Agilent 1100 series lc

Manufactured by Agilent Technologies

Sourced in United States, Germany

The Agilent 1100 Series LC is a high-performance liquid chromatography (HPLC) system designed for analytical and preparative applications. It features a modular design, allowing users to configure the system to meet their specific requirements. The core function of the Agilent 1100 Series LC is to separate, identify, and quantify components in complex mixtures.

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Lab products found in correlation

Hct ultra ion trap mass spectrometer, by Bruker (3 mentions) Hct ultra, by Bruker (2 mentions) Sunfire c18, by Waters Corporation (2 mentions) Msd trap xct plus ion trap mass spectrometer, by Agilent Technologies (2 mentions) Dataanalysis 4, by Bruker (2 mentions) Orbitrap elite mass, by Thermo Fisher Scientific (1 mentions) Fld g1321a, by Agilent Technologies (1 mentions) Agilent 1100 series autosampler, by Agilent Technologies (1 mentions) Agilent 1100 series quaternary pump, by Agilent Technologies (1 mentions) Hct ultra ion, by Bruker (1 mentions) Luna c8 2, by Phenomenex (1 mentions) Tune mix, by Agilent Technologies (1 mentions) Microtof q, by Bruker (1 mentions) Maxis 2 q tof mass spectrometer, by Bruker (1 mentions) Compass dataanalysis 4, by Bruker (1 mentions) Zorbax sb c18 column, by Agilent Technologies (1 mentions) Zorbax sb aq column, by Agilent Technologies (1 mentions) Atlantis t3, by Waters Corporation (1 mentions) Masslynx, by Waters Corporation (1 mentions) Q tof premier mass spectrometer, by Waters Corporation (1 mentions)

23 protocols using agilent 1100 series lc

Mass Spectrometric Analysis of Compounds

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Mass spectra were recorded on an Orbitrap Elite mass spectrometer
(Thermo Fisher Scientific, Waltham, MA) using direct infusion and
heated electrospray ionization. HCD fragmentations were performed
on isolated ions (isolation width typically 5 Da) with stepwise increase
of energy to obtain optimum results.
For LC-MS measurement,
an Agilent 1100 series LC coupled to an Orbitrap Elite mass spectrometer
was used. Separation was achieved on a Zorbax Eclipse Plus C18 column
(2.1 × 150 mm², 3.5 μm) by using a eluation
gradient from 90 to 70% ACN/water (0.1% formic acid) at a flow rate
of 0.1 mL/min over 25 min. Mass spectra were recorded with a resolution
of 240000.

Goetzfried S.K., Gallati C.M., Cziferszky M., Talmazan R.A., Wurst K., Liedl K.R., Podewitz M, & Gust R. (2020). N-Heterocyclic Carbene Gold(I) Complexes: Mechanism of the Ligand Scrambling Reaction and Their Oxidation to Gold(III) in Aqueous Solutions. Inorganic Chemistry, 59(20), 15312-15323.

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Cyanogenic Profiling of Passiflora biflora

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The cyanogenic content of the Passiflora biflora samples was analyzed using liquid chromatography-mass spectrometry (LC-MS/MS) with Agilent 1100 Series LC (Agilent Technologies, Germany) hyphenated to a Bruker HCT-Ultra ion trap mass spectrometer (Bruker Daltonics, Germany) following the procedure of de castro et al. (2019) (link) (see File S4 for details on sample extraction, spectrometry and analyses). Mass spectral data were analyzed with the native data analysis software (Compass DataAnalyses, Bruker Daltonics). The cyanogen compounds of P. biflora were detected and quantified following de castro et al. (2019) (link).
Plant quality traits assumed to be proxies of nutritional value, including nitrogen/carbon ratio (a proxy of protein/carbohydrate-ratio), were measured from the greenhouse-cultivated P. biflora treatment types (average number of individual leaves sampled per P. biflora treatment type: n = 63) with Dualex^® Scientific+ leaf clip meter (Cerovic et al., 2012 (link); File S4). We tested for differences in cyanogen levels and plant quality traits between the treatment groups in an ANOVA including plant origin, treatment and their interaction.

Mattila A.L., Jiggins C.D., Opedal Ø.H., Montejo-Kovacevich G., Pinheiro de castro É.C., McMillan W.O., Bacquet C, & Saastamoinen M. (2021). Evolutionary and ecological processes influencing chemical defense variation in an aposematic and mimetic Heliconius butterfly. PeerJ, 9, e11523.

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Quantitation of Antisense Oligonucleotides in Biological Fluids

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AEX running buffer A, consisted of 20% ACN, 3 M urea, 1 mM EDTA and 25 mM Tris, pH 8; buffer B included 1 M NaClO₄. Plasma and lymph samples were diluted directly in AEX buffer A. We prepared standards of ASO and Palm-ASO in control plasma and lymph at 1 μM and serial dilution in plasma or lymph to 3.9 nM. A PNA oligonucleotide with a sequence fully complimentary to ASO and labeled at the 5′ end with ALEXA488 was added at 2 uM to standards and samples and then heated to 80°C for 2 min and allowed to cool to room temperature for at least 30 min to allow the PNA and ASO or Palm-ASO to hybridize. Duplexed samples were separated on AEX column DNAPac PA200 4 × 250 nm (Thermo Scientific, Waltham, MA, USA) using an Agilent 1100 series LC. Samples were separated with a flow rate of 1 ml/min and a gradient running from 5% to 35% B over 10 min. An Agilent FLD G1321A detected fluorescence using Ex488/Em520. Under these conditions, PNA elutes at 1.2 min, PNA duplexed ASO elutes at 4.9 min, and PNA-duplexed Palm-ASO elutes at 5.6 min (all times ± 3%). Standard curves were established for both ASO and Palm-ASO in control plasma and lymph by plotting concentration against FLD peak area and unknown samples calculated from these standard curves. Technical replicants were run in duplicate.

Chappell A.E., Gaus H.J., Berdeja A., Gupta R., Jo M., Prakash T.P., Oestergaard M., Swayze E.E, & Seth P.P. (2020). Mechanisms of palmitic acid-conjugated antisense oligonucleotide distribution in mice. Nucleic Acids Research, 48(8), 4382-4395.

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LC-MS Analysis of Pea Metabolites

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LC–MS was performed using an Agilent 1100 Series LC (Agilent Technologies) coupled to a Bruker HCT-Ultra ion trap mass spectrometer (Bruker Daltonics), as described^{54 (link)}. The LC–MS data was analysed using Bruker-DataAnalysis 4.0 (Bruker Daltonics). The standards were run diluted in water solutions. The pea homogenate was produced by grinding 500 mg of cut fresh pea epicotyls using a pestle following followed by 10 min of centrifugation at 10 000 g. The undiluted supernatant was used for in vitro tests of metabolic stability.

Mravec J., Kračun S.K., Zemlyanskaya E., Rydahl M.G., Guo X., Pičmanová M., Sørensen K.K., Růžička K, & Willats W.G. (2017). Click chemistry-based tracking reveals putative cell wall-located auxin binding sites in expanding cells. Scientific Reports, 7, 15988.

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LC-MS Analysis of Iridoid Glucosides

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LC-MS analysis was performed using an Agilent 1100 Series LC (Agilent Technologies) coupled to a Bruker HCT-Ultra ion trap mass spectrometer (Bruker Daltonics). The mass spectrometer was run in positive electrospray mode and loganin was detected from integration of extracted ion chromatograms. All iridoid glucosides were detected as single-charged sodium adducts [M + Na⁺]: 7-deoxyloganic acid, m/z 383; loganic acid, m/z 399; secologanin, m/z 411; and loganin, m/z 413. For details on the LC set-up, see Supplementary Table S2.

Larsen B., Fuller V.L., Pollier J., Van Moerkercke A., Schweizer F., Payne R., Colinas M., O’Connor S.E., Goossens A, & Halkier B.A. (2017). Identification of Iridoid Glucoside Transporters in Catharanthus roseus. Plant and Cell Physiology, 58(9), 1507-1518.

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HPLC-ESI-IT-MS Analysis of Pen. expansum Metabolites

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HPLC‐electrospray ionization ion trap mass spectrometry analysis (ESI‐IT‐MS) was performed using an MSD‐Trap‐XCT plus ion trap mass spectrometer equipped with an Agilent ESI source and Agilent 1100 series LC (Agilent Technologies, Wilmington, Del., USA) in positive mode with the mass range of m/z 50–2000. The column used was a SunFire C18, 2·1 × 50 mm, 2·5 μm (Waters, Milford, MA, USA). Separation of the compounds from exudate droplets and condensates of Pen. expansum RcP61 was performed using an isocratic method of solution A: H₂O with 0·1% (v/v) formic acid and B: methanol in a ratio of 40/60 (v/v) for 15 min and a subsequent gradient of 100% B for 30 min at a flow rate of 0·2 ml min⁻¹.

Salo M.J., Marik T., Mikkola R., Andersson M.A., Kredics L., Salonen H, & Kurnitski J. (2019). Penicillium expansum strain isolated from indoor building material was able to grow on gypsum board and emitted guttation droplets containing chaetoglobosins and communesins A, B and D. Journal of Applied Microbiology, 127(4), 1135-1147.

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Agilent 1100 Series LC Setup

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The Agilent 1100 Series LC consists of Agilent 1100 Series Quaternary Pump (G1311A), Agilent 1100 Series Autosampler (G1313A), Agilent 1100 Series Thermostatted Column Compartment (G1316A), Agilent 1100 Series Vacuum Degasser (G1379A), and Agilent 1100 Series variable wavelength UV detector (G1314A).

He Y., Chen S., Yu H., Zhu L., Liu Y., Han C, & Liu C. (2016). Effect of Catnip Charcoal on the In Vivo Pharmacokinetics of the Main Alkaloids of Rhizoma Coptidis. Evidence-based Complementary and Alternative Medicine : eCAM, 2016, 3532159.

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LC-ESI-MS Analysis of Supernatant

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LC-ESI-MS (3 μl supernatant injected) was carried out using an Agilent 1100 Series LC (www.agilent.com) coupled to a Bruker HCT Ultra ion trap mass spectrometer (www.bruker.com). The column was a Phenomenex Luna C8(2) (3 microM, 100A, 150 × 2.0 mm; www.phenomenex.com) preceded by a Phenomenex Gemini C18 SecurityGuard (4 × 2 mm). The oven temperature was maintained at 35 °C. The mobile phases were A, water; B, acetonitrile, both with 0.1% (v/v) HCOOH, and the flow rate was 0.2 mL min⁻¹. The gradient was: 0 to 2 min, isocratic 1% B; 2 to 8.5 min, linear gradient 1 to 3% B; 8.6 to 9.6 isocratic 99% B; 9.7 to 17 min, isocratic 1% B. The mass spectrometer was run in positive electrospray mode.
Selected ion traces were semi-quantified in accordance the instructions of and using the software Bruker HCT Compass Data analysis 4.0 software.

Møller S.R., Yi X., Velásquez S.M., Gille S., Hansen P.L., Poulsen C.P., Olsen C.E., Rejzek M., Parsons H., Zhang Y., Wandall H.H., Clausen H., Field R.A., Pauly M., Estevez J.M., Harholt J., Ulvskov P, & Petersen B.L. (2017). Identification and evolution of a plant cell wall specific glycoprotein glycosyl transferase, ExAD. Scientific Reports, 7, 45341.

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Quantifying Cyanogenic Glucosides in Cassava

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The cyanogenic glucoside contents of roots and leaves of the wild W14 and cultivated KU50 was determined by liquid chromatography–mass spectrometry. Five plants were analysed separately for each of them. A leaf disc was sampled from the first unfolded leaf of each plant by snap-closing the 2-ml-Eppendorf lid tubes. The plant samples were immersed into 300 μl and 500 μl of pre-warmed 85% (v/v) methanol for leaf and tuber, respectively. After closing the tube and securing the lid with a cap lock, the samples were boiled in a water bath at 100 °C for 3 min (leaf) or 5 min (tuber). Then, the MeOH extract was transferred into a new tube, lyophilized to dryness, re-suspended in water in a total volume of 200 μl and filtered through a 0.45-μm filter. Analytical liquid chromatography–mass spectrometry was carried out using an Agilent 1100 Series LC (Agilent Technologies).

Wang W., Feng B., Xiao J., Xia Z., Zhou X., Li P., Zhang W., Wang Y., Møller B.L., Zhang P., Luo M.C., Xiao G., Liu J., Yang J., Chen S., Rabinowicz P.D., Chen X., Zhang H.B., Ceballos H., Lou Q., Zou M., Carvalho L.J., Zeng C., Xia J., Sun S., Fu Y., Wang H., Lu C., Ruan M., Zhou S., Wu Z., Liu H., Kannangara R.M., Jørgensen K., Neale R.L., Bonde M., Heinz N., Zhu W., Wang S., Zhang Y., Pan K., Wen M., Ma P.A., Li Z., Hu M., Liao W., Hu W., Zhang S., Pei J., Guo A., Guo J., Zhang J., Zhang Z., Ye J., Ou W., Ma Y., Liu X., Tallon L.J., Galens K., Ott S., Huang J., Xue J., An F., Yao Q., Lu X., Fregene M., López-Lavalle L.A., Wu J., You F.M., Chen M., Hu S., Wu G., Zhong S., Ling P., Chen Y., Wang Q., Liu G., Liu B., Li K, & Peng M. (2014). Cassava genome from a wild ancestor to cultivated varieties. Nature Communications, 5, 5110.

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LC-MS Analysis of Crosslinking Mixtures

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LC/MS analyses were performed using
an Agilent 1100 series LC coupled to a MicrOTOF-Q (Bruker Daltonics,
Bremen, Germany) or to a maXis II Q-TOF mass spectrometer (Bruker).
The mass spectrometer was operated in positive mode with a capillary
voltage of 4500 V. Acquisitions were performed on the mass range of
200–1850 m/z. Calibration
was performed using the singly charged ions produced by a solution
of Tune mix (G1969–85000, Agilent, U.S.A.). Data analysis was
performed by using Compass DataAnalysis 4.3 (Bruker Daltonics). A
cross-linking reaction mixture containing GSH and PDO 2 (or probe 9) was directly analyzed onto a HPLC connected
to MicrOTOF-Q. Compounds were separated on a XBridge Peptide BEH C18
column (300 Å, 3.5 μm, 2.1 mm × 250 mm) column. The
gradient was generated at a flow rate of 250 μL/min using 0.1%
trifluoroacetic acid (TFA) in water for mobile phase A and ACN containing
0.08% TFA for mobile phase B at 60 °C. Phase B was increased
from 5 to 85% in 45 min.

Cichocki B.A., Khobragade V., Donzel M., Cotos L., Blandin S., Schaeffer-Reiss C., Cianférani S., Strub J.M., Elhabiri M, & Davioud-Charvet E. (2021). A Class of Valuable (Pro-)Activity-Based Protein Profiling Probes: Application to the Redox-Active Antiplasmodial Agent, Plasmodione. JACS Au, 1(5), 669-689.

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