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Surveyor autosampler

Manufactured by Thermo Fisher Scientific
Sourced in United States

The Surveyor autosampler is a laboratory instrument designed to automatically introduce samples into an analytical system, such as a chromatograph or mass spectrometer. It is capable of handling a wide range of sample types and volumes, and can be programmed to perform complex sample preparation and analysis sequences. The Surveyor autosampler provides consistent and reliable sample introduction, improving the efficiency and accuracy of analytical workflows.

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18 protocols using surveyor autosampler

1

Tandem Mass Spectrometry Protocol for Peptide Analysis

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The digestate obtained from the SDS-PAGE gel slices were analyzed by nanoflow liquid chromatography tandem mass spectrometry (nanoLC-MS/MS) using an LTQ-XL ion-trap mass spectrometer (Thermo, Fremont, CA, USA). Reversed phase columns were packed in-house to approximately 7 cm (100 μmi.d.) using 100 Å, 5 μM Zorbax C18 resin (Agilent Technologies, Santa Clara, CA, USA) in a fused silica capillary with an integrated electrospray tip. A 1.8 kV electrospray voltage was applied via a liquid junction upstream of the C18 column. Samples were then injected into the C18 column using a Surveyor autosampler (Thermo, Fremont, CA, USA). The column was washed with buffer A [5% (v/v) ACN, 0.1% (v/v) formic acid] for 10 min at 1 μL/min before each loading. Peptides were subsequently eluted from the C18 column with 0–50% Buffer B [95% (v/v) ACN, 0.1% (v/v) formic acid] over 58 min at 500 nL per min followed by 50–95% Buffer B over 5 min at 500 nL per min. The column eluate was then directed into a nanospray ionization source of the mass spectrometer. Spectra were scanned over the range 400–1500 amu. Automated peak recognition, dynamic exclusion window set to 90s38 (link) and tandem MS of the top six most intense precursor ions at 35% normalization collision energy were performed using Xcalibur™ software (version 2.06) (Thermo, Fremont, CA, USA).
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2

Peptide Analysis by nanoLC-MS/MS

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As previously described [65 ], peptides were analyzed by nanoLC-MS/MS using a LTQ-XL ion-trap mass spectrometer (Thermo Fisher Scientific, San Jose, CA, USA). Reverse phase columns were packed in-house to approximately 7 cm (100 μm i.d.) using 100 Å, 5 μm Zorbax C18 resin (Agilent Technologies, Santa Clara, CA, USA) in a fused silica capillary with an integrated electrospray tip. A 1.8 kV electrospray voltage was applied via a liquid junction up-stream of the C18 column. Samples were injected onto the C18 column using a Surveyor autosampler (Thermo Fisher Scientific), followed by an initial wash with buffer A (5% (v/v) ACN, 0.1% (v/v) formic acid) for 10 min at 1 μL/min. Peptides were eluted from the C18 column with 0%-50% Buffer B (95% (v/v) ACN, 0.1% (v/v) formic acid) over 58 min at 500 nL/min followed by 50–95% Buffer B over 5 min at 500 nL/min. The eluted solution was directed into the nanospray ionization source of the mass spectrometer. Spectra were scanned over the range 400–1500 amu, with automated peak recognition, a dynamic exclusion window set to 90 s and tandem MS of the top 6 most intense precursor ions at 35% normalization collision energy using Xcalibur software (version 2.06; Thermo Fisher Scientific).
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3

LC-MS Analysis of Small Molecules

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Sample separation was carried out using a Surveyor autosampler and an MSPumpPlus (Thermo Fisher Scientific, Runcorn, UK) LC system on a reverse phase Thermo Fisher Scientific Hypersil Gold LC column (1.0 × 100 mm, 5 μm) operated with a Hypersil guard cartridge, suitable for general separations. Mass spectrometry detection was performed using an LCQ ion trap (Thermo Fisher Scientific, Hemel Hempstead, UK) operated using an ESI source in positive mode. Instrument control and data analysis were carried out using Xcalibur 2.0.7 software with data processed using both the Quan Browser Xcalibur tool and Microsoft Excel.
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4

LCMS Analysis of Chemical Compounds

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LCMS
was performed using a system consisting of the following components:
Shimadzu SCL-10A VP system controller with Shimadzu LC-10 AD VP liquid
chromatography pumps with an Alltima C18 3 u (50 × 2.1 mm) reversed-phase
column and gradients of water–acetonitrile supplemented with
0.1% formic acid, a Shimadzu DGU 20A3 prominence degasser, a Thermo
Finnigan surveyor auto sampler, a Thermo Finnigan surveyor PDA detector,
and a Thermo Scientific LCQ Fleet. Gradients were run from 5% MeCN
to 100% MeCN over a 15 min period.
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5

Analysis of C. elegans N-Glycans by LC/MS

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The characterization of N-glycans released from C. elegans and labeled with 2-AB was carried out by LC/MS analysis on an LTQ XL linear ion trap mass spectrometer equipped with an ESI source (Thermo-Electron, San Jose, CA, USA). The mass spectrometry coupled liquid chromatography was performed using a Surveyor autosampler plus and MS pump plus (Thermo Scientific). The column used was a 1.0 mm x 15 cm, 5 µm TSK gel Amide-80 column (Tosoh Bioscience LLC, PA, USA). Solvent A was 20 mM ammonium acetate (pH 6.9) and solvent B was 100% acetonitrile. The flow rate was 40 µl/min. Initial conditions were 20% solvent A/80% solvent B. After 5 minutes solvent B was decreased from 80% to 25% over 100 minutes followed by re-equilibration for 10 minutes at initial conditions.
Mass spectrometer conditions were a spray voltage of 5.0 kV and the capillary temperature was 170°C. The sheath gas flow was set to 20.00 units. For the generation of the MSn spectra, normalized collision energies were set to 35%. The method used was triple play operated by Xcalibur software, with second scan being Zoom MS and third scan was Dependent MS/MS of most intense ion from scan event 2. The isolation width was set to 2 amu. All experiments were performed in the positive ion mode.
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6

Tryptic Peptide Analysis by LC-MS/MS

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LC/MS/MS analysis of the tryptic peptides obtained after in-solution and in-gel protein digests was carried out using LTQ XL™ ion trap mass spectrometer (Thermo Scientific). Separation was performed on PicoFrit C18 nanospray column (New Objective) of 360 um OD x 75um ID x 15um tip opening dimensions. Samples (15 μl each) were injected using a Thermo Scientific Surveyor Autosampler operated in the no waste injection mode with flow rate of 300 nl/min. Peptides were eluted from the in-solution digests at a linear acetonitrile gradient from 2 to 35% for over 210 min, and from the in-gel digests using a linear acetonitrile gradient from 2 to 32% for over 85 min, followed by high and low organic washes for another 5 min. The eluent is introduced directly to the LTQ XL mass spectrometer (Thermo Scientific) via a nanospray source with the spray voltage 1.8 kV and the ion transfer capillary set at 180 °C. MS data was acquired using a data-dependent top 7 method where a full MS scan from m/z 350–1500 was followed by MS/MS scans on the seven most intense ions. Each ion was subjected to Collision Induced Dissociation (CID) for fragmentation and peptide identification.
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7

Analytical Workflow for Phytochemical Profiling

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Filter paper (Whatman No.4, England), rotary evaporator (Stuart Bibby Scientific, RE300DB), electric air‐dried oven (Memmert UN30, Zirndorf), UV–vis spectrophotometer (PerkinElmer, Lamda 950, UV/VIS, UK), blender (Panasonic), electronic analytical balance (Ohaus), freezer (Innova, IN200), electronic hot plate (VWR, Cole‐Parmer, Thermo Scientific, France), gas chromatography system (GC Clarus 690, Perkin Elemer), and reverse‐phase Purospher STAR Hibar HR RP18 end‐capped column (150 mm × 2.1 mm, 3 μm, thermostated at 30°C, Supelco) in a LC system that is composed of: a solvent degasser (SCM1000, Thermo Scientific), a binary high‐pressure pump (1100 series, Agilent Technologies), a Surveyor autosampler thermostated at 4°C (Thermo Scientific), equipped with a UV–visible photodiode array detector (UV6000 LP, Thermo Scientific) and an ion trap mass spectrometer with electrospray ionization source (LCQ Deca, Thermo Scientific).
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8

IRP2 Cisplatin Interaction Analysis

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10 µg of human IRP2 recombinant protein (Origene) was incubated with 500 µg/mL isplatin for 24 h at 4 °C, and LC-MS/MS analysis was performed at ITSI Biosciences (Johnstown, PA). Briefly, IRP2 and cisplatin mixture was reduced/alkylated, suspended in 100 mM triethyl ammonium bicarbonate buffer and digested overnight with trypsin. The digest was dried down and resuspended in 0.1% formic acid. Peptides were desalted using zip tip (EMD Millipore, Billerica, MA), dried and reconstituted in a solution containing 2% acetonitrile and 0.1% formic acid. The peptide samples were loaded onto a PicoFrit C18 nanospray column using a Thermo Scientific Surveyor Autosampler and eluted from the column using a linear 2–30% acetonitrile gradient over 90 minutes for an LTQ XL mass spectrometer analysis (Thermo Scientific, Rockford, IL). Raw data files were searched against the most recent Uniprot database for Human IREB2 (Accession #A0A0A6YY96).
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9

Stable Isotope Analysis of Soil Organic Matter

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Stable carbon isotope measurements were carried out using an HPLC system coupled to a Delta+ XP IRMS through an LC IsoLink interface (Thermo Fisher Scientific, Germany). SEC was performed on a mixed bed analytical column (TSK-GEL GMPWXL-7.8 mm × 30 cm; Tosoh Bioscience, Germany). 100 μL aliquot of soil extracts was injected using an autosampler (Surveyor autosampler, Thermo Fisher Scientific) into the mobile phase that consisted of phosphate buffer 20 mM (pH 6.2) maintained at a constant flow rate of 500 μL min -1 using a Surveyor MS pump. Apparent MW was obtained using a calibration curve plotted with standards having known MW (Malik et al., 2012 (link)(Malik et al., , 2013 for technical details).
Empirical C turnover time (synonymously referred to as mean residence time) of microbial size classes was obtained by estimating the pulse 13 C dilution rate using an exponential function in SigmaPlot (Malik et al., 2015) (link).
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10

Liquid Chromatography-Tandem Mass Spectrometry

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The digested samples were analyzed using a Thermo-Finnigan linear ion-trap (LTQ) mass spectrometer coupled with a Surveyor autosampler and MS HPLC system (Thermo-Finnigan). Tryptic peptides were injected onto the C18 microbore RP column (Zorbax SB-C18, 1.0 mm x 150 mm) at a flow rate of 50 μL/min. The mobile phases A, B, and C were 0.1% formic acid in water, 50% ACN with 0.1% formic acid in water, and 80% ACN with 0.1% formic acid in water, respectively. The gradient elution profile was as follows: 10% B (90% A) for 5 min, 10-95% B (90-5% A) for 120 min, 100% C for 5 min, and 10% B (90% A) for 12 min. The data were collected in the “Triple-Play” (MS scan, Zoom scan, and MS/MS scan) mode with the ESI interface using normalized collision energy of 35%. Dynamic exclusion settings were set to repeat count 1, repeat duration 30 s, exclusion duration 120 s, and exclusion mass width 0.75 m/z (low) and 2.0 m/z (high). Each sample was injected twice.
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