6210 lc tof spectrometer

Manufactured by Agilent Technologies

The 6210 LC-TOF spectrometer is a high-performance liquid chromatography-time of flight mass spectrometer (LC-TOF MS) designed for accurate mass measurements and high-resolution analysis. The instrument utilizes time-of-flight mass analysis to provide precise mass determination of a wide range of analytes. The 6210 LC-TOF spectrometer is capable of acquiring full-scan mass spectra with high sensitivity and resolution.

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Lab products found in correlation

Hplc system, by Agilent Technologies (5 mentions) Chromasolv, by Merck Group (5 mentions) Masshunter workstation software, by Agilent Technologies (5 mentions) Zorbax 300sb c8, by Agilent Technologies (4 mentions) Avance 3 500 mhz nmr spectrometer, by Bruker (2 mentions) Autoflex 3 maldi, by Bruker (2 mentions) Prostar 500 system, by Agilent Technologies (2 mentions) 335 uv vis detector, by Agilent Technologies (2 mentions) 363 fluorescence detector, by Agilent Technologies (1 mentions) Trifluoroacetic acid, by Thermo Fisher Scientific (1 mentions)

7 protocols using 6210 lc tof spectrometer

Protein Analysis by LC-ESI-MS

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Liquid chromatography electrospray ionization mass spectrometry (LC/ESI-MS) was performed on a 6210 LC-TOF spectrometer coupled to an HPLC system (Agilent Technologies). All solvents used were HPLC grade (Chromasolv, Sigma–Aldrich), trifluoroacetic acid (TFA) was from Acros Organics (puriss p.a.). Solvent A was 0.03% TFA in water, solvent B was 95% acetonitrile, 5% water and 0.03% TFA. Just before analysis protein samples were diluted under acidic denaturing conditions to a final concentration of 5 µM with solution A (0.03% TFA in water). Protein samples were firstly desalted on a reverse-phase C8 cartridge (Zorbax 300SB-C8, 5 µm, 300 µm ID × 5 mm, Agilent Technologies) for 3 min at a flow rate of 50 µl min⁻¹ with 100% solvent A and then eluted with 70% solvent B at flow rate of 50 µl min⁻¹ for MS detection. MS acquisition was carried out in positive ion mode in the 300–3200 m/z range. MS spectra were acquired and the data processed with the MassHunter workstation software (v.B.02.00, Agilent Technologies).

McGregor L., Földes T., Bui S., Moulin M., Coquelle N., Blakeley M.P., Rosta E, & Steiner R.A. (2021). Joint neutron/X-ray crystal structure of a mechanistically relevant complex of perdeuterated urate oxidase and simulations provide insight into the hydration step of catalysis. IUCrJ, 8(Pt 1), 46-59.

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Synthesis and Characterization of Gd(III) Contrast Agent

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Unless otherwise noted, materials and solvents were obtained from commercial suppliers and used without further purification. All reactions were performed under an inert nitrogen atmosphere. EMD 60F 254 silica gel plates were used for thin layer chromatography and visualized using UV light or ninhydrin stain. Column chromatography was performed using standard grade 60 Å 230 – 400 mesh silica gel (Sorbent Technologies). ¹H NMR and ¹³C NMR spectra were obtained at room temperature on a Bruker Avance III 500 MHz NMR spectrometer. An Agilent 6210 LC-TOF spectrometer was used to acquire electro spray ionization mass spectra (ESI-MS). Matrix-Assisted Laser Desorption Ionization Time-Of-Flight (MALDI-TOF) mass spectrometry was carried out using a Bruker Autoflex III MALDI. Semi-preparative HPLC was performed on a Waters 19 × 250 mm X bridge C18 Column. Analytical HPLC was performed using a Waters 4.6 × 250 mm 5 μM X bridge C18 column using the Varian Prostar 500 system equipped with a Varian 363 fluorescence detector, and a Varian 335 UV/Vis Detector.
The amine functionalized Gd(III) scaffold (4) was synthesized according to literature procedure.³⁰ For a detailed synthetic procedure of the peg functionalized scaffold (3) and the isothiocyanate functionalized dye (5) see the supporting information.

Harrison V.S., Carney C.E., MacRenaris K.W., Waters E.A, & Meade T.J. (2015). Multimeric Near IR–MR Contrast Agent for Multimodal In Vivo Imaging. Journal of the American Chemical Society, 137(28), 9108-9116.

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LC/ESI-MS Protocol for Protein Analysis

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LC/ESI-MS was performed on a 6210 LC-TOF spectrometer coupled to an HPLC system (Agilent Technologies). All solvents used were HPLC grade (Chromasolv; Sigma-Aldrich). TFA was from Acros Organics (puriss., p.a.). Solvent A was 0.03% TFA in water; solvent B was 95% acetonitrile-5% water-0.03% TFA. Immediately before analysis, protein samples were diluted to a final concentration of 5 μM with solvent A and then desalted on a reverse-phase C8 cartridge (Zorbax 300SB-C8, 5 μm, 300 μm ID 5 mm; Agilent Technologies) at a flow rate of 50 μl/min for 3 min with 100% solvent A and subsequently eluted with 70% solvent B for MS detection. MS acquisition was carried out in the positive ion mode in the 300–3,200 m/z range. MS spectra were acquired and the data processed with MassHunter workstation software (v. B.07.00, Agilent Technologies) and with GPMAW software (v. 7.00b2, Lighthouse Data).

Spittler D., Indorato R.L., Boeri Erba E., Delaforge E., Signor L., Harris S.J., Garcia-Saez I., Palencia A., Gabel F., Blackledge M., Noirclerc-Savoye M, & Petosa C. (2022). Binding stoichiometry and structural model of the HIV-1 Rev/importin β complex. Life Science Alliance, 5(10), e202201431.

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Mass Spectrometry Protein Analysis

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Liquid Chromatography Electrospray Ionization Mass Spectrometry (LC/ESI-MS) was performed on a 6210 LC-TOF spectrometer coupled to a HPLC system (Agilent Technologies). All solvents used were HPLC grade (Chromasolv, Sigma-Aldrich), trifluoroacetic acid (TFA) was from Acros Organics (puriss., p.a.). Just before analysis protein samples were diluted in acidic denaturing conditions to a final concentration of 5 µM with solution A (0.03% TFA in water). Solvent B was 95% acetonitrile-5% water-0.03% TFA. Protein samples were firstly desalted on a reverse phase-C8 cartridge (Zorbax 300SB-C8, 5 μm, 300 µm ID´5 mm, Agilent Technologies) for 3 min at a flow rate of 50 μl/min with 100% solvent A and then eluted and separated onto a RP-C8 column (Jupiter, 5 μm, 300 Å, 1 mm ID × 50 mm, Phenomenex) at a flow rate of 50 μl/min using the following linear gradient: from 5 to 95% solvent B in 15 min, then remaining 2 min at 100% solvent B and finally re-equilibrating the column at 5% solvent B for 10 min. MS acquisition was carried out in the positive ion mode in the 300-3200 m/z range. MS spectra were acquired and the data processed with MassHunter workstation software (v. B.02.00, Agilent Technologies) and with GPMAW software (v. 7.00b2, Lighthouse Data, Denmark).

Lorvellec M., Chouquet A., Koch J., Bally I., Signor L., Vigne J., Dalonneau F., Thielens N.M., Rabilloud T., Dalzon B., Rossi V, & Gaboriaud C. (2023). HMGB1 cleavage by complement C1s and its potent anti-inflammatory product. Frontiers in Immunology, 14, 1151731.

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LC-ESI-MS Analysis of Protein Samples

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Liquid chromatography electrospray ionization mass spectrometry (LC/ESI-MS) was performed on a 6210 LC-TOF spectrometer coupled to a HPLC system (Agilent Technologies). All solvents used were HPLC grade (Chromasolv, Sigma-Aldrich), trifluoroacetic acid (TFA) was from Acros Organics (puriss., p.a.). Solvent A was 0.03% TFA in water; solvent B was 95% acetonitrile-5% water-0.03% TFA. Just before analysis, MBP-ZEBRA samples (10 μM in phosphate-buffered saline: 137 mM NaCl, 2.7 mM KCl, 10 mM Na₂HPO₄, 1.8 mM KH₂PO₄, pH 7.4) containing 0 or 20 mM DTT were diluted to a final concentration of 5 μM with water and 4 μl were injected for MS analysis. Protein samples were first desalted on a reverse phase-C8 cartridge (Zorbax 300SB-C8, 5 μm, 300 μm ID × 5 mm, Agilent Technologies) for 3 min at a flow rate of 50 μl/min with 100% solvent A and then eluted with 70% solvent B at flow rate of 50 μl/min for MS detection. MS acquisition was carried out in the positive ion mode in the 300–3200 m/z range. MS spectra were acquired and the data processed with MassHunter workstation software (v. B.02.00, Agilent Technologies) and GPMAW software (v. 7.00b2, Lighthouse Data, Denmark).

Bernaudat F., Gustems M., Günther J., Oliva M.F., Buschle A., Göbel C., Pagniez P., Lupo J., Signor L., Müller C.W., Morand P., Sattler M., Hammerschmidt W, & Petosa C. (2021). Structural basis of DNA methylation-dependent site selectivity of the Epstein–Barr virus lytic switch protein ZEBRA/Zta/BZLF1. Nucleic Acids Research, 50(1), 490-511.

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Protein Characterization by LC/ESI-MS

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Liquid Chromatography Electrospray Ionization Mass Spectrometry (LC/ESI-MS) analyses were performed on a 6210 LC-TOF spectrometer coupled to a HPLC system (Agilent Technologies).
All solvents used were HPLC grade (Chromasolv, Sigma-Aldrich), trifluoroacetic acid (TFA) was from Acros Organics. Solvent A was 0.03% TFA in water, solvent B was 95% acetonitrile, 5% water, 0.03% TFA. Before analysis, protein samples were diluted in acidic denaturing conditions to a final concentration of 10 µM with solvent A. Protein samples were firstly desalted on a reverse phase-C8 cartridge (Zorbax 300SB-C8, 5 mm, 300 Å 5*0.3 mm, Agilent Technologies) and then eluted with 95% solvent B.
MS spectra were recorded in the positive ion mode in the 300–3200 m/z range and the data processed with MassHunter workstation software (v. B.02.00, Agilent Technologies).

Fouët G., Bally I., Chouquet A., Reiser J.B., Thielens N.M., Gaboriaud C, & Rossi V. (2021). Molecular Basis of Complement C1q Collagen-Like Region Interaction with the Immunoglobulin-Like Receptor LAIR-1. International Journal of Molecular Sciences, 22(10), 5125.

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Synthesis and Characterization of Gd(III) Complexes

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Unless otherwise noted, materials
and solvents were obtained from commercial suppliers and used without
further purification. All reactions were performed under an inert
nitrogen atmosphere. EMD 60F 254 silica gel plates were used for thin
layer chromatography and visualized using UV light or ninhydrin stain.
Column chromatography was performed using standard grade 60 Å
230–400 mesh silica gel (Sorbent Technologies). ¹H NMR and ¹³C NMR spectra were obtained at room temperature
on a Bruker Avance III 500 MHz NMR spectrometer. An Agilent 6210 LC-TOF
spectrometer was used to acquire electrospray ionization mass spectra
(ESI–MS). Matrix-Assisted Laser Desorption Ionization Time-Of-Flight
(MALDI-TOF) mass spectrometry was carried out using a Bruker Autoflex
III MALDI. Semipreparative HPLC was performed on a Waters 19 ×
250 mm² Xbridge C18 Column. Analytical HPLC was performed
using a Waters 4.6 × 250 mm² 5 μM Xbridge C18
column using the Varian Prostar 500 system equipped with a Varian
363 fluorescence detector, and a Varian 335 UV–vis Detector.
The amine functionalized Gd(III) scaffold (4) was
synthesized according to a literature procedure.³⁰ For a detailed synthetic procedure of the PEG functionalized
scaffold (3) and the isothiocyanate functionalized dye
(5), see the SI.

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