [7 (link)]. Prior to analysis by tandem mass spectrometry, samples were divided into 1-4 technical replicates, subjected to bead beating, and digested with trypsin (Promega, Madison WI) in the presence of .1% sodium deoxycholate (Sigma) or .1% PPS silent surfactant (Protein Discovery, Knoxville, TN). Following removal of undigested material by acetonitrile precipitation and brief exposure to a nitrogen dryer, samples were analyzed on an LTQ-Velos mass spectrometer (Thermo Fisher, San Jose CA) coupled to an Eksigent nanoLC 1D+ (Eksigent, Dublin CA). Digested peptides were separated on a HALO C¹⁸ nanocolumn by reverse phase chromatography just prior to reaching the nanospray source. The standard experimental protocol has been detailed previously [13 (link)].

Morgan P., Higdon R., Kolker N., Bauman A., Ilkayeva O., Newgard C., Kolker E., Steele L, & Sedensky M. (2014). Comparison of proteomic and metabolomic profiles of mutants of the mitochondrial respiratory chain in Caenorhabditis elegans. Mitochondrion, 20, 95-102.

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